ID   EDD1_RAT                Reviewed;         920 AA.
AC   Q62671;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   20-FEB-2007, entry version 45.
DE   Ubiquitin-protein ligase EDD1 (EC 6.3.2.-) (Hyperplastic discs protein
DE   homolog) (100 kDa protein) (Fragment).
GN   Name=Edd1; Synonyms=Dd5, Edd, Hyd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Testis;
RX   MEDLINE=92253337; PubMed=1533713; DOI=10.1093/nar/20.7.1471;
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RT   "Molecular characterization of a novel rat protein structurally
RT   related to poly(A) binding proteins and the 70K protein of the U1
RT   small nuclear ribonucleoprotein particle (snRNP).";
RL   Nucleic Acids Res. 20:1471-1475(1992).
RN   [2]
RP   ERRATUM.
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RL   Nucleic Acids Res. 20:2624-2624(1992).
RN   [3]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RX   MEDLINE=99153743; PubMed=10030672; DOI=10.1038/sj.onc.1202249;
RA   Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R.,
RA   Sutherland R.L., Watts C.K.W.;
RT   "Identification of a human HECT family protein with homology to the
RT   Drosophila tumor suppressor gene hyperplastic discs.";
RL   Oncogene 17:3479-3491(1998).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=12239083; DOI=10.1210/en.2002-220262;
RA   Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J.,
RA   Rajapurohitam V., Wing S.S.;
RT   "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase
RT   induced in germ cells of the rat testis and similar to the Drosophila
RT   hyperplastic discs gene.";
RL   Endocrinology 143:3740-3747(2002).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates (By
CC       similarity). May be involved in maturation and/or post-
CC       transcriptional regulation of mRNA. May play a role in control of
CC       cell cycle progression. May have tumor suppressor function.
CC       Regulates DNA topoisomerase II binding protein (TopBP1) for the
CC       DNA damage response. Plays an essential role in extraembryonic
CC       development (By similarity).
CC   -!- SUBUNIT: Binds TOPBP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present
CC       in liver, kidney, lung and brain.
CC   -!- DEVELOPMENTAL STAGE: In early post-natal life, expression in the
CC       testis increases to reach a maximum around day 28.
CC   -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
CC       thioester formation.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- CAUTION: Ref.1 (CAA45756) sequence differs from that shown due to
CC       a frameshift in position 30.
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DR   EMBL; X64411; CAA45756.1; ALT_FRAME; mRNA.
DR   UniGene; Rn.54812; -.
DR   HSSP; O95071; 1I2T.
DR   SMR; Q62671; 515-575.
DR   Ensembl; ENSRNOG00000006816; Rattus norvegicus.
DR   KEGG; rno:117060; -.
DR   RGD; 621236; Dd5.
DR   ArrayExpress; Q62671; -.
DR   GermOnline; ENSRNOG00000006816; Rattus norvegicus.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR002004; PABP_HYD.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00658; PABP; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00517; PolyA; 1.
DR   PROSITE; PS50237; HECT; 1.
KW   Ligase; Nuclear protein; Ubl conjugation pathway.
FT   CHAIN        <1    920       Ubiquitin-protein ligase EDD1.
FT                                /FTId=PRO_0000086933.
FT   DOMAIN      583    920       HECT.
FT   REGION      515    571       PABP-like.
FT   COMPBIAS    108    119       Asp/Glu-rich (acidic).
FT   COMPBIAS    158    181       Pro-rich.
FT   COMPBIAS    451    470       Arg/Glu-rich (mixed charge).
FT   COMPBIAS    479    488       Arg/Asp-rich (mixed charge).
FT   COMPBIAS    610    621       Asp/Glu-rich (acidic).
FT   COMPBIAS    858    878       Pro-rich.
FT   ACT_SITE    889    889       Glycyl thioester intermediate (By
FT                                similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   920 AA;  103950 MW;  465771084536C3AA CRC64;
     ARRERMTARE EASLRTLEGR RRATLLSARQ GMMSARGDFL NYALSLMRSH NDEHSDVLPV
     LDVCSLKHVA YVFQALIYWI KAMNQQTTLD TPQLERKRTR ELLELGIDNE DSEHENDDDT
     SQSATLNDKD DESLPAETGQ NHPFFRRSDS MTFLGCIPPN PFEVPLAEAI PLADQPHLLQ
     PNARKEDLFG RPSQGLYSSS AGSGKCLVEV TMDRNCLEVL PTKMSYAANL KNVMNMQNRQ
     KKAGEDQSML AEEADSSKPG PSAHDVAAQL KSSLLAEIGL TESEGPPLTS FRPQCSFMGM
     VISHDMLLGR WRLSLELFGR VFMEDVGAEP GSILTELGGF EVKESKFRRE MEKLRNQQSR
     DLSLEVDRDR DLLIQQTMRQ LNNHFGRRCA TTPMAVHRVK VTFKDEPGEG SGVARSFYTA
     IAQAFLSNEK LPNLDCIQNA NKGTHTSLMQ RLRNRGERDR EREREREMRR SSGLRAGSRR
     DRDRDFRRQL SIDTRPFRPA SEGNPSDDPD PLPAHRQALG ERLYPRVQAM QPAFASKITG
     MLLELSPAQL LLLLASEDSL RARVEEAMEL IVAHGRENGA DSILDLGLLD SSEKVQENRK
     RHGSSRSVVD MDLDDTDDGD DNAPLFYQPG KRGFYTPRPG KNTEARLNCF RNIGRILGLC
     LLQNELCPIT LNRHVIKVLL GRKVNWHDFA FFDPVMYESL RQLILASQSS DADAVFSAMD
     LAFAVDLCKE EGGGQVELIP NGVNIPVTPQ NVYEYVRKYA EHRMLVVAEQ PLHAMRKGLL
     DVLPKNSLED LTAEDFRLLV NGCGEVNVQM LISFTSFNDE SGENAEKLLQ FKRWFWSIVE
     RMSMTERQDL VYFWTSSPSL PASEEGFQPM PSITIRPPDD QHLPTANTCI SRLYVPLYSS
     KQILKQKLLL AIKTKNFGFV
//
ID   5HT1D_FUGRU             Reviewed;         379 AA.
AC   P79748;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   20-MAR-2007, entry version 40.
DE   5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D)
DE   (5HT1D) (F1D).
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4;
RA   Yamaguchi F., Brenner S.;
RT   "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes
RT   from the Japanese puffer fish, Fugu rubripes.";
RL   Gene 191:219-223(1997).
CC   -!- FUNCTION: This is one of the several different receptors for 5-
CC       hydroxytryptamine (serotonin), a biogenic hormone that functions
CC       as a neurotransmitter, a hormone, and a mitogen. The activity of
CC       this receptor is mediated by G proteins that inhibit adenylate
CC       cyclase activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; X83865; CAA58745.1; -; Genomic_DNA.
DR   HSSP; P08913; 1HLL.
DR   Ensembl; NEWSINFRUG00000120815; Fugu rubripes.
DR   InterPro; IPR000505; 5HT1D_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00514; 5HT1DRECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    379       5-hydroxytryptamine 1D receptor.
FT                                /FTId=PRO_0000068932.
FT   TOPO_DOM      1     36       Extracellular (Potential).
FT   TRANSMEM     37     60       1 (Potential).
FT   TOPO_DOM     61     73       Cytoplasmic (Potential).
FT   TRANSMEM     74     96       2 (Potential).
FT   TOPO_DOM     97    106       Extracellular (Potential).
FT   TRANSMEM    107    132       3 (Potential).
FT   TOPO_DOM    133    152       Cytoplasmic (Potential).
FT   TRANSMEM    153    174       4 (Potential).
FT   TOPO_DOM    175    192       Extracellular (Potential).
FT   TRANSMEM    193    216       5 (Potential).
FT   TOPO_DOM    217    307       Cytoplasmic (Potential).
FT   TRANSMEM    308    331       6 (Potential).
FT   TOPO_DOM    332    339       Extracellular (Potential).
FT   TRANSMEM    340    364       7 (Potential).
FT   TOPO_DOM    365    379       Cytoplasmic (Potential).
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     21     21       N-linked (GlcNAc...) (Potential).
FT   DISULFID    109    186       By similarity.
SQ   SEQUENCE   379 AA;  42302 MW;  99B6E2C0379EBC78 CRC64;
     MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT
     IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC
     TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH
     EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA
     QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR
     ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY
     TVFNDEFKQA FQKLIKFRR
//
ID   ACTB1_FUGRU             Reviewed;         375 AA.
AC   P68142; P53484;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   20-MAR-2007, entry version 16.
DE   Actin, cytoplasmic 1 (Beta-actin A).
GN   Name=ACTB-A;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Widely distributed. Not expressed in skeletal
CC       muscle.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
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DR   EMBL; U37499; AAC59889.1; -; Genomic_DNA.
DR   PIR; S71124; S71124.
DR   HSSP; P02570; 1HLU.
DR   SMR; P68142; 4-371.
DR   Ensembl; NEWSINFRUG00000152503; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      1       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000808.
FT   CHAIN         2    375       Actin, cytoplasmic 1.
FT                                /FTId=PRO_0000000809.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  9C505616D33E9495 CRC64;
     MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB_OREMO              Reviewed;         375 AA.
AC   P68143; P53484;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   20-MAR-2007, entry version 16.
DE   Actin, cytoplasmic 1 (Beta-actin).
GN   Name=ACTB;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei;
OC   Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini;
OC   Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RA   Takeuchi K.;
RT   "Cloning of Tilapia actin cDNAs.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
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DR   EMBL; AB037865; BAA90688.1; -; mRNA.
DR   HSSP; P02570; 1HLU.
DR   SMR; P68143; 4-371.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      1       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000802.
FT   CHAIN         2    375       Actin, cytoplasmic 1.
FT                                /FTId=PRO_0000000803.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  9C505616D33E9495 CRC64;
     MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB2_FUGRU             Reviewed;         375 AA.
AC   P53485;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Actin, cytoplasmic 2 (Beta-actin B).
GN   Name=ACTB-B;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
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DR   EMBL; U38848; AAC59890.1; -; Genomic_DNA.
DR   PIR; S71125; S71125.
DR   HSSP; P02570; 1HLU.
DR   SMR; P53485; 4-371.
DR   Ensembl; NEWSINFRUG00000152503; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      1       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000810.
FT   CHAIN         2    375       Actin, cytoplasmic 2.
FT                                /FTId=PRO_0000000811.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       2      2       N-acetylaspartate (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  1AE990BC0AED0D1C CRC64;
     MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB3_FUGRU             Reviewed;         375 AA.
AC   P53486;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Actin, cytoplasmic 3 (Beta-actin C).
GN   Name=ACTB-C;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in gills, kidney and
CC       skin.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U38849; AAC59891.1; -; Genomic_DNA.
DR   PIR; S71126; S71126.
DR   HSSP; P02570; 2BTF.
DR   SMR; P53486; 4-371.
DR   Ensembl; NEWSINFRUG00000152503; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      1       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000840.
FT   CHAIN         2    375       Actin, cytoplasmic 3.
FT                                /FTId=PRO_0000000841.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41783 MW;  8B451E0DB3399C0B CRC64;
     MEDEVASLVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA SSSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SSGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTC_FUGRU              Reviewed;         377 AA.
AC   P53480;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-APR-2007, entry version 42.
DE   Actin, alpha cardiac.
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in heart. Lower levels
CC       in skeletal muscle and skin.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three genes coding for cardiac actin in
CC       Fugu.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38959; AAC59894.1; -; Genomic_DNA.
DR   EMBL; U38960; AAC59895.1; -; Genomic_DNA.
DR   EMBL; U38961; AAC59896.1; -; Genomic_DNA.
DR   PIR; S71120; S71120.
DR   HSSP; P02568; 1MDU.
DR   SMR; P53480; 6-373.
DR   Ensembl; NEWSINFRUG00000137636; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000826.
FT   CHAIN         3    377       Actin, alpha cardiac.
FT                                /FTId=PRO_0000000827.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41975 MW;  0499A43921D9BBCF CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTSA_FUGRU             Reviewed;         377 AA.
AC   P68140; P53481;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   20-MAR-2007, entry version 16.
DE   Actin, alpha skeletal muscle A (Alpha-actin-1 A).
GN   Name=ACTA1-A;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC       Lower levels in heart.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are two different alpha-skeletal actins in
CC       Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; U38850; AAC59892.1; -; Genomic_DNA.
DR   PIR; S71118; S71118.
DR   HSSP; P02568; 1MDU.
DR   SMR; P68140; 6-373.
DR   Ensembl; NEWSINFRUG00000159793; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000862.
FT   CHAIN         3    377       Actin, alpha skeletal muscle A.
FT                                /FTId=PRO_0000000863.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41945 MW;  1C7185C0F7C19A26 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTS_OREMO              Reviewed;         377 AA.
AC   P68264; P53481;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   20-MAR-2007, entry version 16.
DE   Actin, alpha skeletal muscle (Alpha-actin-1).
GN   Name=ACTA1;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei;
OC   Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini;
OC   Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Takeuchi K.;
RT   "Cloning of Tilapia actin cDNAs.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB037866; BAA90689.1; -; mRNA.
DR   HSSP; P02568; 1MDU.
DR   SMR; P68264; 6-373.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000866.
FT   CHAIN         3    377       Actin, alpha skeletal muscle.
FT                                /FTId=PRO_0000000867.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41945 MW;  1C7185C0F7C19A26 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTSB_FUGRU             Reviewed;         377 AA.
AC   P53482;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Actin, alpha skeletal muscle B (Alpha-actin-1 B).
GN   Name=ACTA1-B;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC       Lower levels in heart, gills and skin.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are two different alpha-skeletal actins in
CC       Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38958; AAC59893.1; -; Genomic_DNA.
DR   PIR; S71119; S71119.
DR   HSSP; P02568; 1MDU.
DR   SMR; P53482; 6-373.
DR   Ensembl; NEWSINFRUG00000161349; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein;
KW   Nucleotide-binding; Structural protein.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000864.
FT   CHAIN         3    377       Actin, alpha skeletal muscle B.
FT                                /FTId=PRO_0000000865.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41977 MW;  A0973DD7B23B0C82 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMG TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTX_FUGRU              Reviewed;         376 AA.
AC   P53483;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 37.
DE   Actin, alpha anomalous.
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38962; AAC59897.1; -; Genomic_DNA.
DR   PIR; S71123; S71123.
DR   HSSP; P02568; 1KXP.
DR   SMR; P53483; 7-372.
DR   Ensembl; NEWSINFRUG00000163710; Fugu rubripes.
DR   InterPro; IPR004001; Actin.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
KW   ATP-binding; Cytoskeleton; Nucleotide-binding; Structural protein.
FT   CHAIN         1    376       Actin, alpha anomalous.
FT                                /FTId=PRO_0000089056.
SQ   SEQUENCE   376 AA;  41979 MW;  DB037F47BA1371D8 CRC64;
     MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ
     SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM
     TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN
     LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR
     YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL
     TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYEEIGPSI IHCKCF
//
ID   ARF3_FUGRU              Reviewed;         181 AA.
AC   P61207; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-APR-2007, entry version 22.
DE   ADP-ribosylation factor 3.
GN   Name=ARF3;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99177347; PubMed=10077531;
RA   Gellner K., Brenner S.;
RT   "Analysis of 148 kb of genomic DNA around the wnt1 locus of Fugu
RT   rubripes.";
RL   Genome Res. 9:251-258(1999).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; AF056116; AAC34390.1; -; Genomic_DNA.
DR   HSSP; P32889; 1RRF.
DR   SMR; P61207; 2-180.
DR   Ensembl; NEWSINFRUG00000161195; Fugu rubripes.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR001806; Ras_trnsfrmng.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS01019; ARF; 1.
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Myristate; Nucleotide-binding; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207390.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_HUMAN              Reviewed;         181 AA.
AC   P61204; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 29.
DE   ADP-ribosylation factor 3.
GN   Name=ARF3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=89345613; PubMed=2474826;
RA   Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J.,
RA   Vaughan M.;
RT   "Molecular cloning, characterization, and expression of human ADP-
RT   ribosylation factors: two guanine nucleotide-dependent activators of
RT   cholera toxin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92078170; PubMed=1744102;
RA   Tsai S.C., Haun R.S., Tsuchiya M., Moss J., Vaughan M.;
RT   "Isolation and characterization of the human gene for ADP-ribosylation
RT   factor 3, a 20-kDa guanine nucleotide-binding protein activator of
RT   cholera toxin.";
RL   J. Biol. Chem. 266:23053-23059(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction
RT   sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Lung, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH PRKCABP.
RX   MEDLINE=20090608; PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
RA   Takeya R., Takeshige K., Sumimoto H.;
RT   "Interaction of the PDZ domain of human PICK1 with class I ADP-
RT   ribosylation factors.";
RL   Biochem. Biophys. Res. Commun. 267:149-155(2000).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; M74493; AAA58359.1; -; Genomic_DNA.
DR   EMBL; M33384; AAA83931.1; -; mRNA.
DR   EMBL; M74491; AAB59425.1; -; mRNA.
DR   EMBL; AF493882; AAM12596.1; -; mRNA.
DR   EMBL; BT006670; AAP35316.1; -; mRNA.
DR   EMBL; BC007647; AAH07647.1; -; mRNA.
DR   EMBL; BC007762; AAH07762.1; -; mRNA.
DR   EMBL; BC017565; AAH17565.1; -; mRNA.
DR   EMBL; BC028402; AAH28402.1; -; mRNA.
DR   PIR; A41570; A41570.
DR   UniGene; Hs.119177; -.
DR   HSSP; P32889; 1RRF.
DR   SMR; P61204; 2-180.
DR   IntAct; P61204; -.
DR   OGP; P16587; -.
DR   Ensembl; ENSG00000134287; Homo sapiens.
DR   HGNC; HGNC:654; ARF3.
DR   MIM; 103190; gene.
DR   ArrayExpress; P61204; -.
DR   GermOnline; ENSG00000134287; Homo sapiens.
DR   RZPD-ProtExp; A0201; -.
DR   RZPD-ProtExp; IOH11881; -.
DR   RZPD-ProtExp; IOH26585; -.
DR   RZPD-ProtExp; IOH6999; -.
DR   RZPD-ProtExp; RZPDo839B12139; -.
DR   RZPD-ProtExp; RZPDo839B12140; -.
DR   RZPD-ProtExp; W0762; -.
DR   GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR   GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR001806; Ras_trnsfrmng.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS01019; ARF; 1.
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Myristate; Nucleotide-binding; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207386.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_MOUSE              Reviewed;         181 AA.
AC   P61205; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 33.
DE   ADP-ribosylation factor 3.
GN   Name=Arf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=97103475; PubMed=8947846;
RA   Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT   "Structure and intracellular localization of mouse ADP-ribosylation
RT   factors type 1 to type 6 (ARF1-ARF6).";
RL   J. Biochem. 120:813-819(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; D87900; BAA13492.1; -; mRNA.
DR   EMBL; BC014778; AAH14778.1; -; mRNA.
DR   EMBL; BC024935; AAH24935.1; -; mRNA.
DR   PIR; JC4947; JC4947.
DR   UniGene; Mm.221298; -.
DR   UniGene; Mm.393057; -.
DR   HSSP; P32889; 1RRF.
DR   SMR; P61205; 2-180.
DR   Ensembl; ENSMUSG00000051853; Mus musculus.
DR   KEGG; mmu:11842; -.
DR   MGI; MGI:99432; Arf3.
DR   ArrayExpress; P61205; -.
DR   GermOnline; ENSMUSG00000051853; Mus musculus.
DR   RZPD-ProtExp; IOM20659; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; TAS:MGI.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR001806; Ras_trnsfrmng.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS01019; ARF; 1.
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Myristate; Nucleotide-binding; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207387.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_RAT                Reviewed;         181 AA.
AC   P61206; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 32.
DE   ADP-ribosylation factor 3 (Liver regeneration-related protein
DE   LRRG202).
GN   Name=Arf3; ORFNames=Ac1-253;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96408698; PubMed=8813705;
RA   Price S.R., Nightingale M.S., Tsuchiya M., Moss J., Vaughan M.;
RT   "Interspecies relationships among ADP-ribosylation factors (ARFs):
RT   evidence of evolutionary pressure to maintain individual identities.";
RL   Mol. Cell. Biochem. 159:15-23(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; L12382; AAA40687.1; -; mRNA.
DR   EMBL; AY325223; AAP92624.1; -; mRNA.
DR   EMBL; BC088865; AAH88865.1; -; mRNA.
DR   UniGene; Rn.106440; -.
DR   HSSP; P32889; 1RRF.
DR   SMR; P61206; 2-180.
DR   IntAct; P61206; -.
DR   Ensembl; ENSRNOG00000033155; Rattus norvegicus.
DR   KEGG; hsa:377; -.
DR   KEGG; rno:140940; -.
DR   RGD; 621273; Arf3.
DR   ArrayExpress; P61206; -.
DR   GermOnline; ENSRNOG00000033155; Rattus norvegicus.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR001806; Ras_trnsfrmng.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS01019; ARF; 1.
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Myristate; Nucleotide-binding; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207389.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   CNR1A_FUGRU             Reviewed;         468 AA.
AC   Q98894;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Cannabinoid receptor type 1A.
GN   Name=CB1A;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406;
RA   Yamaguchi F., Macrae A., Brenner S.;
RT   "Molecular cloning of two cannabinoid type 1-like receptor genes from
RT   the puffer fish Fugu rubripes.";
RL   Genomics 35:603-605(1996).
CC   -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; X94401; CAA64174.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000135782; Fugu rubripes.
DR   InterPro; IPR002230; Cnbnoid_rcpt.
DR   InterPro; IPR000810; Cnoid_rcpt_1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00522; CANABINOID1R.
DR   PRINTS; PR00362; CANNABINOIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    468       Cannabinoid receptor type 1A.
FT                                /FTId=PRO_0000069320.
FT   TOPO_DOM      1    115       Extracellular (Potential).
FT   TRANSMEM    116    141       1 (Potential).
FT   TOPO_DOM    142    153       Cytoplasmic (Potential).
FT   TRANSMEM    154    174       2 (Potential).
FT   TOPO_DOM    175    186       Extracellular (Potential).
FT   TRANSMEM    187    211       3 (Potential).
FT   TOPO_DOM    212    231       Cytoplasmic (Potential).
FT   TRANSMEM    232    254       4 (Potential).
FT   TOPO_DOM    255    272       Extracellular (Potential).
FT   TRANSMEM    273    298       5 (Potential).
FT   TOPO_DOM    299    343       Cytoplasmic (Potential).
FT   TRANSMEM    344    364       6 (Potential).
FT   TOPO_DOM    365    376       Extracellular (Potential).
FT   TRANSMEM    377    398       7 (Potential).
FT   TOPO_DOM    399    468       Cytoplasmic (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   468 AA;  52391 MW;  B8628C1B043B42D7 CRC64;
     MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK
     VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV
     LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH
     KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW
     TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA
     HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA
     IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ
     LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV
//
ID   CNR1B_FUGRU             Reviewed;         470 AA.
AC   Q98895;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Cannabinoid receptor type 1B.
GN   Name=CB1B;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406;
RA   Yamaguchi F., Macrae A., Brenner S.;
RT   "Molecular cloning of two cannabinoid type 1-like receptor genes from
RT   the puffer fish Fugu rubripes.";
RL   Genomics 35:603-605(1996).
CC   -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X94402; CAA64175.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000147906; Fugu rubripes.
DR   InterPro; IPR002230; Cnbnoid_rcpt.
DR   InterPro; IPR000810; Cnoid_rcpt_1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00522; CANABINOID1R.
DR   PRINTS; PR00362; CANNABINOIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    470       Cannabinoid receptor type 1B.
FT                                /FTId=PRO_0000069321.
FT   TOPO_DOM      1    113       Extracellular (Potential).
FT   TRANSMEM    114    139       1 (Potential).
FT   TOPO_DOM    140    151       Cytoplasmic (Potential).
FT   TRANSMEM    152    172       2 (Potential).
FT   TOPO_DOM    173    184       Extracellular (Potential).
FT   TRANSMEM    185    209       3 (Potential).
FT   TOPO_DOM    210    229       Cytoplasmic (Potential).
FT   TRANSMEM    230    252       4 (Potential).
FT   TOPO_DOM    253    270       Extracellular (Potential).
FT   TRANSMEM    271    296       5 (Potential).
FT   TOPO_DOM    297    341       Cytoplasmic (Potential).
FT   TRANSMEM    342    362       6 (Potential).
FT   TOPO_DOM    363    374       Extracellular (Potential).
FT   TRANSMEM    375    396       7 (Potential).
FT   TOPO_DOM    397    470       Cytoplasmic (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   470 AA;  52081 MW;  CEE87CD37FDF9192 CRC64;
     MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI
     PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA
     ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK
     DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI
     SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH
     HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM
     VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD
     SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV
//
ID   CO9_FUGRU               Reviewed;         586 AA.
AC   P79755;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   20-MAR-2007, entry version 44.
DE   Complement component C9 precursor.
GN   Name=C9;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98038993; PubMed=9373156; DOI=10.1016/S0378-1119(97)00423-X;
RA   Yeo G.S.H., Elgar G., Sandford R., Brenner S.;
RT   "Cloning and sequencing of complement component C9 and its linkage to
RT   DOC-2 in the pufferfish Fugu rubripes.";
RL   Gene 200:203-211(1997).
CC   -!- FUNCTION: C9 is the final component of the complement system to be
CC       added in the assembly of the membrane attack complex. It is able
CC       to enter lipid bilayers, forming transmembrane channels (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted protein.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 LDL-receptor class A domain.
CC   -!- SIMILARITY: Contains 1 MACPF domain.
CC   -!- SIMILARITY: Contains 2 TSP type-1 domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U87241; AAC60288.1; -; Genomic_DNA.
DR   HSSP; Q07954; 1CR8.
DR   Ensembl; NEWSINFRUG00000146434; Fugu rubripes.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013032; EGF_like_reg.
DR   InterPro; IPR002172; LDL_rcpt_A.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR000884; TSP1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00209; TSP1; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MAC_PERFORIN; 1.
DR   PROSITE; PS50092; TSP1; 2.
KW   Complement alternate pathway; Complement pathway; Cytolysis;
KW   EGF-like domain; Glycoprotein; Immune response; Innate immunity;
KW   Membrane attack complex; Repeat; Signal.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    586       Complement component C9.
FT                                /FTId=PRO_0000023608.
FT   DOMAIN       36     89       TSP type-1 1.
FT   DOMAIN       94    131       LDL-receptor class A.
FT   DOMAIN      274    487       MACPF.
FT   DOMAIN      490    524       EGF-like.
FT   DOMAIN      543    585       TSP type-1 2.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    274    274       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    354    354       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   DISULFID     37     72       By similarity.
FT   DISULFID     48     51       By similarity.
FT   DISULFID     82     88       By similarity.
FT   DISULFID     96    108       By similarity.
FT   DISULFID    103    121       By similarity.
FT   DISULFID    115    129       By similarity.
FT   DISULFID    136    175       By similarity.
FT   DISULFID    363    389       By similarity.
FT   DISULFID    494    510       By similarity.
FT   DISULFID    497    512       By similarity.
FT   DISULFID    514    523       By similarity.
SQ   SEQUENCE   586 AA;  65198 MW;  8466EB7B8B8FDC18 CRC64;
     MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG
     VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD
     CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN
     PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST
     EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD
     EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI
     QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES
     AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ
     ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV
     TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC
//
ID   DRD1L_FUGRU             Reviewed;         459 AA.
AC   P53452;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 37.
DE   D(1)-like dopamine receptor.
GN   Name=D14;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80174; CAA56455.1; -; Genomic_DNA.
DR   PIR; A56849; A56849.
DR   HSSP; P08913; 1HLL.
DR   Ensembl; NEWSINFRUG00000145469; Fugu rubripes.
DR   InterPro; IPR001413; Dopa1A_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00565; DOPAMINED1AR.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    459       D(1)-like dopamine receptor.
FT                                /FTId=PRO_0000069382.
FT   TOPO_DOM      1     23       Extracellular (Potential).
FT   TRANSMEM     24     49       1 (Potential).
FT   TOPO_DOM     50     60       Cytoplasmic (Potential).
FT   TRANSMEM     61     87       2 (Potential).
FT   TOPO_DOM     88     96       Extracellular (Potential).
FT   TRANSMEM     97    119       3 (Potential).
FT   TOPO_DOM    120    138       Cytoplasmic (Potential).
FT   TRANSMEM    139    164       4 (Potential).
FT   TOPO_DOM    165    191       Extracellular (Potential).
FT   TRANSMEM    192    216       5 (Potential).
FT   TOPO_DOM    217    269       Cytoplasmic (Potential).
FT   TRANSMEM    270    297       6 (Potential).
FT   TOPO_DOM    298    311       Extracellular (Potential).
FT   TRANSMEM    312    333       7 (Potential).
FT   TOPO_DOM    334    459       Cytoplasmic (Potential).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   DISULFID     96    187       By similarity.
SQ   SEQUENCE   459 AA;  51080 MW;  B69857A3A4E4E10B CRC64;
     MAQNFSTVGD GKQMLLERDS SKRVLTGCFL SLLIFTTLLG NTLVCVAVTK FRHLRSKVTN
     FFVISLAISD LLVAILVMPW KAATEIMGFW PFGEFCNIWV AFDIMCSTAS ILNLCVISVD
     RYWAISSPFR YERKMTPKVA CLMISVAWTL SVLISFIPVQ LNWHKAQTAS YVELNGTYAG
     DLPPDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQKQIRRIS ALERAAESAQ
     NRHSSMGNSL SMESECSFKM SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCEADD
     TTDFPCISST TFDVFVWFGW ANSSLNPIIY AFNADFRKAF SILLGCHRLC PGNSAIEIVS
     INNTGAPLSN PSCQYQPKSH IPKEGNHSSS YVIPHSILCQ EEELQKKDGF GGEMEVGLVN
     NAMEKVSPAI SGNFDSDAAV TLETINPITQ NGQHKSMSC
//
ID   DRD2L_FUGRU             Reviewed;         463 AA.
AC   P53453;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 34.
DE   D(2)-like dopamine receptor.
GN   Name=D215;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80175; CAA56456.1; -; Genomic_DNA.
DR   HSSP; P08913; 1HLL.
DR   InterPro; IPR001922; Dopa_D2_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00567; DOPAMINED2R.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    463       D(2)-like dopamine receptor.
FT                                /FTId=PRO_0000069392.
FT   TOPO_DOM      1     35       Extracellular (Potential).
FT   TRANSMEM     36     58       1 (Potential).
FT   TOPO_DOM     59     69       Cytoplasmic (Potential).
FT   TRANSMEM     70     95       2 (Potential).
FT   TOPO_DOM     96    106       Extracellular (Potential).
FT   TRANSMEM    107    128       3 (Potential).
FT   TOPO_DOM    129    149       Cytoplasmic (Potential).
FT   TRANSMEM    150    172       4 (Potential).
FT   TOPO_DOM    173    187       Extracellular (Potential).
FT   TRANSMEM    188    211       5 (Potential).
FT   TOPO_DOM    212    392       Cytoplasmic (Potential).
FT   TRANSMEM    393    416       6 (Potential).
FT   TOPO_DOM    417    425       Extracellular (Potential).
FT   TRANSMEM    426    449       7 (Potential).
FT   TOPO_DOM    450    463       Cytoplasmic (Potential).
FT   CARBOHYD     10     10       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     16     16       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   DISULFID    105    183       By similarity.
SQ   SEQUENCE   463 AA;  52120 MW;  A54B178D7718AF6B CRC64;
     MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE
     KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI
     LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ
     SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI
     PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK
     QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA
     PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR
     CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC
//
ID   DRD5L_FUGRU             Reviewed;         463 AA.
AC   P53454;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 36.
DE   D(5)-like dopamine receptor.
GN   Name=DL;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80177; CAA56457.1; -; Genomic_DNA.
DR   PIR; B56849; B56849.
DR   HSSP; P08913; 1HLL.
DR   Ensembl; NEWSINFRUG00000140201; Fugu rubripes.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    463       D(5)-like dopamine receptor.
FT                                /FTId=PRO_0000069409.
FT   TOPO_DOM      1     39       Extracellular (Potential).
FT   TRANSMEM     40     65       1 (Potential).
FT   TOPO_DOM     66     76       Cytoplasmic (Potential).
FT   TRANSMEM     77    103       2 (Potential).
FT   TOPO_DOM    104    112       Extracellular (Potential).
FT   TRANSMEM    113    135       3 (Potential).
FT   TOPO_DOM    136    154       Cytoplasmic (Potential).
FT   TRANSMEM    155    180       4 (Potential).
FT   TOPO_DOM    181    198       Extracellular (Potential).
FT   TRANSMEM    199    223       5 (Potential).
FT   TOPO_DOM    224    273       Cytoplasmic (Potential).
FT   TRANSMEM    274    301       6 (Potential).
FT   TOPO_DOM    302    315       Extracellular (Potential).
FT   TRANSMEM    316    337       7 (Potential).
FT   TOPO_DOM    338    463       Cytoplasmic (Potential).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   DISULFID    112    194       By similarity.
SQ   SEQUENCE   463 AA;  51096 MW;  7FD627F69A699F6B CRC64;
     MENFYNETEP TEPRGGVDPL RVVTAAEDVP APVGGVSVRA LTGCVLCALI VSTLLGNTLV
     CAAVIKFRHL RSKVTNAFVV SLAVSDLFVA VLVMPWRAVS EVAGVWLFGR FCDTWVAFDI
     MCSTASILNL CVISMDRYWA ISNPFRYERR MTRRFAFLMI AVAWTLSVLI SFIPVQLNWH
     RADNNSSAHE QGDCNASLNR TYAISSSLIS FYIPVLIMVG TYTRIFRIAQ TQIRRISSLE
     RAAGQRAQNQ SHRASTHDES ALKTSFKRET KVLKTLSVIM GVFVFCWLPF FVLNCVVPFC
     DVDKVGEPPC VSDTTFNIFV WFGWANSSLN PVIYAFNADF RKAFTTILGC SKFCSSSAVQ
     AVDFSNELVS YHHDTTLQKE PVPGPGAHRL VAPLPQNRGD AGPNFDKVSV VSDDSRADRN
     LLLPAILQCD CEAEISLDMV PFGSSGPADS FLIPGQIQDL GDL
//
ID   EI2BB_FUGRU             Reviewed;         355 AA.
AC   Q90511;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   20-MAR-2007, entry version 27.
DE   Translation initiation factor eIF-2B subunit beta (eIF-2B GDP-GTP
DE   exchange factor subunit beta) (S20I15).
GN   Name=EIF2B2; Synonyms=EIF2BB;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R.,
RA   Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated
RT   with familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor
CC       2-bound GDP for GTP (By similarity).
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma,
CC       delta and epsilon (By similarity).
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U40756; AAC59777.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000126267; Fugu rubripes.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B...; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; ISS:UniProtKB.
DR   GO; GO:0051716; P:cellular response to stimulus; ISS:UniProtKB.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   InterPro; IPR000649; IF-2B_related.
DR   PANTHER; PTHR10233; IF-2B; 1.
DR   Pfam; PF01008; IF-2B; 1.
KW   Initiation factor; Protein biosynthesis.
FT   CHAIN         1    355       Translation initiation factor eIF-2B
FT                                subunit beta.
FT                                /FTId=PRO_0000156065.
SQ   SEQUENCE   355 AA;  39130 MW;  4375743877F6B132 CRC64;
     MPGADKEVDL TERIEAFLSD LKRGGSGTGP LRGSSETARE TTALLRRITA QARWSSAGDL
     MEIIRKEGRR LIAAQPSETT VGNMIRRVLK IIREEYARSR GSSEEADQQE SLHKLLTSGG
     LSEENFRQHF AALRANVIEA INELLTELEG TTDNIAMQAL EHIHSNEVIM TVGRSRTVEA
     FLKDAARKRK FHVIVAECAP FCQGHKMATS LSTAGIETTV IADAAIFAVM SRVNKVIIGT
     QTVLANGGLR AVNGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDTFH KFVSPHEVLP
     FTEGEILSKV NVHCPVFDYV PPELITLFIS NIGGHAPSYI YRLMSELYHP EDHEL
//
ID   EM55_FUGRU              Reviewed;         467 AA.
AC   P49697;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   20-MAR-2007, entry version 45.
DE   55 kDa erythrocyte membrane protein (p55) (Membrane protein,
DE   palmitoylated 1).
GN   Name=MPP1;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=96047329; PubMed=7558025; DOI=10.1006/geno.1995.1075;
RA   Elgar G.S., Rattray F.M., Greystrong J.S., Brenner S.;
RT   "Genomic structure and nucleotide sequence of the p55 gene of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 27:442-446(1995).
CC   -!- SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By
CC       similarity).
CC   -!- PTM: Extensively palmitoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X81359; CAA57127.1; -; Genomic_DNA.
DR   PIR; A57627; A57627.
DR   HSSP; O14936; 1KGD.
DR   Ensembl; NEWSINFRUG00000131184; Fugu rubripes.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylt/Ca.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR001452; SH3.
DR   InterPro; IPR011511; SH3_2.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   ProDom; PD000066; SH3; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
KW   Lipoprotein; Membrane; Palmitate; SH3 domain.
FT   CHAIN         1    467       55 kDa erythrocyte membrane protein.
FT                                /FTId=PRO_0000094567.
FT   DOMAIN       73    154       PDZ.
FT   DOMAIN      160    230       SH3.
FT   DOMAIN      283    452       Guanylate kinase-like.
SQ   SEQUENCE   467 AA;  52609 MW;  48BA1CE3ED524EDC CRC64;
     MTLKSNKNEP ALILDSVTSV RTALSDLYLE QLLQNKPTDK QAAMQTYENK GAEVFSNGSA
     GHINGAELSR MREVAFEKNQ SEPLGVTLKL NDKQRCSVAR ILHGGMIHRQ GSLHEGDEIA
     EINGKSVANQ TVDQLQKILK ETNGVVTMKI IPRPQSRSKP CEMYMRGQFD YDPAMDDLIP
     CKEAGLKFQT GDIIQIINKQ DPNWWQGRVE NNAANFAGLI PSPELQEWRA ASKSKAREGS
     QSCSPFGKKK KCKDKYLAKH SSIFDQLDVI SYEEVVRLPA FKRKTLVLIG APGVGRRHIK
     NVLLTKYPEK FSYPVPHTTR PQRKGDANGE EYFFISNEAM TKCISANELL EYGSFQGYMF
     GTITETIQKI HEQDKIALLD VEPQTMKVLR TADFGPLMVF IAPTDTAAQT ENLQMIQKES
     ETILNTYRQY FDVVLVNNDV NESVKIVEEA LEHATTTPQW VPVSWVY
//
ID   FOS_FUGRU               Reviewed;         376 AA.
AC   P53450;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 37.
DE   Proto-oncogene protein c-fos (Cellular oncogene fos).
GN   Name=FOS;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R.,
RA   Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated
RT   with familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
CC       covalently linked complex with the JUN/AP-1 transcription factor.
CC       C-fos has a critical function in regulating the development of
CC       cells destined to form and maintain the skeleton. It is thought to
CC       have an important role in signal transduction, cell proliferation
CC       and differentiation (By similarity).
CC   -!- SUBUNIT: Heterodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U40757; AAC59778.1; -; Genomic_DNA.
DR   HSSP; P01100; 1FOS.
DR   SMR; P53450; 123-182.
DR   TRANSFAC; T02205; -.
DR   Ensembl; NEWSINFRUG00000132419; Fugu rubripes.
DR   InterPro; IPR011700; bZIP_2.
DR   InterPro; IPR008917; Euk_TF_DNA_bd.
DR   InterPro; IPR000837; Leuzip_Fos.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF07716; bZIP_2; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
KW   DNA-binding; Nuclear protein; Phosphorylation; Proto-oncogene.
FT   CHAIN         1    376       Proto-oncogene protein c-fos.
FT                                /FTId=PRO_0000076473.
FT   DOMAIN      149    177       Leucine-zipper.
FT   DNA_BIND    123    144       Basic motif.
SQ   SEQUENCE   376 AA;  40826 MW;  BFC28534431DB491 CRC64;
     MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT
     AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE
     EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI
     LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN
     SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA
     AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS
     NDQSSDSLSS PTLLAL
//
ID   G6PD_FUGRU              Reviewed;         530 AA.
AC   P54996;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-APR-2007, entry version 44.
DE   Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (G6PD).
GN   Name=G6PD;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95331796; PubMed=7607684; DOI=10.1016/0888-7543(95)80179-P;
RA   Mason P.J., Stevens D.J., Luzzatto L., Brenner S., Aparicio S.;
RT   "Genomic structure and sequence of the Fugu rubripes glucose-6-
RT   phosphate dehydrogenase gene (G6PD).";
RL   Genomics 26:587-591(1995).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; X83611; CAA58590.2; -; Genomic_DNA.
DR   PIR; A56841; A56841.
DR   HSSP; P11413; 1QKI.
DR   SMR; P54996; 43-530.
DR   Ensembl; NEWSINFRUG00000135749; Fugu rubripes.
DR   InterPro; IPR001282; G6PDH.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   ProDom; PD001129; G6PD; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
KW   Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase.
FT   CHAIN         1    530       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068088.
FT   ACT_SITE    278    278       Proton acceptor (By similarity).
FT   BINDING      55     55       NADP (By similarity).
FT   BINDING      87     87       NADP (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   BINDING     220    220       Substrate (By similarity).
SQ   SEQUENCE   530 AA;  60469 MW;  FC73FB53D834EF29 CRC64;
     MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK
     KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN
     SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN
     RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW
     NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR
     DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH
     NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM
     SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF
     TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL
//
ID   HD_FUGRU                Reviewed;        3148 AA.
AC   P51112;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 34.
DE   Huntingtin (Huntington disease protein homolog) (HD protein).
GN   Name=HD;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95375788; PubMed=7647794; DOI=10.1038/ng0595-67;
RA   Baxendale S., Abdulla S., Elgar G., Buck D., Berks M., Micklem G.,
RA   Durbin R., Bates G., Brenner S., Beck S., Lehrach H.;
RT   "Comparative sequence analysis of the human and pufferfish
RT   Huntington's disease genes.";
RL   Nat. Genet. 10:67-76(1995).
CC   -!- FUNCTION: May play a role in microtubule-mediated transport or
CC       vesicle function.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- POLYMORPHISM: The poly-Gln region (four residues) does not appear
CC       to be polymorphic, explaining the absence of a HD-like disorder.
CC   -!- SIMILARITY: Belongs to the hungtintin family.
CC   -!- SIMILARITY: Contains 10 HEAT repeats.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X82939; CAA58112.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000144943; Fugu rubripes.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR000091; Huntingtin.
DR   InterPro; IPR002885; PPR.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF02985; HEAT; 4.
DR   PRINTS; PR00375; HUNTINGTIN.
DR   TIGRFAMs; TIGR00756; PPR; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
KW   Nuclear protein; Repeat.
FT   CHAIN         1   3148       Huntingtin.
FT                                /FTId=PRO_0000083941.
FT   REPEAT      149    186       HEAT 1.
FT   REPEAT      191    228       HEAT 2.
FT   REPEAT      760    797       HEAT 3.
FT   REPEAT      861    898       HEAT 4.
FT   REPEAT     1419   1456       HEAT 5.
FT   MOTIF      2398   2407       Nuclear export signal (By similarity).
FT   COMPBIAS     18     21       Poly-Gln.
FT   COMPBIAS    679    682       Poly-Ala.
FT   COMPBIAS   1104   1108       Poly-Ser.
SQ   SEQUENCE   3148 AA;  348937 MW;  D9358676B0345243 CRC64;
     MATMEKLMKA FESLKSFQQQ QGPPTAEEIV QRQKKEQATT KKDRVSHCLT ICENIVAQSL
     RTSPEFQKLL GIAMEMFLLC SDDSESDVRM VADECLNRII KALMDSNLPR LQLELYKEIK
     KNGASRSLRA ALWRFAELAH LIRPQKCRPY LVNLLPCLTR ITKRQEETIQ ETLAAAMPKI
     MAALGHFAND GEIKMLLKSF VANLKSSSPT IRRTAASSAV SVCQHSRRTS YFYTWLLNVL
     LGLLVPVDEE HHSHLILGVL LTLRYLMPLL QQQVNTISLK GSFGVMQKEA DVQPAPEQLL
     QVYELTLHYT QHWDHNVVTA ALELLQQTLR TPPPELLHVL ITAGSIQHAS VFRQDIESRA
     RSGSILELIA GGGSTCSPLL HRKHRGKMLS GEEDALEDDP EKTDVTTGYF TAVGADNSSA
     AQVDIITQQP RSSQHTIQPG DSVDLSASSE QGGRGGGASA SDTPESPNDE EDMLSRSSSC
     GANITPETVE DATPENPAQE GRPVGGSGAY DHSLPPSDSS QTTTEGPDSA VTPSDVAELV
     LDGSESQYSG MQIGTLQDEE DEGTATSSQE DPPDPFLRSA LALSKPHLFE SRGHNRQGSD
     SSVDRFIPKD EPPEPEPDNK MSRIKGAIGH YTDRGAEPVV HCVRLLSASF LLTGQKNGLT
     PDRDVRVSVK ALAVSCVGAA AALHPEAFFN SLYLEPLDGL RAEEQQYISD VLGFIDHGDP
     QIRGATAILC AAIIQAALSK MRYNIHSWLA SVQSKTGNPL SLVDLVPLLQ KALKDESSVT
     CKMACSAVRH CIMSLCGSTL SELGLRLVVD LFALKDSSYW LVRTELLETL AEMDFRLVNF
     LERKSEALHK GEHHYTGRLR LQERVLNDVV IQLLGDDDPR VRHVAASAVS RLVSRLFFDC
     DQGQADPVVA IARDQSSVYL QLLMHETQPP SQLTVSTITR TYRGFNLSNN VADVTVENNL
     SRVVTAVSHA FTSSTSRALT FGCCEALCLL AVHFPICTWT TGWHCGHISS QSSFSSRVGR
     SRGRTLSVSQ SGSTPASSTT SSAVDPERRT LTVGTANMVL SLLSSAWFPL DLSAHQDALL
     LCGNLLAAVA PKCLRNPWAG EDDSSSSSTN TSGGTHKMEE PWAALSDRAF VAMVEQLFSH
     LLKVLNICAH VLDDTPPGPP VKATLPSLTN TPSLSPIRRK GKDKDAVDSS SAPLSPKKGN
     EANTGRPTES TGSTAVHKST TLGSFYHLPP YLKLYDVLKA THANFKVMLD LHSNQEKFGS
     FLRAALDVLS QLLELATLND INKCVEEILG YLKSCFSREP TMATVCVQQL LKTLFGTNLA
     SQYEGFLSGP SRSQGKALRL GSSSLRPGLY HYCFMAPYTH FTQALADASL RNMVQAEHEQ
     DTSGWFDVMQ KTSNQLRSNI ANAARHRGDK NAIHNHIRLF EPLVIKALKQ YTTSTSVALQ
     RQVLDLLAQL VQLRVNYCLL DSDQVFIGFV LKQFEYIEVG QFRDSEAIIP NIFFFLVLLS
     YERYHSKQII SIPKIIQLCD GIMASGRKAV THAIPALQPI VHDLFVLRGS NKADAGKELE
     TQKEVVVSML LRLVQYHQVL EMFILVLQQC HKENEDKWKR LSRQIADVIL PMIAKQQMHL
     DSPEALGVLN TLFETVAPSS LRPVDMLLKS MFTTPVTMAS VATVQLWVSG ILAVLRVLVS
     QSTEDIVLSR IHELSLSPHL LSCHTIKRLQ QPNLSPSDQP AGDGQQNQEP NGEAQKSLPE
     ETFARFLIQL VGVLLDDISS RHVKVDITEQ QHTFYCQQLG TLLMCLIHVF KSGMFRRITV
     AASRLLKGES GSGHSGIEFY PLEGLNSMVH CLITTHPSLV LLWCQVLLII DYTNYSWWTE
     VHQTPKGHSL SCTKLLSPHS SGEGEEKPET RLAMINREIV RRGALILFCD YVCQNLHDSE
     HLTWLIVNHV RDLIDLSHEP PVQDFISAVH RNSAASGLFI QAIQSRCDNL NSPTMLKKTL
     QCLEGIHLSQ SGSLLMLYVD KLLSTPFRVL ARMVDTLACR RVEMLLAETL QNSVAQLPLE
     ELHRIQEYLQ TSGLAQRHQR FYSLLDRFRA TVSDTSSPST PVTSHPLDGD PPPAPELVIA
     DKEWYVALVK SQCCLHGDVS LLETTELLTK LPPADLLSVM SCKEFNLSLL CPCLSLGVQR
     LLRGQGSLLL ETALQVTLEQ LAGATGLLPV PHHSFIPTSH PQSHWKQLAE VYGDPGFYSR
     VLSLCRALSQ YLLTVKQLPS SLRIPSDKEH LITTFTCAAT EVVVWHLLQD QLPLSVDLQW
     ALSCLCLALQ QPCVWNKLST PEYNTHTCSL IYCLHHIILA VAVSPGDQLL HPERKKTKAL
     RHSDDEDQVD SVHDNHTLEW QACEIMAELV EGLQSVLSLG HHRNTAFPAF LTPTLRNIII
     SLSRLPLVNS HTRVPPLVWK LGWSPQPGGE FGTTLPEIPV DFLQEKDVFR EFLYRINTLG
     WSNRTQFEET WATLLGVLVT QPITMDQEEE TQQEEDLERT QLNVLAVQAI TSLVLSAMTL
     PTAGNPAVSC LEQQPRNKSL KALETRFGRK LAVIRGEVER EIQALVSKRD NVHTYHPYHA
     WDPVPSLSAA SPGTLISHEK LLLQINTERE LGNMDYKLGQ VSIHSVWLGN NITPLREEEW
     GEDEDDEADP PAPTSPPLSP INSRKHRAGV DIHSCSQFLL ELYSQWVIPG SPSNRKTPTI
     LISEVVRSLL AVSDLFTERN QFDMMFSTLM ELQKLHPPED EILNQYLVPA ICKAAAVLGM
     DKAIAEPVCR LLETTLRSTH LPSRMGALHG VLYVLECDLL DDTAKQLIPT VSEYLLSNLR
     AIAHCVNLHN QQHVLVMCAV AFYMMENYPL DVGTEFMAGI IQLCGVMVSA SEDSTPSIIY
     HCVLRGLERL LLSEQLSRVD GEALVKLSVD RVNMPSPHRA MAALGLMLTC MYTGKEKASP
     AARSAHSDPQ VPDSESIIVA MERVSVLFDR IRKGLPSEAR VVARILPQFL DDFFPPQDIM
     NKVIGEFLSN QQPYPQFMAT VVYKVFQTLH ATGQSSMVRD WVLLSLSNFT QRTPVAMAMW
     SLSCFFVSAS TSQWISALLP HVISRMGSSD VVDVNLFCLV AMDFYRHQID EELDRRAFQS
     VFETVASPGS PYFQLLACLQ SIHQDKSL
//
ID   HIRA_FUGRU              Reviewed;        1025 AA.
AC   O42611;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   20-MAR-2007, entry version 40.
DE   HIRA protein (TUP1-like enhancer of split protein 1).
GN   Name=HIRA; Synonyms=TUPLE1;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=98201624; PubMed=9524281; DOI=10.1016/S0378-1119(98)00010-9;
RA   Llevadot R., Estivill X., Scambler P., Pritchard M.;
RT   "Isolation and genomic characterization of the TUPLE1/HIRA gene of the
RT   pufferfish Fugu rubripes.";
RL   Gene 208:279-283(1998).
CC   -!- FUNCTION: Could have a part in mechanisms of transcriptional
CC       regulation similar to that played by yeast HIR1 and HIR2 together.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the WD repeat HIR1 family.
CC   -!- SIMILARITY: Contains 4 WD repeats.
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DR   EMBL; U94325; AAC60370.1; -; Genomic_DNA.
DR   EMBL; U94324; AAC60369.1; -; mRNA.
DR   UniGene; Tru.1844; -.
DR   HSSP; P16649; 1ERJ.
DR   Ensembl; NEWSINFRUG00000154061; Fugu rubripes.
DR   InterPro; IPR011494; Hira.
DR   InterPro; IPR001680; WD40.
DR   Pfam; PF07569; Hira; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   ProDom; PD000018; WD40; 3.
DR   SMART; SM00320; WD40; 8.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
KW   Nuclear protein; Repeat; Transcription; Transcription regulation;
KW   WD repeat.
FT   CHAIN         1   1025       HIRA protein.
FT                                /FTId=PRO_0000051021.
FT   REPEAT       68     98       WD 1.
FT   REPEAT      129    159       WD 2.
FT   REPEAT      172    202       WD 3.
FT   REPEAT      266    313       WD 4.
FT   COMPBIAS    673    682       Poly-Ala.
FT   COMPBIAS    685    688       Poly-Ala.
SQ   SEQUENCE   1025 AA;  111857 MW;  A4212152D75B6A37 CRC64;
     MKLLKPSWVS HNGKPIFSVD IHPDGTKFAT GGQGEDSGKV MIWNMAPVLK EEDEKNENVP
     KMLCQMDNHL ACVNCVRWSN NGLYLASGGD DKLVMVWKRA ALIGPSTVFG SSNKLANVEQ
     WRCVTILRNH TGDVMDVSWS PHDVWLASCS VDNTIVIWNA RKFPEMVTCL RGHTGLVKGL
     TWDPVGKYIA SQADDHSLRV WRTVDWQMEA NITKPFSECG GTTHVLRLSW SPDGQYLVSA
     HAMNNSGPTA QIVERDGWRT NMDFVGHRKA VTVVKFNPKI FKKKQKNGGS PKPSCPYCCC
     AVGSKDRSLS VWLTSLKRPL VVIHDLFDKS IMDISWTLTG LGMLVCSMDG TVAYLDFSLD
     ELGDPLSEEE KNSIHQNIYG KSLAITNTEP QLSTTIIENP EMLKYQQERR NSTQANSGPG
     ATGSESATPK LNSVMNGESL EDIRKNLLKK QVETRTPDGR RRITPLCIAQ LDTGDFSPAL
     FNSAPILPSG SSMSNQLTSQ LSSDSSPGQA PPLGLRPSQD PMLISPPPSS AAKVLEDNKD
     GVKSCLLLTS ASKIEPMKAL DSRFTERSKA TPGATAAIAS STGLTPSERP KESTPMQKDV
     KSKEDTSSDS EDKMATINKN LAFNKRKPEL LMDGAEVVEK RKKGRPRKDK MAASIAQPLT
     QTTSPAEREP SRAAAAGAGA AAPTAAAALK LPTPSIKKAF TLQVSMDPSV VLEVENEVSV
     VAGSRLSQLR CSRDGRDWNT LLPSSVLTAA GSSDVVAVAS QDRMLSVFSS CGRRLLPAIQ
     LATPASALHC SAHFVMVLTS GATLSVWDVH KQKALVKNES LLTILSGAAV TVSQSMLTQQ
     GVPVVGLSNG KSYCFSLSLE TWTLIADTAD SLVQCADFRN CLPNQDAPMS SGPLAAMQGR
     NFNAGRLASR LSSTPHHLQQ SMTLAFLENQ LASALTLQSA QEYRYWLLIY ARFLVNEGSE
     YRLRELCKEL LGPVHKSATT SWEPTTLGLR KRDLLREVLP VVGENLRFQR LFTEYQDQLE
     LLRNK
//
ID   RS24_FUGRU              Reviewed;         132 AA.
AC   O42387;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   20-MAR-2007, entry version 25.
DE   40S ribosomal protein S24.
GN   Name=RPS24;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Crosio C., Cecconi F., Giorgi M., Amaldi F., Mariottini P.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribosomal protein S24e family.
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DR   EMBL; AJ001398; CAA04728.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000143641; Fugu rubripes.
DR   LinkHub; O42387; -.
DR   InterPro; IPR001976; Ribosomal_S24E.
DR   PANTHER; PTHR10496; Ribosomal_S24E; 1.
DR   Pfam; PF01282; Ribosomal_S24e; 1.
DR   ProDom; PD006052; Ribosomal_S24E; 1.
DR   PROSITE; PS00529; RIBOSOMAL_S24E; 1.
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    132       40S ribosomal protein S24.
FT                                /FTId=PRO_0000137627.
SQ   SEQUENCE   132 AA;  15305 MW;  DC437F60F20C14F5 CRC64;
     MNDTVTVRTR KFMTNRLLQR KQMVVDVLHP GKATVPKTEI REKLAKMYKT TPDVVFVFGF
     RTQFGGGKTT GFAMVYDSLD YAKKNEPKHR LARHGLFEKK KTSRKQRKER KNRMKKVRGT
     KKASVGASKK KD
//
ID   RS7_FUGRU               Reviewed;         194 AA.
AC   P50894; P53548;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 27.
DE   40S ribosomal protein S7.
GN   Name=RPS7;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96371061; PubMed=8774896; DOI=10.1093/nar/24.16.3167;
RA   Cecconi F., Crosio C., Mariottini P., Cesareni G., Giorgi M.,
RA   Brenner S., Amaldi F.;
RT   "A functional role for some Fugu introns larger than the typical short
RT   ones: the example of the gene coding for ribosomal protein S7 and
RT   snoRNA U17.";
RL   Nucleic Acids Res. 24:3167-3172(1996).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S7e family.
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DR   EMBL; X94942; CAA64412.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000124260; Fugu rubripes.
DR   InterPro; IPR000554; Ribosomal_S7E.
DR   PANTHER; PTHR11278; Ribosomal_S7E; 1.
DR   Pfam; PF01251; Ribosomal_S7e; 1.
DR   ProDom; PD006276; Ribosomal_S7E; 2.
DR   PROSITE; PS00948; RIBOSOMAL_S7E; 1.
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    194       40S ribosomal protein S7.
FT                                /FTId=PRO_0000174194.
FT   COMPBIAS     98    120       Arg/Lys-rich (basic).
SQ   SEQUENCE   194 AA;  22206 MW;  D202501948D47E86 CRC64;
     MFSTSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGSRKAI
     IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRS KNKQKRPRSR
     TLTSVHDAIL EDLVFPSEIV GKRIRVKMDS SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL
     TGKDVVFEFP EFQL
//
ID   SSRL_FUGRU              Reviewed;         289 AA.
AC   O42179;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   20-MAR-2007, entry version 33.
DE   Somatostatin-like receptor F_48D10.1.
GN   Name=F_48D10.1;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hawkins J., Gillam B.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -!- CAUTION: Seems to lack the C-terminal part (TM6 and TM7).
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DR   EMBL; AF013613; AAB86684.1; -; Genomic_DNA.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00384; OPIOIDR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane.
FT   CHAIN         1    289       Somatostatin-like receptor F_48D10.1.
FT                                /FTId=PRO_0000070133.
FT   TOPO_DOM      1     57       Extracellular (Potential).
FT   TRANSMEM     58     79       1 (Potential).
FT   TOPO_DOM     80     89       Cytoplasmic (Potential).
FT   TRANSMEM     90    110       2 (Potential).
FT   TOPO_DOM    111    126       Extracellular (Potential).
FT   TRANSMEM    127    148       3 (Potential).
FT   TOPO_DOM    149    170       Cytoplasmic (Potential).
FT   TRANSMEM    171    191       4 (Potential).
FT   TOPO_DOM    192    240       Extracellular (Potential).
FT   TRANSMEM    241    261       5 (Potential).
FT   TOPO_DOM    262    289       Cytoplasmic (Potential).
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   DISULFID    125    221       By similarity.
SQ   SEQUENCE   289 AA;  32172 MW;  4F5A1776911D0ADA CRC64;
     MEPLDQTPGF PLSPEPNYWY ETTPSLLLVS YPHLLDISSN QSTQSVPFQG SSALLTAVIY
     ITVFVVGLTG NTLAIYVVLR YAGMKTVTNI YILNLAVADE LYIVGLPFLA TQNVLSYWPF
     GSFLCRVVMT ADSMNQFTSI FCLTVMSIDR YLAVVHPIRS TKWRHPRVAK VVSAAVWAVS
     FVVVLPVVIF SDVQVRPSRP LQVGTSSKCL VKRVQETFNS CNMIWPEPKN VWSTAFILYT
     AMVGFFGPLL IICLCYLLIV IKVRHRMSAA QVGAVVSTCP LNICCLSRR
//
ID   SYH_FUGRU               Reviewed;         519 AA.
AC   P70076;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   20-MAR-2007, entry version 41.
DE   Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase)
DE   (HisRS).
GN   Name=HARS; Synonyms=HISS;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=96323249; PubMed=8710896; DOI=10.1073/pnas.93.16.8485;
RA   Brenner S., Corrochano L.M.;
RT   "Translocation events in the evolution of aminoacyl-tRNA
RT   synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8485-8489(1996).
CC   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; Z54243; CAA91012.1; -; Genomic_DNA.
DR   Ensembl; NEWSINFRUG00000150159; Fugu rubripes.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR004516; HisS.
DR   InterPro; IPR009068; S15_NS1_RNA_bd.
DR   InterPro; IPR002314; tRNA-synt_2b.
DR   InterPro; IPR006195; tRNA_ligase_II.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    519       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_0000136337.
SQ   SEQUENCE   519 AA;  57913 MW;  A1CBF5752070759E CRC64;
     MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV
     LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY
     DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD
     FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC
     STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA
     CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE
     APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR
     TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI
     LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA
//
ID   SYV_FUGRU               Reviewed;        1217 AA.
AC   P49696;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   20-MAR-2007, entry version 40.
DE   Valyl-tRNA synthetase (EC 6.1.1.9) (Valine--tRNA ligase) (ValRS).
GN   Name=VARS; Synonyms=VARS1;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97396021; PubMed=9254008;
RA   Lim E.H., Corrochano L.M., Elgar G., Brenner S.;
RT   "Genomic structure and sequence analysis of the valyl-tRNA synthetase
RT   gene of the Japanese pufferfish, Fugu rubripes.";
RL   DNA Seq. 7:141-151(1997).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- SIMILARITY: Contains 1 GST-like domain.
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DR   EMBL; X91856; CAA62967.1; -; Genomic_DNA.
DR   HSSP; P96142; 1IVS.
DR   Ensembl; NEWSINFRUG00000142988; Fugu rubripes.
DR   InterPro; IPR013155; Anticodon_V_L_bd.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR010987; GST_C_like.
DR   InterPro; IPR002300; tRNA-synt_1a.
DR   InterPro; IPR001412; tRNA-synt_I.
DR   InterPro; IPR002303; tRNA-synt_val.
DR   InterPro; IPR010978; tRNA_bd_arm.
DR   InterPro; IPR009080; tRNAsyn_1a_bd.
DR   InterPro; IPR009008; ValRS_IleRS_edit.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1   1217       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000106256.
FT   DOMAIN        1      ?       GST-like.
FT   MOTIF       293    303       "HIGH" region.
FT   MOTIF       809    813       "KMSKS" region.
FT   BINDING     812    812       ATP (By similarity).
SQ   SEQUENCE   1217 AA;  138218 MW;  5E08AF24B5C8A7A1 CRC64;
     MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT
     GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR
     NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT
     EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD
     VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH
     LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK
     FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS
     KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV
     ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT
     PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI
     KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM
     DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV
     SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM
     VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN
     LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL
     WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA
     IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT
     EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL
     TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV
     NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ
     TELEKVKEAM DNFQKMM
//
ID   TCPD_FUGRU              Reviewed;         536 AA.
AC   P53451;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   T-complex protein 1 subunit delta (TCP-1-delta) (CCT-delta).
GN   Name=CCT4; Synonyms=CCTD;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=96125198; PubMed=8543170; DOI=10.1016/0378-1119(95)00604-4;
RA   Yoda T., Morita T., Kawatsu K., Sueki K., Shibata T., Hamano Y.;
RT   "Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu
RT   rubripes rubripes.";
RL   Gene 166:249-253(1995).
CC   -!- FUNCTION: Molecular chaperone; assist the folding of proteins upon
CC       ATP hydrolysis. Known to play a role, in vitro, in the folding of
CC       actin and tubulin.
CC   -!- SUBUNIT: Hetero-oligomeric complex of about 850 to 900 kDa that
CC       forms two stacked rings, 12 to 16 nm in diameter.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
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DR   EMBL; D49483; BAA08447.1; -; mRNA.
DR   EMBL; D49484; BAA18913.1; -; Genomic_DNA.
DR   UniGene; Tru.1843; -.
DR   HSSP; P48424; 1A6D.
DR   Ensembl; NEWSINFRUG00000131796; Fugu rubripes.
DR   InterPro; IPR012717; Chap_CCT_delta.
DR   InterPro; IPR002194; Chaperonin_TCP-1.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   InterPro; IPR008950; GroEL-ATPase.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   TIGRFAMs; TIGR02342; chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN         1    536       T-complex protein 1 subunit delta.
FT                                /FTId=PRO_0000128336.
SQ   SEQUENCE   536 AA;  57716 MW;  B3ED3285FAC18D07 CRC64;
     MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD
     EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL
     LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL
     APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK
     AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS
     ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE
     EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA
     GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR
     HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR
//
ID   ACH2_DROME              Reviewed;         576 AA.
AC   P17644; Q9VC73;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-APR-2007, entry version 78.
DE   Acetylcholine receptor subunit alpha-like 2 precursor.
GN   Name=nAcR-alpha-96Ab; Synonyms=Acr96Ab, AcrE, sad; ORFNames=CG6844;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Head;
RX   MEDLINE=90301489; PubMed=2114015; DOI=10.1093/nar/18.12.3640;
RA   Baumann A., Jonas P., Gundelfinger E.D.;
RT   "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila
RT   nicotinic acetylcholine receptors.";
RL   Nucleic Acids Res. 18:3640-3640(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Head;
RX   MEDLINE=90353591; PubMed=2117557; DOI=10.1016/0014-5793(90)81170-S;
RA   Jonas P., Baumann A., Merz B., Gundelfinger E.D.;
RT   "Structure and developmental expression of the D alpha 2 gene encoding
RT   a novel nicotinic acetylcholine receptor protein of Drosophila
RT   melanogaster.";
RL   FEBS Lett. 269:264-268(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90360975; PubMed=1697262;
RA   Sawruk E., Schloss P., Betz H., Schmitt B.;
RT   "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, a
RT   novel developmentally regulated alpha-subunit.";
RL   EMBO J. 9:2671-2677(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and
CC       leads to opening of an ion-conducting channel across the plasma
CC       membrane.
CC   -!- INTERACTION:
CC       Q9VHK6:CG9836; NbExp=1; IntAct=EBI-93751, EBI-141585;
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: CNS in embryos.
CC   -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages.
CC   -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9)
CC       family.
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DR   EMBL; X52274; CAA36517.1; -; mRNA.
DR   EMBL; X53583; CAA37652.1; -; mRNA.
DR   EMBL; AE003748; AAF56303.1; -; Genomic_DNA.
DR   EMBL; AY058446; AAL13675.1; -; mRNA.
DR   PIR; S11679; ACFFA2.
DR   UniGene; Dm.2363; -.
DR   DIP; DIP:22674N; -.
DR   IntAct; P17644; -.
DR   Ensembl; CG6844; Drosophila melanogaster.
DR   KEGG; dme:Dmel_CG6844; -.
DR   FlyBase; FBgn0000039; nAcR-alpha-96Ab.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-013190-MONOMER; -.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-013191-MONOMER; -.
DR   GermOnline; CG6844; Drosophila melanogaster.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR006029; Neu_channel_TM.
DR   InterPro; IPR006202; Neur_chan_lig_bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR002394; Nic_ach_rcpt.
DR   Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 2.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
KW   Complete proteome; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Postsynaptic membrane; Receptor; Signal; Transmembrane;
KW   Transport.
FT   SIGNAL        1     21       Probable.
FT   CHAIN        22    576       Acetylcholine receptor subunit alpha-like
FT                                2.
FT                                /FTId=PRO_0000000300.
FT   TOPO_DOM     22    261       Extracellular (Potential).
FT   TRANSMEM    262    285       Potential.
FT   TRANSMEM    293    311       Potential.
FT   TRANSMEM    327    346       Potential.
FT   TOPO_DOM    347    526       Cytoplasmic (Potential).
FT   TRANSMEM    527    545       Potential.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   DISULFID    169    183       By similarity.
FT   DISULFID    243    244       Associated with receptor activation (By
FT                                similarity).
SQ   SEQUENCE   576 AA;  65506 MW;  97D6A46CADC3F42F CRC64;
     MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI
     RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY
     VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ
     QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY
     YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL
     LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP
     WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD
     SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV
     AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT
     FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN
//
ID   HBA_HUMAN               Reviewed;         142 AA.
AC   P69905; P01922; Q96KF1; Q9NYR7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-APR-2007, entry version 41.
DE   Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin).
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX   MEDLINE=81088339; PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5;
RA   Michelson A.M., Orkin S.H.;
RT   "The 3' untranslated regions of the duplicated human alpha-globin
RT   genes are unexpectedly divergent.";
RL   Cell 22:371-377(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RX   MEDLINE=80137531; PubMed=6244294;
RA   Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K.,
RA   Deriel J.K., Forget B.G., Weissman S.M.;
RT   "Nucleotide sequence of the coding portion of human alpha globin
RT   messenger RNA.";
RL   J. Biol. Chem. 255:2807-2815(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
RX   MEDLINE=81175088; PubMed=6452630;
RA   Liebhaber S.A., Goossens M.J., Kan Y.W.;
RT   "Cloning and complete nucleotide sequence of human 5'-alpha-globin
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6946451;
RA   Orkin S.H., Goff S.C., Hechtman R.L.;
RT   "Mutation in an intervening sequence splice junction in man.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32.
RX   MEDLINE=21303311; PubMed=11410421;
RA   Zhao Y., Xu X.;
RT   "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-
RT   thalassemia in a Chinese family with HbH disease.";
RL   Haematologica 86:541-542(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX   MEDLINE=21295668; PubMed=11402454;
RA   Zhao Y., Zhong M., Liu Z., Xu X.;
RT   "Rapid detection of the common alpha-thalassemia-2 determinants by PCR
RT   assay.";
RL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RC   TISSUE=Blood;
RA   Kutlar F., Leithner C., Kutlar A.;
RT   "Rapid sequencing of mRNA of the human alpha two globin, directly
RT   isolated from reticulocytes in whole blood.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA1).
RC   TISSUE=Blood;
RA   Kutlar F., Leithner C., Kutlar A.;
RT   "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated
RT   region is different than alpha two globin.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RA   Kutlar F., Holley L., Leithner C., Kutlar A.;
RT   "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)'
RT   mutation was detected on the alpha-1 globin mRNA by sequencing of
RT   cDNA.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63.
RC   TISSUE=Blood;
RA   Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.;
RT   "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2
RT   globin gene of an Hispanic girl.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
RX   MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA   Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA   Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2
RT   Mb of the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALPHA-2).
RC   TISSUE=Bone marrow, Brain, Lung, and Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=13872627;
RA   Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
RA   Rudloff V., Wittmann-Liebold B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [15]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=13954546;
RA   Hill R.J., Konigsberg W.;
RT   "The structure of human hemoglobin: IV. The chymotryptic digestion of
RT   the alpha chain of human hemoglobin.";
RL   J. Biol. Chem. 237:3151-3156(1962).
RN   [16]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=14093912; DOI=10.1021/bi00906a030;
RA   Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.;
RT   "The amino acid sequence of the alpha chain of human fetal
RT   hemoglobin.";
RL   Biochemistry 2:1353-1357(1963).
RN   [17]
RP   PROTEIN SEQUENCE OF 2-32.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
RA   Fermi G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5-
RT   A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
RA   Baldwin J.M.;
RT   "The structure of human carbonmonoxy haemoglobin at 2.7-A
RT   resolution.";
RL   J. Mol. Biol. 136:103-128(1980).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
RX   MEDLINE=92381041; PubMed=1512262;
RA   Silva M.M., Rogers P.H., Arnone A.;
RT   "A third quaternary structure of human hemoglobin A at 1.7-A
RT   resolution.";
RL   J. Biol. Chem. 267:17248-17256(1992).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
RX   MEDLINE=98332748; PubMed=9665850; DOI=10.1006/jmbi.1998.1868;
RA   Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T.,
RA   Baker E.N.;
RT   "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy
RT   form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
RL   J. Mol. Biol. 280:475-484(1998).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38
RP   INS.
RX   MEDLINE=93192190; PubMed=8448109; DOI=10.1021/bi00061a007;
RA   Kavanaugh J.S., Moo-Penn W.F., Arnone A.;
RT   "Accommodation of insertions in helices: the mutation in hemoglobin
RT   Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha
RT   bulge.";
RL   Biochemistry 32:2509-2513(1993).
RN   [23]
RP   VARIANT AL-AIN ABU DHABI ASP-19.
RX   MEDLINE=93053723; PubMed=1428941;
RA   Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y.,
RA   Kister J., Galacteros F., Wajcman H.;
RT   "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin
RT   variant discovered in an Emiratee family.";
RL   Hemoglobin 16:355-362(1992).
RN   [24]
RP   VARIANT ATAGO TYR-86.
RX   MEDLINE=72030550; PubMed=5115619;
RA   Fujiwara N., Maekawa T., Matsuda G.;
RT   "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human
RT   hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and
RT   myoglobins. VI.";
RL   Int. J. Protein Res. 3:35-39(1971).
RN   [25]
RP   VARIANT AUCKLAND ASN-88.
RX   MEDLINE=97463291; PubMed=9322075;
RA   Brennan S.O., Matthews J.R.;
RT   "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal
RT   histidine identified by electrospray mass spectrometry.";
RL   Hemoglobin 21:393-403(1997).
RN   [26]
RP   VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
RA   Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J.,
RA   Jones R.T.;
RT   "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10)
RT   Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).";
RL   Biochim. Biophys. Acta 336:344-360(1974).
RN   [27]
RP   VARIANT CEMENELUM TRP-93.
RX   PubMed=8148419;
RA   Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.;
RT   "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the
RT   alpha 1/beta 2 interface that displays a moderate increase in oxygen
RT   affinity.";
RL   Ann. Hematol. 68:73-76(1994).
RN   [28]
RP   VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
RX   MEDLINE=85130255; PubMed=6526652;
RA   Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C.,
RA   Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z.,
RA   Duan Y.-Q., Zhang G.-Y.;
RT   "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin
RT   [alpha 16(A14)Lys-->Met] found in China.";
RL   Hemoglobin 8:569-581(1984).
RN   [29]
RP   VARIANT CLINIC LYS-61 DEL.
RX   PubMed=10206681;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:5<412::AID-HUMU14>3.3.CO;2-I;
RA   Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.;
RT   "Alpha-thalassaemia due to a single codon deletion in the alpha 1-
RT   globin gene. Computational structural analysis of the new alpha-chain
RT   variant.";
RL   Hum. Mutat. 11:412-412(1998).
RN   [30]
RP   VARIANT DAVENPORT HIS-79.
RX   MEDLINE=91331854; PubMed=2101836;
RA   Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K.,
RA   Huisman T.H.J.;
RT   "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2.";
RL   Hemoglobin 14:599-605(1990).
RN   [31]
RP   VARIANT EVANS MET-63.
RX   MEDLINE=90109650; PubMed=2606724;
RA   Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C.,
RA   Lutcher C.L., Felice A.E., Huisman T.H.J.;
RT   "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin
RT   causing a mild hemolytic anemia.";
RL   Hemoglobin 13:557-566(1989).
RN   [32]
RP   VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
RX   MEDLINE=89323437; PubMed=2752146;
RA   Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.;
RT   "Locus assignment of two alpha-globin structural mutants from the
RT   Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish
RT   Town (alpha 27 Val).";
RL   Blood 74:833-835(1989).
RN   [33]
RP   VARIANT GODAVARI THR-96.
RX   MEDLINE=98153063; PubMed=9494044;
RA   Wajcman H., Kister J., Riou J., Galacteros F., Girot R.,
RA   Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.;
RT   "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid
RT   substitution in the alpha 1 beta 2 interface that modifies the
RT   electrophoretic mobility of hemoglobin.";
RL   Hemoglobin 22:11-22(1998).
RN   [34]
RP   VARIANT GRADY GLU-PHE-THR-119 INS.
RX   MEDLINE=75010592; PubMed=4528583;
RA   Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.;
RT   "Hemoglobin Grady: the first example of a variant with elongated
RT   chains due to an insertion of residues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974).
RN   [35]
RP   VARIANT HANAMAKI GLU-140.
RX   MEDLINE=92340291; PubMed=1634363;
RA   Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.;
RT   "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu
RT   beta 2, found in a Japanese family.";
RL   Hemoglobin 16:67-71(1992).
RN   [36]
RP   VARIANT HANDA MET-91.
RX   MEDLINE=83056269; PubMed=6815131;
RA   Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
RT   "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and
RT   biosynthesis of a new slightly higher oxygen affinity variant.";
RL   Hemoglobin 6:379-389(1982).
RN   [37]
RP   VARIANT HASHARON HIS-48.
RX   MEDLINE=69165810; PubMed=5780195;
RA   Charache S., Mondzac A.M., Gessner U.;
RT   "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found
RT   in low concentration.";
RL   J. Clin. Invest. 48:834-847(1969).
RN   [38]
RP   VARIANT HOBART ARG-21.
RX   MEDLINE=88006902; PubMed=3654264;
RA   Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D.,
RA   Jupe D.M.D., Baikie M.J.;
RT   "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain
RT   hemoglobin variant.";
RL   Hemoglobin 11:211-220(1987).
RN   [39]
RP   VARIANT INKSTER VAL-86.
RX   MEDLINE=74302151; PubMed=4212045;
RA   Reed R.E., Winter W.P., Rucknagel D.L.;
RT   "Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2)
RT   coexisting with beta-thalassaemia in a Caucasian family.";
RL   Br. J. Haematol. 26:475-484(1974).
RN   [40]
RP   VARIANT KANAGAWA MET-41.
RX   MEDLINE=92340282; PubMed=1634355;
RA   Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T.,
RA   Harano K., Imai K.;
RT   "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with
RT   an increased oxygen affinity.";
RL   Hemoglobin 16:1-10(1992).
RN   [41]
RP   VARIANT KURDISTAN TYR-48.
RX   MEDLINE=94252883; PubMed=8195005;
RA   Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C.,
RA   Heister J.G.A.M., Amons R., Bernini L.F.;
RT   "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in
RT   combination with beta (0)-thalassemia.";
RL   Hemoglobin 18:11-18(1994).
RN   [42]
RP   VARIANT KUROSAKI GLU-8.
RX   MEDLINE=96031515; PubMed=7558876;
RA   Harano T., Harano K., Imai K., Murakami T., Matsubara H.;
RT   "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found
RT   in a Japanese woman.";
RL   Hemoglobin 19:197-201(1995).
RN   [43]
RP   VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
RX   MEDLINE=95229430; PubMed=7713747;
RA   Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.;
RT   "A case of HB J-Meerut (or Hb J-Birmingham) [alpha
RT   120(H3)Ala-->Glu].";
RL   Hemoglobin 18:433-435(1994).
RN   [44]
RP   VARIANT MELUSINE SER-115.
RX   MEDLINE=94124250; PubMed=8294199;
RA   Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.;
RT   "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin
RT   variant.";
RL   Hemoglobin 17:397-405(1993).
RN   [45]
RP   VARIANT MONTGOMERY ARG-49.
RX   MEDLINE=75109326; PubMed=1115799;
RA   Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
RA   Atkins R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [46]
RP   VARIANT PETAH TIKVA ASP-111.
RX   MEDLINE=81134478; PubMed=7470621;
RA   Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I.,
RA   Kirschman C.;
RT   "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new
RT   unstable variant with alpha-thalassemia-like expression.";
RL   Blood 57:705-711(1981).
RN   [47]
RP   VARIANT PHNOM PENH ILE-118 INS.
RX   MEDLINE=98112407; PubMed=9452028;
RA   Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D.,
RA   Galacteros F.;
RT   "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence
RT   for a hotspot for insertion of residues in the third exon of the
RT   alpha1-globin gene.";
RL   Hum. Mutat. Suppl. 1:S20-S22(1998).
RN   [48]
RP   VARIANT PORT HURON ARG-57.
RX   MEDLINE=92202056; PubMed=1802882;
RA   Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.;
RT   "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant.";
RL   Hemoglobin 15:381-391(1991).
RN   [49]
RP   VARIANT SAWARA ALA-7.
RX   MEDLINE=74008827; PubMed=4744335;
RA   Sumida I., Ohta Y., Imamura T., Yanase T.;
RT   "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine.";
RL   Biochim. Biophys. Acta 322:23-26(1973).
RN   [50]
RP   VARIANT SHENYANG GLU-27.
RX   MEDLINE=83135048; PubMed=7161109;
RA   Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.;
RT   "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable
RT   variant found in China.";
RL   Hemoglobin 6:625-628(1982).
RN   [51]
RP   VARIANT SUAN-DOK ARG-110.
RX   MEDLINE=80006169; PubMed=478977;
RA   Sanguansermsri T., Matragoon S., Changloah L., Flatz G.;
RT   "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2):
RT   an unstable variant associated with alpha-thalassemia.";
RL   Hemoglobin 3:161-174(1979).
RN   [52]
RP   VARIANT SUN PRAIRIE PRO-131.
RX   MEDLINE=91177710; PubMed=2079430;
RA   Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B.,
RA   Webber B.B., Codrington J.F., Huisman T.H.J.;
RT   "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable
RT   variant occurring in low quantities.";
RL   Hemoglobin 14:479-489(1990).
RN   [53]
RP   VARIANT SWAN RIVER GLY-7.
RX   MEDLINE=96351655; PubMed=8745434;
RA   Harano T., Harano K., Imai K., Terunuma S.;
RT   "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man.";
RL   Hemoglobin 20:75-78(1996).
RN   [54]
RP   VARIANT THIONVILLE GLU-2.
RX   MEDLINE=92316953; PubMed=1618774;
RA   Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S.,
RA   Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C.,
RA   Rosa J., Wajcman H.;
RT   "Hemoglobin Thionville. An alpha-chain variant with a substitution of
RT   a glutamate for valine at NA-1 and having an acetylated methionine NH2
RT   terminus.";
RL   J. Biol. Chem. 267:12682-12691(1992).
RN   [55]
RP   VARIANT TUNIS-BIZERTE PRO-130.
RX   MEDLINE=95306384; PubMed=7786798;
RA   Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.;
RT   "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro
RT   unstable variant with thalassaemic phenotype.";
RL   Br. J. Haematol. 90:71-76(1995).
RN   [56]
RP   VARIANT TURRIFF GLU-100.
RX   MEDLINE=92340284; PubMed=1634357;
RA   Langdown J.V., Davidson R.J., Williamson D.;
RT   "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the
RT   interference of abnormal hemoglobins in Hb A1c determination.";
RL   Hemoglobin 16:11-17(1992).
RN   [57]
RP   VARIANT VAL DE MARNE ARG-134.
RX   MEDLINE=94124251; PubMed=8294200;
RA   Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.;
RT   "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant
RT   with moderate increase in oxygen affinity.";
RL   Hemoglobin 17:407-417(1993).
RN   [58]
RP   VARIANT WESTMEAD GLN-123.
RX   MEDLINE=92155975; PubMed=1686260;
RA   Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.;
RT   "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase
RT   chain reaction and Stu I cleavage.";
RL   Hemoglobin 15:291-295(1991).
RN   [59]
RP   VARIANT WOODVILLE TYR-7.
RX   MEDLINE=86167529; PubMed=3754246;
RA   Como P.F., Barber S., Sage R.E., Kronenberg H.;
RT   "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine.";
RL   Hemoglobin 10:135-141(1986).
RN   [60]
RP   VARIANT YUDA ASP-131.
RX   MEDLINE=93053734; PubMed=1428950;
RA   Fujisawa K., Hattori Y., Ohba Y., Ando S.;
RT   "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with
RT   low oxygen affinity.";
RL   Hemoglobin 16:435-439(1992).
RN   [61]
RP   VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
RX   MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961;
RA   Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
RA   Melevendi C., Rasore A., Galacteros F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the alpha-
RT   chain and Hb Duino has two residues substituted in the beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
RN   [62]
RP   VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104.
RX   PubMed=10569723;
RA   Lacan P., Francina A., Souillet G., Aubry M., Couprie N.,
RA   Dementhon L., Becchi M.;
RT   "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln,
RT   alpha2], a variant on the distal histidine, and Hb CHarolles
RT   [alpha103(G10)His-Tyr, alpha1].";
RL   Hemoglobin 23:345-352(1999).
RN   [63]
RP   VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127.
RX   PubMed=14576901; DOI=10.1590/S0100-879X2003001100004;
RA   Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.;
RT   "Screening for mutations in human alpha-globin genes by nonradioactive
RT   single-strand conformation polymorphism.";
RL   Braz. J. Med. Biol. Res. 36:1471-1474(2003).
RN   [64]
RP   VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT
RP   ALA-95.
RX   PubMed=15495251; DOI=10.1002/ajh.20184;
RA   Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E.,
RA   Lakka V., Santacroce R., Abraham D.J., Asakura T.;
RT   "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant
RT   with very low oxygen affinity.";
RL   Am. J. Hematol. 77:268-276(2004).
RN   [65]
RP   VARIANT PLASENCIA ARG-126.
RX   PubMed=15921163;
RA   Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M.,
RA   Mateo M., Salvador M., Benavente C.;
RT   "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia:
RT   Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2).";
RL   Hemoglobin 29:113-117(2005).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- INTERACTION:
CC       Q9NZD4:AHSP; NbExp=1; IntAct=EBI-714680, EBI-720250;
CC       P68871:HBB; NbExp=1; IntAct=EBI-714680, EBI-715554;
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- PTM: The initiator Met is not cleaved in variant Thionville and is
CC       acetylated.
CC   -!- DISEASE: Defects in HBA1/HBA2 are the cause of alpha-thalassemia
CC       [MIM:141800]. The thalassemias are the most common monogenic
CC       diseases and occur mostly in Mediterranean and Southeast Asian
CC       populations. The hallmark of alpha-thalassemia is an imbalance in
CC       globin-chain production in the adult HbA molecule. The level of
CC       alpha chain production can range from none to very nearly normal
CC       levels. Deletion of both copies of each of the two alpha-globin
CC       genes causes alpha(0)-thalassemia, also known as homozygous alpha-
CC       thalassemia. Due to the complete absence of alpha chains, the
CC       predominant fetal hemoglobin is a tetramer of gamma-chains (Bart
CC       hemoglobin) that has essentially no oxygen carrying capacity. This
CC       causes oxygen starvation in the fetal tissues and leads to hydrops
CC       fetalis, prenatal lethality or early neonatal death. The loss of
CC       three alpha genes results in high levels of a tetramer of four
CC       beta chains (hemoglobin H), causing a severe and life-threatening
CC       anemia known as hemoglobin H disease. Untreated, most patients die
CC       in childhood or early adolescence. The loss of two alpha genes
CC       results in mild alpha-thalassemia, also known as heterozygous
CC       alpha-thalassemia. Affected individuals have small red cells and a
CC       mild anemia (microcytosis). If three of the four alpha-globin
CC       genes are functional, individuals are completely asymptomatic.
CC       Some rare forms of alpha-thalassemia are due to point mutations
CC       (non-deletional alpha-thalassemia). The thalassemic phenotype is
CC       due to unstable globin alpha chains that are rapidly catabolized
CC       prior to formation of the alpha-beta heterotetramers.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- WEB RESOURCE: NAME=HbVar;
CC       NOTE=Human hemoglobin variants and thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1".
CC   -!- WEB RESOURCE: NAME=HbVar;
CC       NOTE=Human hemoglobin variants and thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=HBA1".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=HBA2".
CC   -!- WEB RESOURCE: NAME=SHMPD;
CC       NOTE=The Singapore human mutation and polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBA1".
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DR   EMBL; J00153; AAB59407.1; -; Genomic_DNA.
DR   EMBL; J00153; AAB59408.1; -; Genomic_DNA.
DR   EMBL; V00491; CAA23750.1; -; Genomic_DNA.
DR   EMBL; V00493; CAA23752.1; -; mRNA.
DR   EMBL; V00488; CAA23748.1; -; Genomic_DNA.
DR   EMBL; V00516; CAA23774.1; -; Genomic_DNA.
DR   EMBL; AF230076; AAF72612.1; -; Genomic_DNA.
DR   EMBL; AF525460; AAM83102.1; -; Genomic_DNA.
DR   EMBL; AF097635; AAC72839.1; -; mRNA.
DR   EMBL; AF105974; AAC97373.1; -; mRNA.
DR   EMBL; AF349571; AAK37554.1; -; mRNA.
DR   EMBL; AF536204; AAN04486.1; -; Genomic_DNA.
DR   EMBL; AE006462; AAK61215.1; -; Genomic_DNA.
DR   EMBL; AE006462; AAK61216.1; -; Genomic_DNA.
DR   EMBL; Z84721; CAB06554.1; -; Genomic_DNA.
DR   EMBL; Z84721; CAB06555.1; -; Genomic_DNA.
DR   EMBL; BC005931; AAH05931.1; -; mRNA.
DR   EMBL; BC008572; AAH08572.1; -; mRNA.
DR   EMBL; BC032122; AAH32122.1; -; mRNA.
DR   EMBL; BC050661; AAH50661.1; -; mRNA.
DR   PIR; A90807; HAHU.
DR   PIR; C93303; HACZP.
DR   PIR; I58217; HACZ.
DR   UniGene; Hs.449630; -.
DR   PDB; 1A00; X-ray; A/C=1-142.
DR   PDB; 1A01; X-ray; A/C=1-142.
DR   PDB; 1A0U; X-ray; A/C=1-142.
DR   PDB; 1A0Z; X-ray; A/C=1-142.
DR   PDB; 1A3N; X-ray; A/C=1-142.
DR   PDB; 1A3O; X-ray; A/C=1-142.
DR   PDB; 1A9W; X-ray; A/C=1-142.
DR   PDB; 1ABW; X-ray; A=1-142.
DR   PDB; 1ABY; X-ray; A=1-142.
DR   PDB; 1AJ9; X-ray; A=1-142.
DR   PDB; 1B86; X-ray; A/C=1-142.
DR   PDB; 1BAB; X-ray; A/C=3-142.
DR   PDB; 1BBB; X-ray; A/C=1-142.
DR   PDB; 1BIJ; X-ray; A/C=1-142.
DR   PDB; 1BUW; X-ray; A=1-142, C=-.
DR   PDB; 1BZ0; X-ray; A/C=1-142.
DR   PDB; 1BZ1; X-ray; A/C=1-142.
DR   PDB; 1BZZ; X-ray; A/C=3-142.
DR   PDB; 1C7B; X-ray; A/C=3-142.
DR   PDB; 1C7C; X-ray; A=1-142.
DR   PDB; 1C7D; X-ray; A=1-142.
DR   PDB; 1CLS; X-ray; A/C=1-142.
DR   PDB; 1CMY; X-ray; A/C=1-142.
DR   PDB; 1COH; X-ray; A/C=1-142.
DR   PDB; 1DKE; X-ray; A/C=1-142.
DR   PDB; 1DXT; X-ray; A/C=1-142.
DR   PDB; 1DXU; X-ray; A/C=1-142.
DR   PDB; 1DXV; X-ray; A/C=1-142.
DR   PDB; 1FDH; X-ray; A=1-142.
DR   PDB; 1FN3; X-ray; A/C=1-142.
DR   PDB; 1G9V; X-ray; A/C=1-142.
DR   PDB; 1GBU; X-ray; A/C=1-142.
DR   PDB; 1GBV; X-ray; A/C=1-142.
DR   PDB; 1GLI; X-ray; A/C=3-142.
DR   PDB; 1GZX; X-ray; A/C=1-142.
DR   PDB; 1HAB; X-ray; A/C=1-142.
DR   PDB; 1HAC; X-ray; A/C=1-142.
DR   PDB; 1HBA; X-ray; A/C=1-142.
DR   PDB; 1HBB; X-ray; A/C=1-142.
DR   PDB; 1HBS; X-ray; A/C/E/G=1-142.
DR   PDB; 1HCO; X-ray; A=1-142.
DR   PDB; 1HDB; X-ray; A/C=1-142.
DR   PDB; 1HGA; X-ray; A/C=1-142.
DR   PDB; 1HGB; X-ray; A/C=1-142.
DR   PDB; 1HGC; X-ray; A/C=1-142.
DR   PDB; 1HHO; X-ray; A=1-142.
DR   PDB; 1IRD; X-ray; A=1-142.
DR   PDB; 1J3Y; X-ray; A/C/E/G=1-142.
DR   PDB; 1J3Z; X-ray; A/C/E/G=1-142.
DR   PDB; 1J40; X-ray; A/C/E/G=1-142.
DR   PDB; 1J41; X-ray; A/C/E/G=1-142.
DR   PDB; 1J7S; X-ray; A/C=3-142.
DR   PDB; 1J7W; X-ray; A/C=3-142.
DR   PDB; 1J7Y; X-ray; A/C=3-142.
DR   PDB; 1JY7; X-ray; A/C/P/R/U/W=1-142.
DR   PDB; 1K0Y; X-ray; A/C=1-142.
DR   PDB; 1K1K; X-ray; A=1-142.
DR   PDB; 1KD2; X-ray; A/C=1-142.
DR   PDB; 1LFL; X-ray; A/C/P/R=-.
DR   PDB; 1LFQ; X-ray; A=-.
DR   PDB; 1LFT; X-ray; A=-.
DR   PDB; 1LFV; X-ray; A=-.
DR   PDB; 1LFY; X-ray; A=-.
DR   PDB; 1LFZ; X-ray; A=-.
DR   PDB; 1LJW; X-ray; A=1-142.
DR   PDB; 1M9P; X-ray; A/C=1-142.
DR   PDB; 1MKO; X-ray; A/C=1-142.
DR   PDB; 1NEJ; X-ray; A/C=1-142.
DR   PDB; 1NIH; X-ray; A/C=1-142.
DR   PDB; 1NQP; X-ray; A/C=1-142.
DR   PDB; 1O1I; X-ray; A=1-142.
DR   PDB; 1O1J; X-ray; A=1-142.
DR   PDB; 1O1K; X-ray; A/C=3-142.
DR   PDB; 1O1L; X-ray; A=1-142.
DR   PDB; 1O1M; X-ray; A=1-142.
DR   PDB; 1O1N; X-ray; A=1-142.
DR   PDB; 1O1O; X-ray; A/C=1-142.
DR   PDB; 1O1P; X-ray; A=1-142.
DR   PDB; 1QI8; X-ray; A/C=3-142.
DR   PDB; 1QSH; X-ray; A/C=1-142.
DR   PDB; 1QSI; X-ray; A/C=1-142.
DR   PDB; 1QXD; X-ray; A/C=1-142.
DR   PDB; 1QXE; X-ray; A/C=1-142.
DR   PDB; 1R1X; X-ray; A=1-142.
DR   PDB; 1R1Y; X-ray; A/C=1-142.
DR   PDB; 1RPS; X-ray; A/C=1-142.
DR   PDB; 1RQ3; X-ray; A/C=1-142.
DR   PDB; 1RQ4; X-ray; A/C=1-142.
DR   PDB; 1RQA; X-ray; A/C=1-142.
DR   PDB; 1RVW; X-ray; A=1-142.
DR   PDB; 1SDK; X-ray; A/C=1-142.
DR   PDB; 1SDL; X-ray; A/C=1-142.
DR   PDB; 1SHR; X-ray; A/C=1-142.
DR   PDB; 1SI4; X-ray; A/C=1-142.
DR   PDB; 1THB; X-ray; A/C=1-142.
DR   PDB; 1UIW; X-ray; A/C/E/G=1-142.
DR   PDB; 1VWT; X-ray; A/C=1-142.
DR   PDB; 1XXT; X-ray; A/C=1-142.
DR   PDB; 1XY0; X-ray; A/C=3-142.
DR   PDB; 1XYE; X-ray; A/C=3-142.
DR   PDB; 1XZ2; X-ray; A/C=1-142.
DR   PDB; 1XZ4; X-ray; A/C=3-142.
DR   PDB; 1XZ5; X-ray; A/C=3-142.
DR   PDB; 1XZ7; X-ray; A/C=3-142.
DR   PDB; 1XZU; X-ray; A/C=3-142.
DR   PDB; 1XZV; X-ray; A/C=3-142.
DR   PDB; 1Y01; X-ray; B=1-142.
DR   PDB; 1Y09; X-ray; A/C=3-142.
DR   PDB; 1Y0A; X-ray; A/C=3-142.
DR   PDB; 1Y0C; X-ray; A/C=3-142.
DR   PDB; 1Y0D; X-ray; A/C=1-141.
DR   PDB; 1Y0T; X-ray; A/C=1-142.
DR   PDB; 1Y0W; X-ray; A/C=1-142.
DR   PDB; 1Y22; X-ray; A/C=1-142.
DR   PDB; 1Y2Z; X-ray; A/C=1-142.
DR   PDB; 1Y31; X-ray; A/C=1-142.
DR   PDB; 1Y35; X-ray; A/C=1-142.
DR   PDB; 1Y45; X-ray; A/C=1-142.
DR   PDB; 1Y46; X-ray; A/C=1-142.
DR   PDB; 1Y4B; X-ray; A/C=1-142.
DR   PDB; 1Y4F; X-ray; A/C=1-142.
DR   PDB; 1Y4G; X-ray; A/C=1-142.
DR   PDB; 1Y4P; X-ray; A/C=1-142.
DR   PDB; 1Y4Q; X-ray; A/C=1-142.
DR   PDB; 1Y4R; X-ray; A/C=1-142.
DR   PDB; 1Y4V; X-ray; A/C=1-142.
DR   PDB; 1Y5F; X-ray; A/C=1-142.
DR   PDB; 1Y5J; X-ray; A/C=1-142.
DR   PDB; 1Y5K; X-ray; A/C=1-142.
DR   PDB; 1Y7C; X-ray; A/C=1-142.
DR   PDB; 1Y7D; X-ray; A/C=1-142.
DR   PDB; 1Y7G; X-ray; A/C=1-142.
DR   PDB; 1Y7Z; X-ray; A/C=1-142.
DR   PDB; 1Y83; X-ray; A/C=1-142.
DR   PDB; 1Y85; X-ray; A/C=1-142.
DR   PDB; 1Y8W; X-ray; A/C=3-142.
DR   PDB; 1YDZ; X-ray; A/C=3-142.
DR   PDB; 1YE0; X-ray; A/C=1-142.
DR   PDB; 1YE1; X-ray; A/C=1-142.
DR   PDB; 1YE2; X-ray; A/C=1-142.
DR   PDB; 1YEN; X-ray; A/C=1-142.
DR   PDB; 1YEO; X-ray; A/C=1-142.
DR   PDB; 1YEQ; X-ray; A/C=1-142.
DR   PDB; 1YEU; X-ray; A/C=1-142.
DR   PDB; 1YEV; X-ray; A/C=1-142.
DR   PDB; 1YFF; X-ray; A/C/E/G=1-142.
DR   PDB; 1YG5; X-ray; A/C=1-142.
DR   PDB; 1YGD; X-ray; A/C=1-142.
DR   PDB; 1YGF; X-ray; A/C=1-142.
DR   PDB; 1YH9; X-ray; A/C=1-142.
DR   PDB; 1YHE; X-ray; A/C=1-142.
DR   PDB; 1YHR; X-ray; A/C=1-142.
DR   PDB; 1YIE; X-ray; A/C=1-142.
DR   PDB; 1YIH; X-ray; A/C=1-142.
DR   PDB; 1YVQ; X-ray; A/C=1-142.
DR   PDB; 1YVT; X-ray; A=1-142.
DR   PDB; 1YZI; X-ray; A=1-142.
DR   PDB; 1Z8U; X-ray; B/D=1-142.
DR   PDB; 2D5Z; X-ray; A/C=1-142.
DR   PDB; 2D60; X-ray; A/C=1-142.
DR   PDB; 2DN1; X-ray; A=1-142.
DR   PDB; 2DN2; X-ray; A/C=1-142.
DR   PDB; 2DN3; X-ray; A=1-142.
DR   PDB; 2H35; NMR; A=1-142, C=-.
DR   PDB; 2HBC; X-ray; A=1-142.
DR   PDB; 2HBD; X-ray; A=1-142.
DR   PDB; 2HBE; X-ray; A=1-142.
DR   PDB; 2HBF; X-ray; A=1-142.
DR   PDB; 2HBS; X-ray; A/C/E/G=1-142.
DR   PDB; 2HCO; X-ray; A=1-142.
DR   PDB; 2HHD; X-ray; A/C=1-142.
DR   PDB; 2HHE; X-ray; A/C=1-142.
DR   PDB; 4HHB; X-ray; A/C=1-142.
DR   PDB; 6HBW; X-ray; A/C=1-142.
DR   IntAct; P69905; -.
DR   SWISS-2DPAGE; P69905; HUMAN.
DR   DOSAC-COBS-2DPAGE; P01922; HUMAN.
DR   DOSAC-COBS-2DPAGE; P69905; HUMAN.
DR   REPRODUCTION-2DPAGE; P69905; HUMAN.
DR   Siena-2DPAGE; P69905; -.
DR   Ensembl; ENSG00000188536; Homo sapiens.
DR   H-InvDB; HIX0023258; -.
DR   HGNC; HGNC:4823; HBA1.
DR   HGNC; HGNC:4824; HBA2.
DR   MIM; 141800; gene+phenotype.
DR   MIM; 141850; gene.
DR   MIM; 141860; gene.
DR   DrugBank; APRD00796; Amodiaquine.
DR   DrugBank; APRD00468; Chloroquine.
DR   DrugBank; APRD01053; Iron Dextran.
DR   DrugBank; APRD00300; Mefloquine.
DR   DrugBank; APRD00604; Primaquine.
DR   DrugBank; APRD00563; Quinine.
DR   LinkHub; P69905; -.
DR   GermOnline; ENSG00000188536; Homo sapiens.
DR   GermOnline; ENSG00000206172; Homo sapiens.
DR   RZPD-ProtExp; IOH7452; -.
DR   RZPD-ProtExp; M0373; -.
DR   RZPD-ProtExp; RZPDo834G076; -.
DR   RZPD-ProtExp; S0333; -.
DR   GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; TAS:UniProtKB.
DR   GO; GO:0015671; P:oxygen transport; TAS:UniProtKB.
DR   InterPro; IPR002338; Alpha_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   InterPro; IPR002339; Pi_haem.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Disease mutation; Heme; Iron; Metal-binding; Oxygen transport;
KW   Polymorphism; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052653.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
FT   VARIANT       2      2       V -> E (in Thionville; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002719.
FT   VARIANT       3      3       L -> R (in ChongQing; O(2) affinity up).
FT                                /FTId=VAR_002720.
FT   VARIANT       6      6       A -> D (in J-Toronto).
FT                                /FTId=VAR_002721.
FT   VARIANT       6      6       A -> P (in Karachi).
FT                                /FTId=VAR_002722.
FT   VARIANT       7      7       D -> A (in Sawara; O(2) affinity up).
FT                                /FTId=VAR_002723.
FT   VARIANT       7      7       D -> G (in Swan River).
FT                                /FTId=VAR_002724.
FT   VARIANT       7      7       D -> N (in Dunn; O(2) affinity up).
FT                                /FTId=VAR_002725.
FT   VARIANT       7      7       D -> V (in Ferndown; O(2) affinity up).
FT                                /FTId=VAR_002726.
FT   VARIANT       7      7       D -> Y (in Woodville; O(2) affinity up).
FT                                /FTId=VAR_002727.
FT   VARIANT       8      8       K -> E (in Kurosaki).
FT                                /FTId=VAR_002728.
FT   VARIANT      11     11       V -> F (in dbSNP:rs1799896).
FT                                /FTId=VAR_014605.
FT   VARIANT      12     12       K -> E (in Anantharaj).
FT                                /FTId=VAR_002729.
FT   VARIANT      13     13       A -> D (in J-Paris 1/J-Aljezur).
FT                                /FTId=VAR_002730.
FT   VARIANT      15     15       W -> R (in Evanston; O(2) affinity up).
FT                                /FTId=VAR_002731.
FT   VARIANT      16     16       G -> R (in Ottawa/Siam).
FT                                /FTId=VAR_002732.
FT   VARIANT      17     17       K -> M (in Harbin; slightly unstable).
FT                                /FTId=VAR_002733.
FT   VARIANT      17     17       K -> N (in Beijing).
FT                                /FTId=VAR_002734.
FT   VARIANT      19     19       G -> D (in Al-Ain Abu Dhabi).
FT                                /FTId=VAR_002735.
FT   VARIANT      19     19       G -> R (in Handsworth).
FT                                /FTId=VAR_002736.
FT   VARIANT      20     20       A -> D (in J-Kurosh).
FT                                /FTId=VAR_002737.
FT   VARIANT      20     20       A -> E (in J-Tashikuergan).
FT                                /FTId=VAR_002738.
FT   VARIANT      21     21       H -> Q (in Le Lamentin).
FT                                /FTId=VAR_002739.
FT   VARIANT      21     21       H -> R (in Hobart).
FT                                /FTId=VAR_002740.
FT   VARIANT      22     22       A -> D (in J-Nyanza).
FT                                /FTId=VAR_002741.
FT   VARIANT      22     22       A -> P (in Fontainebleau).
FT                                /FTId=VAR_002742.
FT   VARIANT      23     23       G -> D (in J-Medellin).
FT                                /FTId=VAR_002743.
FT   VARIANT      24     24       E -> G (in Reims; slightly unstable).
FT                                /FTId=VAR_002744.
FT   VARIANT      24     24       E -> K (in Chad).
FT                                /FTId=VAR_002745.
FT   VARIANT      25     25       Y -> H (in Luxembourg; unstable).
FT                                /FTId=VAR_002746.
FT   VARIANT      27     27       A -> E (in Shenyang; unstable).
FT                                /FTId=VAR_002747.
FT   VARIANT      27     27       A -> V (in Campinas).
FT                                /FTId=VAR_025387.
FT   VARIANT      28     28       E -> D (in Hekinan).
FT                                /FTId=VAR_002748.
FT   VARIANT      28     28       E -> G (in Fort Worth).
FT                                /FTId=VAR_002749.
FT   VARIANT      28     28       E -> V (in Spanish town).
FT                                /FTId=VAR_002750.
FT   VARIANT      31     31       E -> K (in O-Padova).
FT                                /FTId=VAR_002751.
FT   VARIANT      32     32       R -> K (causes alpha-thalassemia).
FT                                /FTId=VAR_025002.
FT   VARIANT      32     32       R -> S (in Prato; unstable).
FT                                /FTId=VAR_002752.
FT   VARIANT      35     35       L -> R (in Queens/Ogi).
FT                                /FTId=VAR_002753.
FT   VARIANT      38     38       P -> PE (in Catonsville).
FT                                /FTId=VAR_002755.
FT   VARIANT      38     38       P -> R (in Bourmedes).
FT                                /FTId=VAR_002754.
FT   VARIANT      41     41       K -> M (in Kanagawa; O(2) affinity up).
FT                                /FTId=VAR_002756.
FT   VARIANT      42     42       T -> S (in Miyano; O(2) affinity up).
FT                                /FTId=VAR_002757.
FT   VARIANT      44     44       F -> L (in Hirosaki; unstable).
FT                                /FTId=VAR_002758.
FT   VARIANT      45     45       P -> L (in Milledgeville; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002759.
FT   VARIANT      45     45       P -> R (in Kawachi; O(2) affinity up).
FT                                /FTId=VAR_002760.
FT   VARIANT      46     46       H -> Q (in Bari).
FT                                /FTId=VAR_002761.
FT   VARIANT      46     46       H -> R (in Fort de France; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002762.
FT   VARIANT      48     48       D -> A (in Cordele; unstable).
FT                                /FTId=VAR_002763.
FT   VARIANT      48     48       D -> G (in Umi/Michigan; unstable).
FT                                /FTId=VAR_002764.
FT   VARIANT      48     48       D -> H (in Hasharon/Sinai; unstable).
FT                                /FTId=VAR_002765.
FT   VARIANT      48     48       D -> Y (in Kurdistan).
FT                                /FTId=VAR_002766.
FT   VARIANT      49     49       L -> R (in Montgomery).
FT                                /FTId=VAR_002767.
FT   VARIANT      50     50       S -> R (in Savaria).
FT                                /FTId=VAR_002768.
FT   VARIANT      51     51       H -> R (in Aichi; slightly unstable).
FT                                /FTId=VAR_002769.
FT   VARIANT      52     52       G -> D (in J-Abidjan).
FT                                /FTId=VAR_002770.
FT   VARIANT      52     52       G -> R (in Russ).
FT                                /FTId=VAR_002771.
FT   VARIANT      54     54       A -> D (in J-Rovigo; unstable).
FT                                /FTId=VAR_002772.
FT   VARIANT      55     55       Q -> R (in Hikoshima/Shimonoseki).
FT                                /FTId=VAR_002773.
FT   VARIANT      57     57       K -> R (in Port Huron).
FT                                /FTId=VAR_002774.
FT   VARIANT      57     57       K -> T (in Thailand).
FT                                /FTId=VAR_002775.
FT   VARIANT      58     58       G -> R (in L-Persian Gulf).
FT                                /FTId=VAR_002776.
FT   VARIANT      59     59       H -> Q (in Boghe).
FT                                /FTId=VAR_025388.
FT   VARIANT      59     59       H -> Y (in M-Boston/M-Osaka; O(2)
FT                                affinity down).
FT                                /FTId=VAR_002777.
FT   VARIANT      60     60       G -> D (in Adana; unstable; causes alpha-
FT                                thalassemia; dbSNP:rs28928878).
FT                                /FTId=VAR_002778.
FT   VARIANT      60     60       G -> V (in Tottori; unstable).
FT                                /FTId=VAR_002779.
FT   VARIANT      61     61       K -> N (in Zambia; dbSNP:rs28928887).
FT                                /FTId=VAR_002780.
FT   VARIANT      61     61       Missing (in Clinic; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002781.
FT   VARIANT      62     62       K -> N (in J-Buda).
FT                                /FTId=VAR_002782.
FT   VARIANT      62     62       K -> T (in J-Anatolia).
FT                                /FTId=VAR_002783.
FT   VARIANT      63     63       V -> M (in Evans; unstable).
FT                                /FTId=VAR_002784.
FT   VARIANT      64     64       A -> D (in Pontoise; unstable).
FT                                /FTId=VAR_002785.
FT   VARIANT      65     65       D -> Y (in Persepolis).
FT                                /FTId=VAR_002786.
FT   VARIANT      69     69       N -> K (in G-Philadelphia;
FT                                dbSNP:rs1060339).
FT                                /FTId=VAR_002787.
FT   VARIANT      72     72       A -> E (in J-Habana).
FT                                /FTId=VAR_002788.
FT   VARIANT      72     72       A -> V (in Ozieri).
FT                                /FTId=VAR_002789.
FT   VARIANT      73     73       H -> R (in Daneskgah-Teheran).
FT                                /FTId=VAR_002790.
FT   VARIANT      75     75       D -> A (in Lille).
FT                                /FTId=VAR_002791.
FT   VARIANT      75     75       D -> G (in Chapel Hill).
FT                                /FTId=VAR_002792.
FT   VARIANT      75     75       D -> N (in G-Pest).
FT                                /FTId=VAR_002793.
FT   VARIANT      76     76       D -> A (in Duan).
FT                                /FTId=VAR_002794.
FT   VARIANT      76     76       D -> H (in Q-Iran).
FT                                /FTId=VAR_002795.
FT   VARIANT      77     77       M -> K (in Noko).
FT                                /FTId=VAR_002796.
FT   VARIANT      77     77       M -> T (in Aztec).
FT                                /FTId=VAR_002797.
FT   VARIANT      78     78       P -> R (in Guizhou).
FT                                /FTId=VAR_002798.
FT   VARIANT      79     79       N -> H (in Davenport).
FT                                /FTId=VAR_002799.
FT   VARIANT      79     79       N -> K (in Stanleyville-2).
FT                                /FTId=VAR_002800.
FT   VARIANT      80     80       A -> G (in Singapore).
FT                                /FTId=VAR_012662.
FT   VARIANT      81     81       L -> R (in Ann Arbor; unstable).
FT                                /FTId=VAR_002801.
FT   VARIANT      82     82       S -> C (in Nigeria).
FT                                /FTId=VAR_002802.
FT   VARIANT      83     83       A -> D (in Garden State).
FT                                /FTId=VAR_002803.
FT   VARIANT      85     85       S -> R (in Etobicoke; O(2) affinity up).
FT                                /FTId=VAR_002804.
FT   VARIANT      86     86       D -> V (in Inkster; O(2) affinity up).
FT                                /FTId=VAR_002805.
FT   VARIANT      86     86       D -> Y (in Atago; O(2) affinity up).
FT                                /FTId=VAR_002806.
FT   VARIANT      87     87       L -> R (in Moabit; unstable).
FT                                /FTId=VAR_002807.
FT   VARIANT      88     88       H -> N (in Auckland; unstable).
FT                                /FTId=VAR_002808.
FT   VARIANT      88     88       H -> R (in Iwata; unstable).
FT                                /FTId=VAR_002809.
FT   VARIANT      89     89       A -> S (in Loire; O(2) affinity up).
FT                                /FTId=VAR_002810.
FT   VARIANT      91     91       K -> M (in Handa; O(2) affinity up).
FT                                /FTId=VAR_002811.
FT   VARIANT      92     92       L -> P (in Port Phillip; unstable;
FT                                dbSNP:rs17407508).
FT                                /FTId=VAR_002812.
FT   VARIANT      93     93       R -> Q (in J-Cape Town; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002813.
FT   VARIANT      93     93       R -> W (in Cemenelum; O(2) affinity up).
FT                                /FTId=VAR_020775.
FT   VARIANT      95     95       D -> A (in Bassett; markedly reduced
FT                                oxygen affinity).
FT                                /FTId=VAR_025389.
FT   VARIANT      95     95       D -> Y (in Setif; unstable).
FT                                /FTId=VAR_002814.
FT   VARIANT      96     96       P -> A (in Denmark Hill; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002815.
FT   VARIANT      96     96       P -> T (in Godavari; O(2) affinity up).
FT                                /FTId=VAR_002816.
FT   VARIANT      98     98       N -> K (in Dallas; O(2) affinity up).
FT                                /FTId=VAR_002817.
FT   VARIANT     100    100       K -> E (in Turriff).
FT                                /FTId=VAR_002818.
FT   VARIANT     103    103       S -> R (in Manitoba; slightly unstable).
FT                                /FTId=VAR_002819.
FT   VARIANT     104    104       H -> R (in Contaldo; unstable).
FT                                /FTId=VAR_002820.
FT   VARIANT     104    104       H -> Y (in Charolles).
FT                                /FTId=VAR_025390.
FT   VARIANT     110    110       L -> R (in Suan-Dok; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002821.
FT   VARIANT     111    111       A -> D (in Petah Tikva; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002822.
FT   VARIANT     113    113       H -> D (in Hopkins-II; unstable).
FT                                /FTId=VAR_002823.
FT   VARIANT     114    114       L -> H (in Twin Peaks).
FT                                /FTId=VAR_002824.
FT   VARIANT     115    115       P -> L (in Nouakchott).
FT                                /FTId=VAR_002825.
FT   VARIANT     115    115       P -> R (in Chiapas).
FT                                /FTId=VAR_002826.
FT   VARIANT     115    115       P -> S (in Melusine).
FT                                /FTId=VAR_002827.
FT   VARIANT     116    116       A -> D (in J-Tongariki).
FT                                /FTId=VAR_002828.
FT   VARIANT     117    117       E -> A (in Ube-4).
FT                                /FTId=VAR_002829.
FT   VARIANT     117    117       E -> EHLPAE (in Zaire).
FT                                /FTId=VAR_002830.
FT   VARIANT     118    118       F -> FI (in Phnom Penh).
FT                                /FTId=VAR_002831.
FT   VARIANT     119    119       T -> TEFT (in Grady).
FT                                /FTId=VAR_002832.
FT   VARIANT     121    121       A -> E (in J-Meerut/J-Birmingham).
FT                                /FTId=VAR_002833.
FT   VARIANT     122    122       V -> M (in Owari).
FT                                /FTId=VAR_002834.
FT   VARIANT     123    123       H -> Q (in Westmead).
FT                                /FTId=VAR_002835.
FT   VARIANT     126    126       L -> P (in Quong Sze; causes alpha-
FT                                thalassemia).
FT                                /FTId=VAR_002836.
FT   VARIANT     126    126       L -> R (in Plasencia; family with
FT                                moderate microcytosis and hypochromia).
FT                                /FTId=VAR_025391.
FT   VARIANT     127    127       D -> G (in West One).
FT                                /FTId=VAR_025392.
FT   VARIANT     127    127       D -> V (in Fukutomi; O(2) affinity up).
FT                                /FTId=VAR_002837.
FT   VARIANT     127    127       D -> Y (in Monteriore; O(2) affinity up).
FT                                /FTId=VAR_002838.
FT   VARIANT     128    128       K -> N (in Jackson).
FT                                /FTId=VAR_002839.
FT   VARIANT     130    130       L -> P (in Tunis-Bizerte; unstable;
FT                                causes alpha-thalassemia).
FT                                /FTId=VAR_002840.
FT   VARIANT     131    131       A -> D (in Yuda; O(2) affinity down).
FT                                /FTId=VAR_002842.
FT   VARIANT     131    131       A -> P (in Sun Prairie; unstable).
FT                                /FTId=VAR_002841.
FT   VARIANT     132    132       S -> P (in Questembert; highly unstable;
FT                                causes alpha-thalassemia).
FT                                /FTId=VAR_002843.
FT   VARIANT     134    134       S -> R (in Val de Marne; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002844.
FT   VARIANT     136    136       V -> E (in Pavie).
FT                                /FTId=VAR_002845.
FT   VARIANT     137    137       L -> M (in Chicago).
FT                                /FTId=VAR_002846.
FT   VARIANT     137    137       L -> P (in Bibba; unstable; causes alpha-
FT                                thalassemia).
FT                                /FTId=VAR_002847.
FT   VARIANT     139    139       S -> P (in Attleboro; O(2) affinity up).
FT                                /FTId=VAR_002848.
FT   VARIANT     140    140       K -> E (in Hanamaki; O(2) affinity up).
FT                                /FTId=VAR_002849.
FT   VARIANT     140    140       K -> T (in Tokoname; O(2) affinity up).
FT                                /FTId=VAR_002850.
FT   VARIANT     141    141       Y -> H (in Rouen; O(2) affinity up).
FT                                /FTId=VAR_002851.
FT   VARIANT     142    142       R -> C (in Nunobiki; O(2) affinity up).
FT                                /FTId=VAR_002852.
FT   VARIANT     142    142       R -> H (in Suresnes; O(2) affinity up).
FT                                /FTId=VAR_002854.
FT   VARIANT     142    142       R -> L (in Legnano; O(2) affinity up).
FT                                /FTId=VAR_002853.
FT   VARIANT     142    142       R -> P (in Singapore).
FT                                /FTId=VAR_002855.
FT   HELIX         4     15
FT   HELIX        16     20
FT   HELIX        21     35
FT   HELIX        37     42
FT   HELIX        53     71
FT   HELIX        73     75
FT   HELIX        76     79
FT   HELIX        81     89
FT   HELIX        96    112
FT   TURN        114    116
FT   HELIX       119    136
FT   TURN        137    139
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBA_PANPA               Reviewed;         142 AA.
AC   P69906; P01922;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 20.
DE   Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin).
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; C93303; HACZP.
DR   SMR; P69906; 2-142.
DR   InterPro; IPR002338; Alpha_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   InterPro; IPR002339; Pi_haem.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052717.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBA_PANTR               Reviewed;         142 AA.
AC   P69907; P01922;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-FEB-2007, entry version 25.
DE   Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin).
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=84169526; PubMed=6689503; DOI=10.1093/nar/11.24.8915;
RA   Liebhaber S.A., Begley K.A.;
RT   "Structural and evolutionary analysis of the two chimpanzee alpha-
RT   globin mRNAs.";
RL   Nucleic Acids Res. 11:8915-8929(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=66071496; PubMed=5855051;
RA   Rifkin D.B., Konigsberg W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X00226; CAA25044.1; -; mRNA.
DR   EMBL; X00227; CAA25045.1; -; mRNA.
DR   PIR; I58217; HACZ.
DR   SMR; P69907; 2-142.
DR   KEGG; hsa:3039; -.
DR   KEGG; hsa:3040; -.
DR   InterPro; IPR002338; Alpha_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   InterPro; IPR002339; Pi_haem.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052720.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBB_HUMAN               Reviewed;         147 AA.
AC   P68871; P02023; Q13852; Q14481; Q14510; Q45KT0; Q6FI08; Q8IZI1;
AC   Q9BX96; Q9UCP8; Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 43.
DE   Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin).
GN   Name=HBB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=81064667; PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6;
RA   Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.;
RT   "The nucleotide sequence of the human beta-globin gene.";
RL   Cell 21:647-651(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=77126403; PubMed=1019344;
RA   Marotta C., Forget B., Cohen-Solal M., Weissman S.M.;
RT   "Nucleotide sequence analysis of coding and noncoding regions of human
RT   beta-globin mRNA.";
RL   Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Lu L., Hu Z.H., Du C.S., Fu Y.S.;
RT   "DNA sequence of the human beta-globin gene isolated from a healthy
RT   Chinese.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE, AND VARIANT DURHAM-N.C. PRO-115.
RC   TISSUE=Blood;
RA   Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.;
RT   "Electrophoretically silent, very unstable, thalassemic mutation at
RT   codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA
RT   sequencing of mRNA, from a Russian women.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE, AND VARIANT LOUISVILLE LEU-43.
RC   TISSUE=Blood;
RA   Kutlar F., Harbin J., Brisco J., Kutlar A.;
RT   "Rapid detection of electrophoretically silent, unstable human
RT   hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA
RT   sequencing of mRNA.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE, AND VARIANT TY GARD GLN-125.
RC   TISSUE=Blood;
RA   Kutlar F., Holley L., Leithner C., Kutlar A.;
RT   "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a
RT   Caucasian female with erythrocytosis.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D.,
RA   Kutlar F.;
RT   "Heterozygote C->A beta-thalassemia mutation at the intron-2/848
RT   nucleotide of beta globin gene was detected on a Northern European
RT   (Caucasian) individual.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-7 AND SER-140.
RC   TISSUE=Blood;
RA   Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.;
RT   "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on
RT   the same chromosome with hemoglobin S mutation, detected in an
RT   African-American family.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE, AND VARIANT O-ARAB.
RC   TISSUE=Blood;
RA   Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.;
RT   "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta-
RT   thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish
RT   patient.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Li W.J.;
RT   "Thalassaemic trait cause by C-T substitution at position -90 in
RT   proximal CACCC box of beta-globin gene in China family.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7.
RX   PubMed=16175509; DOI=10.1086/491748;
RA   Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.;
RT   "The beta-globin recombinational hotspot reduces the effects of strong
RT   selection around HbC, a recently arisen mutation providing resistance
RT   to malaria.";
RL   Am. J. Hum. Genet. 77:637-642(2005).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=13872627;
RA   Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
RA   Rudloff V., Wittmann-Liebold B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [15]
RP   NUCLEOTIDE SEQUENCE OF 122-147.
RX   MEDLINE=85205333; PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9;
RA   Lang K.M., Spritz R.A.;
RT   "Cloning specific complete polyadenylylated 3'-terminal cDNA
RT   segments.";
RL   Gene 33:191-196(1985).
RN   [16]
RP   ACETYLATION AT LYS-145.
RX   PubMed=4531009;
RA   Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.;
RT   "Sites of acetylation of sickle cell hemoglobin by aspirin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974).
RN   [17]
RP   INTERACTION WITH HAPTOGLOBIN.
RX   MEDLINE=86242088; PubMed=3718478;
RA   Yoshioka N., Atassi M.Z.;
RT   "Haemoglobin binding with haptoglobin. Localization of the
RT   haptoglobin-binding sites on the beta-chain of human haemoglobin by
RT   synthetic overlapping peptides encompassing the entire chain.";
RL   Biochem. J. 234:453-456(1986).
RN   [18]
RP   GLYCATION AT VAL-2.
RX   MEDLINE=78138698; PubMed=635569;
RA   Bunn H.F., Gabbay K.H., Gallop P.M.;
RT   "The glycosylation of hemoglobin: relevance to diabetes mellitus.";
RL   Science 200:21-27(1978).
RN   [19]
RP   NITRIC OXIDE-BINDING.
RX   MEDLINE=20056222; PubMed=10588683; DOI=10.1073/pnas.96.25.14206;
RA   Durner J., Gow A.J., Stamler J.S., Glazebrook J.;
RT   "Ancient origins of nitric oxide signaling in biological systems.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999).
RN   [20]
RP   S-NITROSYLATION AT CYS-94.
RX   MEDLINE=99060083; PubMed=9843411; DOI=10.1021/bi9816711;
RA   Chan N.L., Rogers P.H., Arnone A.;
RT   "Crystal structure of the S-nitroso form of liganded human
RT   hemoglobin.";
RL   Biochemistry 37:16459-16464(1998).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND MASS SPECTROMETRY.
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [22]
RP   ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
RX   PubMed=4123689;
RA   Finch J.T., Perutz M.F., Bertles J.F., Doebler J.;
RT   "Structure of sickled erythrocytes and of sickle-cell hemoglobin
RT   fibers.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7.
RX   PubMed=1195378; DOI=10.1016/S0022-2836(75)80108-2;
RA   Wishner B.C., Ward K.B., Lattman E.E., Love W.E.;
RT   "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.";
RL   J. Mol. Biol. 98:179-194(1975).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
RA   Fermi G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5-
RT   A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
RX   PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
RA   Baldwin J.M.;
RT   "The structure of human carbonmonoxy haemoglobin at 2.7-A
RT   resolution.";
RL   J. Mol. Biol. 136:103-128(1980).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8;
RA   Fermi G., Perutz M.F., Shaanan B., Fourme R.;
RT   "The crystal structure of human deoxyhaemoglobin at 1.74 A
RT   resolution.";
RL   J. Mol. Biol. 175:159-174(1984).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
RX   MEDLINE=92232710; PubMed=1567857; DOI=10.1021/bi00131a030;
RA   Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.;
RT   "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta
RT   Trp-->Arg: a mutation that creates an intersubunit chloride-binding
RT   site.";
RL   Biochemistry 31:4111-4121(1992).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
RX   PubMed=1507231; DOI=10.1016/0022-2836(92)90638-Z;
RA   Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.;
RT   "Structure-function relationships in the low-affinity mutant
RT   haemoglobin Aalborg (Gly74 (E18)beta-->Arg).";
RL   J. Mol. Biol. 226:883-888(1992).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=8642597; DOI=10.1006/jmbi.1996.0124;
RA   Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.;
RT   "Crystal structure of T state haemoglobin with oxygen bound at all
RT   four haems.";
RL   J. Mol. Biol. 256:775-792(1996).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38;
RP   GLY-38 AND TYR-38.
RX   PubMed=9521756; DOI=10.1021/bi9708702;
RA   Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.;
RT   "High-resolution crystal structures of human hemoglobin with mutations
RT   at tryptophan 37beta: structural basis for a high-affinity T-state.";
RL   Biochemistry 37:4358-4373(1998).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7.
RX   PubMed=9830011; DOI=10.1074/jbc.273.49.32690;
RA   Harrington D.J., Adachi K., Royer W.E. Jr.;
RT   "Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp.
RT   Implications for the structure and formation of the sickle cell
RT   fiber.";
RL   J. Biol. Chem. 273:32690-32696(1998).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7.
RX   PubMed=12454462; DOI=10.1107/S0907444902016426;
RA   Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L.,
RA   Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.;
RT   "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A
RT   resolution.";
RL   Acta Crystallogr. D 58:2038-2042(2002).
RN   [33]
RP   VARIANT ALABAMA LYS-40.
RX   MEDLINE=75109326; PubMed=1115799;
RA   Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
RA   Atkins R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [34]
RP   VARIANT ALESHA MET-68.
RX   MEDLINE=93322192; PubMed=8330974;
RA   Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S.,
RA   Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.;
RT   "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable
RT   hemoglobin variant identified through sequencing of amplified DNA.";
RL   Hemoglobin 17:217-225(1993).
RN   [35]
RP   VARIANT J-ALTGELDS GARDENS ASP-93.
RX   MEDLINE=79067354; PubMed=721609;
RA   Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.;
RT   "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a
RT   substitution of the proximal histidine of the beta-chain.";
RL   Hemoglobin 2:403-415(1978).
RN   [36]
RP   VARIANT ANKARA ASP-11.
RX   MEDLINE=74297498; PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0;
RA   Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.;
RT   "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp).";
RL   FEBS Lett. 42:121-123(1974).
RN   [37]
RP   VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128.
RX   MEDLINE=86216227; PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0;
RA   Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S.,
RA   Webber B.B., Altay C., Martinez A.V.;
RT   "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family
RT   and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish
RT   family; correction of a previously published identification.";
RL   Biochim. Biophys. Acta 871:229-231(1986).
RN   [38]
RP   VARIANT J-AUCKLAND ASP-26.
RX   MEDLINE=88006903; PubMed=3654265;
RA   Williamson D., Wells R.M.G., Anderson R., Matthews J.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb J-
RT   Auckland [beta 25(B7)Gly-->Asp].";
RL   Hemoglobin 11:221-230(1987).
RN   [39]
RP   VARIANT AURORA TYR-140.
RX   MEDLINE=96352910; PubMed=8718692;
RA   Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.;
RT   "Identification of a new high oxygen affinity hemoglobin variant: Hb
RT   Aurora [beta 139(H17) Asn-->Tyr].";
RL   Hemoglobin 19:335-341(1995).
RN   [40]
RP   VARIANT BREST LYS-128.
RX   MEDLINE=88256755; PubMed=3384710;
RA   Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J.,
RA   Briere J., Galacteros F.;
RT   "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human
RT   hemoglobin variant located at the alpha 1 beta 1 interface with
RT   specific electrophoretic behavior.";
RL   Hemoglobin 12:179-188(1988).
RN   [41]
RP   VARIANT BRISBANE HIS-69.
RX   MEDLINE=81239159; PubMed=6166590;
RA   Brennan S.O., Wells R.M., Smith H., Carrell R.W.;
RT   "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen
RT   affinity variant.";
RL   Hemoglobin 5:325-335(1981).
RN   [42]
RP   VARIANT BUNBURY ASN-95.
RX   MEDLINE=84031649; PubMed=6629823;
RA   Como P.F., Kennett D., Wilkinson T., Kronenberg H.;
RT   "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury:
RT   alpha 2 beta 2 [94 (FG1) Asp replaced by Asn].";
RL   Hemoglobin 7:413-421(1983).
RN   [43]
RP   VARIANT J-CAIRO GLN-66.
RX   MEDLINE=76114933; PubMed=1247583;
RA   Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.;
RT   "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin
RT   variant discovered in an Egyptian family.";
RL   Biochim. Biophys. Acta 420:97-104(1976).
RN   [44]
RP   VARIANT CAMPERDOWN SER-105.
RX   MEDLINE=75184109; PubMed=1138922;
RA   Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M.,
RA   Kronenberg H.;
RT   "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6)
RT   arginine->serine).";
RL   Biochim. Biophys. Acta 393:195-200(1975).
RN   [45]
RP   VARIANT CARIBBEAN ARG-92.
RX   MEDLINE=77048866; PubMed=992050; DOI=10.1016/0014-5793(76)80662-X;
RA   Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E.,
RA   Seakins M., Lang A., Middleton A., Lehmann H.;
RT   "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly
RT   haemoglobin with a low oxygen affinity.";
RL   FEBS Lett. 69:99-102(1976).
RN   [46]
RP   VARIANT CITY OF HOPE SER-70.
RX   MEDLINE=85006311; PubMed=6434492;
RA   Rahbar S., Asmerom Y., Blume K.G.;
RT   "A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope
RT   beta 69 (E13) Gly-->Ser.";
RL   Hemoglobin 8:333-342(1984).
RN   [47]
RP   VARIANT COIMBRA GLU-100.
RX   MEDLINE=92267852; PubMed=1814856;
RA   Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M.,
RA   Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.;
RT   "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered
RT   high oxygen affinity variant.";
RL   Hemoglobin 15:487-496(1991).
RN   [48]
RP   VARIANT COSTA RICA ARG-78.
RX   MEDLINE=96235282; PubMed=8641705; DOI=10.1007/s004390050145;
RA   Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H.,
RA   Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.;
RT   "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example
RT   of a somatic cell mutation in a globin gene.";
RL   Hum. Genet. 97:829-833(1996).
RN   [49]
RP   VARIANT DEBROUSSE PRO-97.
RX   MEDLINE=96180033; PubMed=8602627;
RA   Lacan P., Kister J., Francina A., Souillet G., Galacteros F.,
RA   Delaunay J., Wajcman H.;
RT   "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable
RT   hemoglobin with twofold increased oxygen affinity.";
RL   Am. J. Hematol. 51:276-281(1996).
RN   [50]
RP   VARIANT DHONBURI GLY-127.
RX   MEDLINE=90379198; PubMed=2399911;
RA   Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J.,
RA   Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P.,
RA   Galacteros F.;
RT   "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable
RT   beta variant producing a beta-thalassemia intermedia phenotype in
RT   association with beta zero-thalassemia.";
RL   Am. J. Hematol. 35:96-99(1990).
RN   [51]
RP   VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, AND DESCRIPTION OF
RP   VARIANT DUINO.
RX   MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961;
RA   Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
RA   Melevendi C., Rasore A., Galacteros F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the alpha-
RT   chain and Hb Duino has two residues substituted in the beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
RN   [52]
RP   VARIANT DURHAM-N.C. PRO-115.
RX   MEDLINE=93244842; PubMed=1301199;
RA   Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M.,
RA   Melevendi C., Pirastu M., Cao A.;
RT   "A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro),
RT   causing a severe beta-thalassemia intermedia phenotype.";
RL   Hum. Mutat. 1:124-128(1992).
RN   [53]
RP   VARIANT DURHAM-N.C. PRO-115.
RX   MEDLINE=94154273; PubMed=8111050;
RA   de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.;
RT   "A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro],
RT   produces a dominant thalassemia-like phenotype.";
RL   Blood 83:1109-1116(1994).
RN   [54]
RP   VARIANT J-EUROPA ASP-63.
RX   MEDLINE=96407264; PubMed=8811317;
RA   Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F.,
RA   Wajcman H.;
RT   "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties
RT   in a new variant involving a residue located distal to the heme.";
RL   Hemoglobin 20:135-140(1996).
RN   [55]
RP   VARIANT GEELONG ASP-140.
RX   MEDLINE=92010939; PubMed=1917539;
RA   Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B.,
RA   Tibben E.A., Wilkinson T., Kronenberg H.;
RT   "Hb Geelong [beta 139(H17)Asn-->Asp].";
RL   Hemoglobin 15:85-95(1991).
RN   [56]
RP   VARIANT GRANGE-BLANCHE VAL-28.
RX   MEDLINE=88030044; PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4;
RA   Baklouti F., Giraud Y., Francina A., Richard G., Perier C.,
RA   Geyssant A., Jaubert J., Brizard C., Delaunay J.;
RT   "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with
RT   normal expression and increased affinity for oxygen.";
RL   FEBS Lett. 223:59-62(1987).
RN   [57]
RP   VARIANT GRAZ LEU-3.
RX   MEDLINE=93138927; PubMed=1487420;
RA   Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P.,
RA   Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.;
RT   "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant
RT   observed in four families from southern Austria.";
RL   Hemoglobin 16:493-501(1992).
RN   [58]
RP   VARIANT HELSINKI MET-83.
RX   MEDLINE=77062201; PubMed=826083;
RA   Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F.,
RA   Nagai K., Lang A., Lehmann H.;
RT   "Hb Helsinki: a variant with a high oxygen affinity and a substitution
RT   at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).";
RL   Acta Haematol. 56:257-275(1976).
RN   [59]
RP   VARIANT HIMEJI ASP-141.
RX   MEDLINE=86167527; PubMed=3754244;
RA   Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M.,
RA   Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.;
RT   "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin
RT   with increased beta N-terminal glycation.";
RL   Hemoglobin 10:109-126(1986).
RN   [60]
RP   VARIANT HINSDALE LYS-140.
RX   MEDLINE=90093866; PubMed=2513289;
RA   Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.;
RT   "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central
RT   cavity showing reduced affinity for oxygen and 2,3-
RT   diphosphoglycerate.";
RL   Hemoglobin 13:455-464(1989).
RN   [61]
RP   VARIANT HINWIL ASN-39.
RX   MEDLINE=96351651; PubMed=8745430;
RA   Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C.,
RA   Cao A., Breitenstein U., Fehr J., Tuchschmid P.;
RT   "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected
RT   in a Swiss family.";
RL   Hemoglobin 20:31-40(1996).
RN   [62]
RP   VARIANT HOWICK GLY-38.
RX   MEDLINE=94193408; PubMed=8144352;
RA   Owen M.C., Ockelford P.A., Wells R.M.G.;
RT   "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant
RT   of the alpha 1 beta 2 contact.";
RL   Hemoglobin 17:513-521(1993).
RN   [63]
RP   VARIANT INDIANAPOLIS ARG-113.
RX   MEDLINE=79151109; PubMed=429365;
RA   Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G.,
RA   Tsistrakis G.A.;
RT   "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An
RT   unstable variant detectable only by isotopic labeling.";
RL   J. Biol. Chem. 254:3479-3482(1979).
RN   [64]
RP   VARIANT ISEHARA ASN-93.
RX   MEDLINE=92155974; PubMed=1787097;
RA   Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.;
RT   "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable
RT   variant with a proximal histidine substitution at the heme contact.";
RL   Hemoglobin 15:279-290(1991).
RN   [65]
RP   VARIANT ISTAMBUL GLN-93.
RX   MEDLINE=73054825; PubMed=4639022;
RA   Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J.,
RA   Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.;
RT   "Hemoglobin Istanbul: substitution of glutamine for histidine in a
RT   proximal histidine (F8(92)).";
RL   J. Clin. Invest. 51:2380-2387(1972).
RN   [66]
RP   VARIANT JACKSONVILLE ASP-55.
RX   MEDLINE=91331861; PubMed=2101840;
RA   Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H.,
RA   Moo-Penn W.F.;
RT   "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable
RT   variant found in a patient with hemolytic anemia.";
RL   Hemoglobin 14:653-659(1990).
RN   [67]
RP   VARIANT JIANGHUA ILE-121.
RX   MEDLINE=84007581; PubMed=6618888;
RA   Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H.,
RA   Huang P.Y., Chen S.S., Jai P.C., Yang K.G.;
RT   "Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-
RT   moving variant found in China.";
RL   Hemoglobin 7:321-326(1983).
RN   [68]
RP   VARIANT KARLSKOGA HIS-22.
RX   MEDLINE=93322190; PubMed=8330972;
RA   Landin B.;
RT   "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving
RT   variant found in Sweden.";
RL   Hemoglobin 17:201-208(1993).
RN   [69]
RP   VARIANT KNOSSOS SER-28.
RX   MEDLINE=83079719; PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1;
RA   Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y.,
RA   Komis G., Sellaye M., Boussiou M., Rosa J.;
RT   "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to
RT   Ser. A new abnormal hemoglobin present as a silent beta-thalassemia.";
RL   FEBS Lett. 147:247-250(1982).
RN   [70]
RP   VARIANT KODAIRA GLN-147.
RX   MEDLINE=92340295; PubMed=1634367;
RA   Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R.,
RA   Matsunaga T.;
RT   "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an
RT   amino acid substitution at the C-terminus.";
RL   Hemoglobin 16:85-91(1992).
RN   [71]
RP   VARIANT KOFU ILE-85.
RX   MEDLINE=86303641; PubMed=3744871;
RA   Harano T., Harano K., Ueda S., Imai N., Kitazumi T.;
RT   "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu
RT   or alpha 2 beta 2 84 (EF8) Thr-->Ile.";
RL   Hemoglobin 10:417-420(1986).
RN   [72]
RP   VARIANT HRADEC KRALOVE ASP-116.
RX   MEDLINE=94042221; PubMed=7693620;
RA   Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P.,
RA   Huisman T.H.J.;
RT   "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a
RT   severely unstable hemoglobin variant resulting in a dominant beta-
RT   thalassemia trait in a Czech family.";
RL   Hemoglobin 17:319-328(1993).
RN   [73]
RP   VARIANT LA DESIRADE VAL-130.
RX   MEDLINE=87165149; PubMed=3557994;
RA   Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N.,
RA   Galacteros F., Feingold J., Rosa J.;
RT   "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new
RT   unstable hemoglobin.";
RL   Hemoglobin 10:593-605(1986).
RN   [74]
RP   VARIANT LA ROCHE-SUR-YON HIS-82.
RX   MEDLINE=92172947; PubMed=1540659; DOI=10.1016/0925-4439(92)90052-O;
RA   Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C.,
RA   Cottenceau D., Galacteros F.;
RT   "Structure of the EF corner favors deamidation of asparaginyl residues
RT   in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5)
RT   Leu-->His].";
RL   Biochim. Biophys. Acta 1138:127-132(1992).
RN   [75]
RP   VARIANT LAS PALMAS PHE-50.
RX   MEDLINE=88256753; PubMed=3384708;
RA   Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H.,
RA   Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.;
RT   "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable
RT   hemoglobin variant.";
RL   Hemoglobin 12:163-170(1988).
RN   [76]
RP   VARIANT LINKOPING THR-37.
RX   MEDLINE=88083482; PubMed=3691763;
RA   Berlin G., Wranne B., Jeppsson J.-O.;
RT   "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity
RT   hemoglobin variant found in two families of Finnish origin.";
RL   Eur. J. Haematol. 39:452-456(1987).
RN   [77]
RP   VARIANT MAPUTO TYR-48.
RX   MEDLINE=84031650; PubMed=6629824;
RA   Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L.,
RA   Labie D.;
RT   "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6)
RT   Asp replaced by Tyr) in combination with hemoglobin S, identified by
RT   high performance liquid chromatography (HPLC).";
RL   Hemoglobin 7:423-433(1983).
RN   [78]
RP   VARIANT MATERA LYS-56.
RX   MEDLINE=90346586; PubMed=2384314;
RA   Sciarratta G.V., Ivaldi G.;
RT   "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant
RT   in an Italian family.";
RL   Hemoglobin 14:79-85(1990).
RN   [79]
RP   VARIANT MIYASHIRO GLY-24.
RX   MEDLINE=82166873; PubMed=7338468;
RA   Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H.,
RA   Shinohara T., Hori T., Takayama J.;
RT   "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an
RT   electrophoretically silent variant discovered by the isopropanol
RT   test.";
RL   Hemoglobin 5:653-666(1981).
RN   [80]
RP   VARIANT MIZUHO PRO-69.
RX   MEDLINE=77248961; PubMed=893142;
RA   Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.;
RT   "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new
RT   unstable variant associated with severe hemolytic anemia.";
RL   Hemoglobin 1:467-477(1977).
RN   [81]
RP   VARIANT MUSCAT VAL-33.
RX   MEDLINE=92387956; PubMed=1517102;
RA   Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D.,
RA   Liu J.C., McKie K.M., Huisman T.H.J.;
RT   "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed
RT   in association with HB S in an Arabian family.";
RL   Hemoglobin 16:259-266(1992).
RN   [82]
RP   VARIANT N-TIMONE GLU-9.
RX   MEDLINE=90236754; PubMed=2634671;
RA   Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C.,
RA   Blouquit Y., Craescu C.T., Galacteros F.;
RT   "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving
RT   variant with normal stability and oxygen affinity.";
RL   Hemoglobin 13:743-747(1989).
RN   [83]
RP   VARIANT NAGOYA PRO-98.
RX   MEDLINE=85206960; PubMed=3838976;
RA   Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C.,
RA   Shibata K., Shimokata H., Kuzuya F., Miwa S.;
RT   "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97
RT   (FG4) His-->Pro.";
RL   Hemoglobin 9:11-24(1985).
RN   [84]
RP   VARIANT D-NEATH ALA-122.
RX   MEDLINE=93322197; PubMed=8330979;
RA   Welch S.G., Bateman C.;
RT   "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D
RT   family.";
RL   Hemoglobin 17:255-259(1993).
RN   [85]
RP   VARIANT NORTH CHICAGO SER-37.
RX   MEDLINE=86139289; PubMed=3937824;
RA   Rahbar S., Louis J., Lee T., Asmerom Y.;
RT   "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high
RT   affinity hemoglobin.";
RL   Hemoglobin 9:559-576(1985).
RN   [86]
RP   VARIANT NORTH SHORE-CARACAS GLU-135.
RX   MEDLINE=77246803; PubMed=891976; DOI=10.1016/0014-5793(77)80453-5;
RA   Arends T., Lehmann H., Plowman D., Stathopoulou R.;
RT   "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by
RT   glutamic acid.";
RL   FEBS Lett. 80:261-265(1977).
RN   [87]
RP   VARIANT OLOMOUC ASP-87.
RX   MEDLINE=87307470; PubMed=3623975;
RA   Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B.,
RA   Kutlar A., Huisman T.H.J.;
RT   "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen
RT   affinity variant.";
RL   Hemoglobin 11:151-155(1987).
RN   [88]
RP   VARIANT PALMERSTON NORTH PHE-24.
RX   MEDLINE=83135041; PubMed=7161106;
RA   Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.;
RT   "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new
RT   variant identified in a patient with polycythemia.";
RL   Hemoglobin 6:569-575(1982).
RN   [89]
RP   VARIANT PIERRE-BENITE ASP-91.
RX   MEDLINE=88256754; PubMed=3384709;
RA   Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J.,
RA   Delaunay J.;
RT   "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity
RT   variant found in a French family.";
RL   Hemoglobin 12:171-177(1988).
RN   [90]
RP   VARIANT PRESBYTERIAN LYS-109.
RX   MEDLINE=78215075; PubMed=668922; DOI=10.1016/0014-5793(78)80720-0;
RA   Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.;
RT   "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A
RT   hemoglobin variant with low oxygen affinity.";
RL   FEBS Lett. 92:53-56(1978).
RN   [91]
RP   VARIANT PUTTELANGE VAL-141.
RX   MEDLINE=96101899; PubMed=8522332; DOI=10.1007/BF00210304;
RA   Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I.,
RA   Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J.,
RA   Goossens M., Galacteros F.;
RT   "Germline mosaicism for an alanine to valine substitution at residue
RT   beta 140 in hemoglobin Puttelange, a new variant with high oxygen
RT   affinity.";
RL   Hum. Genet. 96:711-716(1995).
RN   [92]
RP   VARIANT QUIN-HAI ARG-79.
RX   MEDLINE=84031648; PubMed=6629822;
RA   Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y.,
RA   Chang F.Q., Chow Y.C., Chiu Y.;
RT   "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new
RT   abnormal hemoglobin found in Guangdong, China.";
RL   Hemoglobin 7:407-412(1983).
RN   [93]
RP   VARIANT RAMBAM ASP-70.
RX   MEDLINE=98432396; PubMed=9761252;
RA   Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W.,
RA   van Dorsselaer A., Wieland H.;
RT   "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment
RT   of diabetic control: characterization by electrospray mass
RT   spectrometry and HPLC.";
RL   Clin. Chem. 44:2172-2177(1998).
RN   [94]
RP   VARIANT RANDWICK GLY-16.
RX   MEDLINE=88256752; PubMed=3384707;
RA   Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F.,
RA   Kwan Y.L., Holland R.A.B.;
RT   "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-
RT   chain hemoglobin variant.";
RL   Hemoglobin 12:149-161(1988).
RN   [95]
RP   VARIANT RIO GRANDE THR-9.
RX   MEDLINE=83185445; PubMed=6857757;
RA   Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.,
RA   Therrell B.L. Jr.;
RT   "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant
RT   found in a Mexican-American family.";
RL   Hemoglobin 7:91-95(1983).
RN   [96]
RP   VARIANT RUSH GLN-102.
RX   MEDLINE=74080282; PubMed=4129558;
RA   Adams J.G. III, Winter W.P., Tausk K., Heller P.;
RT   "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin
RT   causing mild hemolytic anemia.";
RL   Blood 43:261-269(1974).
RN   [97]
RP   VARIANT SAITAMA PRO-118.
RX   MEDLINE=83185440; PubMed=6687721;
RA   Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y.,
RA   Miyaji T.;
RT   "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant
RT   causing hemolytic disease.";
RL   Hemoglobin 7:47-56(1983).
RN   [98]
RP   VARIANT M-SASKATOON TYR-64.
RX   PubMed=13897827;
RA   Gerald P.S., Efron M.L.;
RT   "Chemical studies of several varieties of Hb M.";
RL   Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961).
RN   [99]
RP   VARIANT SHELBY/LESLIE/DEACONESS LYS-132.
RX   MEDLINE=85130256; PubMed=6526653;
RA   Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.;
RT   "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the
RT   structure of hemoglobin Deaconess and hemoglobin Leslie.";
RL   Hemoglobin 8:583-593(1984).
RN   [100]
RP   VARIANT J-SICILIA ASN-66.
RX   MEDLINE=74302182; PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5;
RA   Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.;
RT   "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia.";
RL   FEBS Lett. 39:200-204(1974).
RN   [101]
RP   VARIANT STANMORE ALA-112.
RX   MEDLINE=92010936; PubMed=1917537;
RA   Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T.,
RA   Kronenberg H., Holland R.A.B., Tibben E.A.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb
RT   Stanmore [beta 111(G13)Val-->Ala].";
RL   Hemoglobin 15:53-65(1991).
RN   [102]
RP   VARIANT ST MANDE TYR-103.
RX   MEDLINE=81212764; PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0;
RA   Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F.,
RA   Chevrier M., Bordahandy C., Rosa J.;
RT   "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low
RT   oxygen affinity variant.";
RL   FEBS Lett. 126:114-116(1981).
RN   [103]
RP   VARIANT WINDSOR ASP-12.
RX   MEDLINE=90093865; PubMed=2599880;
RA   Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B.,
RA   Tibben E.A.;
RT   "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta-
RT   chain hemoglobin variant producing a hemolytic anemia.";
RL   Hemoglobin 13:437-453(1989).
RN   [104]
RP   VARIANT YAHATA TYR-113.
RX   MEDLINE=92010926; PubMed=1917530;
RA   Harano T., Harano K., Kushida Y., Ueda S.;
RT   "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in
RT   a Japanese: structural confirmation by DNA sequencing of the beta-
RT   globin gene.";
RL   Hemoglobin 15:109-113(1991).
RN   [105]
RP   VARIANT YOKOHAMA PRO-32.
RX   MEDLINE=82166874; PubMed=7338469;
RA   Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S.,
RA   Matsumoto N.;
RT   "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting
RT   for Pro, causing hemolytic anemia.";
RL   Hemoglobin 5:667-678(1981).
RN   [106]
RP   VARIANT ZENGCHENG MET-115.
RX   MEDLINE=91177717; PubMed=2079435;
RA   Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J.,
RA   Zeng Y.T., Shen M.;
RT   "Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met.";
RL   Hemoglobin 14:555-557(1990).
RN   [107]
RP   VARIANT IRAQ-HALABJA VAL-11.
RX   PubMed=10398311;
RX   DOI=10.1002/(SICI)1096-8652(199907)61:3<187::AID-AJH5>3.0.CO;2-7;
RA   Deutsch S., Darbellay R., Offord R., Frutiger A., Kister J.,
RA   Wajcman H., Beris P.;
RT   "Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain
RT   silent variant in a family with multiple Hb disorders.";
RL   Am. J. Hematol. 61:187-193(1999).
RN   [108]
RP   VARIANT VILLEJUIF ILE-124.
RX   PubMed=11300351; DOI=10.1081/HEM-100103071;
RA   Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C.,
RA   Pucci P.;
RT   "Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern
RT   Italy.";
RL   Hemoglobin 25:67-78(2001).
RN   [109]
RP   VARIANT TSUKUMI TYR-118.
RX   PubMed=11300344; DOI=10.1081/HEM-100103076;
RA   North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J.,
RA   Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.;
RT   "Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman.";
RL   Hemoglobin 25:107-110(2001).
RN   [110]
RP   VARIANT CANTERBURY PHE-113.
RX   PubMed=11939514; DOI=10.1081/HEM-120002942;
RA   Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A.,
RA   Ferguson M.M.;
RT   "Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable
RT   variant.";
RL   Hemoglobin 26:67-69(2002).
RN   [111]
RP   VARIANT PYRGOS ASP-84, AND VARIANT E LYS-27.
RX   PubMed=12144064; DOI=10.1081/HEM-120005459;
RA   Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P.,
RA   Srisomsap C., Svasti J., Fucharoen S.;
RT   "Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E
RT   [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia.";
RL   Hemoglobin 26:191-196(2002).
RN   [112]
RP   VARIANT SANTANDER ASP-35.
RX   PubMed=12603091; DOI=10.1081/HEM-120016378;
RA   Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E.,
RA   Rodrigo E., Arias M.;
RT   "Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable
RT   variant found as a de novo mutation in a Spanish patient.";
RL   Hemoglobin 27:31-35(2003).
RN   [113]
RP   VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117.
RX   PubMed=12908805; DOI=10.1081/HEM-120023384;
RA   Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J.,
RA   Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L.,
RA   Galacteros F.;
RT   "Two new hemoglobin variants with increased oxygen affinity: Hb Nantes
RT   [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu].";
RL   Hemoglobin 27:191-199(2003).
RN   [114]
RP   VARIANT LYS-27.
RX   PubMed=15481886; DOI=10.1081/HEM-120040334;
RA   Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.;
RT   "The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta-
RT   globin anomalies in the Lao Theung population of southern Laos.";
RL   Hemoglobin 28:197-204(2004).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- INTERACTION:
CC       P69905:HBA1; NbExp=1; IntAct=EBI-715554, EBI-714680;
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- PTM: Glucose reacts non-enzymatically with the N-terminus of the
CC       beta chain to form a stable ketoamine linkage. This takes place
CC       slowly and continuously throughout the 120-day life span of the
CC       red blood cell. The rate of glycation is increased in patients
CC       with diabetes mellitus.
CC   -!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+)
CC       and then transferred to Cys-94 to allow capture of O(2).
CC   -!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin
CC       exposure. Ref.21 reports the identification of HBB acetylated on
CC       Lys-145 in the cytosolic fraction of HeLa cells. This may results
CC       from a contamination of the sample.
CC   -!- DISEASE: Defects in HBB are the cause of beta-thalassemia
CC       [MIM:141900]. The thalassemias are the most common monogenic
CC       diseases and occur mostly in Mediterranean and Southeast Asian
CC       populations. The hallmark of beta-thalassemia is an imbalance in
CC       globin-chain production in the adult HbA molecule. Absence of beta
CC       chain causes beta(0)-thalassemia, while reduced amounts of
CC       detectable beta globin causes beta(+)-thalassemia. In the severe
CC       forms of beta-thalassemia, the excess alpha globin chains
CC       accumulate in the developing erythroid precursors in the marrow.
CC       Their deposition leads to a vast increase in erythroid apoptosis
CC       that in turn causes ineffective erythropoiesis and severe
CC       microcytic hypochromic anemia. Clinically, beta-thalassemia is
CC       divided into thalassemia major (transfusion dependent),
CC       thalassemia intermedia (of intermediate severity), and thalassemia
CC       minor (asymptomatic).
CC   -!- DISEASE: Defects in HBB are the cause of sickle cell anemia
CC       [MIM:603903]; also known as sickle cell disease. Sickle cell
CC       anemia is characterized by abnormally shaped red cells resulting
CC       in chronic anemia and periodic episodes of pain, serious
CC       infections and damage to vital organs. Normal red blood cells are
CC       round and flexible and flow easily through blood vessels, but in
CC       sickle cell anemia, the abnormal hemoglobin (called Hb S) causes
CC       red blood cells to become stiff. They are C-shaped and resembles a
CC       sickle. These stiffer red blood cells can led to microvascular
CC       occlusion thus cutting off the blood supply to nearby tissues.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- WEB RESOURCE: NAME=HbVar;
CC       NOTE=Human hemoglobin variants and thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=HBB".
CC   -!- WEB RESOURCE: NAME=SHMPD;
CC       NOTE=The Singapore human mutation and polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB".
CC   -----------------------------------------------------------------------
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DR   EMBL; U01317; AAA16334.1; -; Genomic_DNA.
DR   EMBL; V00497; CAA23756.1; -; mRNA.
DR   EMBL; V00499; CAA23758.1; -; Genomic_DNA.
DR   EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA.
DR   EMBL; L26462; AAA21100.1; -; Genomic_DNA.
DR   EMBL; L26463; AAA21101.1; -; Genomic_DNA.
DR   EMBL; L26464; AAA21102.1; -; Genomic_DNA.
DR   EMBL; L26465; AAA21103.1; -; Genomic_DNA.
DR   EMBL; L26466; AAA21104.1; -; Genomic_DNA.
DR   EMBL; L26467; AAA21105.1; -; Genomic_DNA.
DR   EMBL; L26468; AAA21106.1; -; Genomic_DNA.
DR   EMBL; L26469; AAA21107.1; -; Genomic_DNA.
DR   EMBL; L26470; AAA21108.1; -; Genomic_DNA.
DR   EMBL; L26471; AAA21109.1; -; Genomic_DNA.
DR   EMBL; L26472; AAA21110.1; -; Genomic_DNA.
DR   EMBL; L26473; AAA21111.1; -; Genomic_DNA.
DR   EMBL; L26474; AAA21112.1; -; Genomic_DNA.
DR   EMBL; L26475; AAA21113.1; -; Genomic_DNA.
DR   EMBL; L26476; AAA21114.1; -; Genomic_DNA.
DR   EMBL; L26477; AAA21115.1; -; Genomic_DNA.
DR   EMBL; L26478; AAA21116.1; -; Genomic_DNA.
DR   EMBL; L48213; AAA88063.1; -; Genomic_DNA.
DR   EMBL; L48214; AAA88061.1; -; Genomic_DNA.
DR   EMBL; L48215; AAA88059.1; -; Genomic_DNA.
DR   EMBL; L48216; AAA88065.1; -; Genomic_DNA.
DR   EMBL; L48217; AAA88067.1; -; Genomic_DNA.
DR   EMBL; M36640; AAA52634.1; -; Genomic_DNA.
DR   EMBL; M11428; AAA52633.1; -; mRNA.
DR   EMBL; M25079; AAA35597.1; -; mRNA.
DR   EMBL; M25113; AAA35966.1; -; mRNA.
DR   EMBL; L48932; AAA88054.1; -; Genomic_DNA.
DR   EMBL; AF007546; AAB62944.1; -; Genomic_DNA.
DR   EMBL; AF117710; AAD19696.1; -; mRNA.
DR   EMBL; AF181989; AAF00489.1; -; mRNA.
DR   EMBL; AF349114; AAK29639.1; -; mRNA.
DR   EMBL; AY260740; AAP21062.1; -; Genomic_DNA.
DR   EMBL; AY136510; AAN11320.1; -; mRNA.
DR   EMBL; AY163866; AAN84548.1; -; Genomic_DNA.
DR   EMBL; AF527577; AAM92001.1; -; Genomic_DNA.
DR   EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA.
DR   EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA.
DR   EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA.
DR   EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA.
DR   EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA.
DR   EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA.
DR   EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA.
DR   EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA.
DR   EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA.
DR   EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA.
DR   EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA.
DR   EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA.
DR   EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA.
DR   EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA.
DR   EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA.
DR   EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA.
DR   EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA.
DR   EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA.
DR   EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA.
DR   EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA.
DR   EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA.
DR   EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA.
DR   EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA.
DR   EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA.
DR   EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA.
DR   EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA.
DR   EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA.
DR   EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA.
DR   EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA.
DR   EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA.
DR   EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA.
DR   EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA.
DR   EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA.
DR   EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA.
DR   EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA.
DR   EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA.
DR   EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA.
DR   EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA.
DR   EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA.
DR   EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA.
DR   EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA.
DR   EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA.
DR   EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA.
DR   EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA.
DR   EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA.
DR   EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA.
DR   EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA.
DR   EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA.
DR   EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA.
DR   EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA.
DR   EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA.
DR   EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA.
DR   EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA.
DR   EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA.
DR   EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA.
DR   EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA.
DR   EMBL; CR536530; CAG38767.1; -; mRNA.
DR   EMBL; CR541913; CAG46711.1; -; mRNA.
DR   EMBL; BC007075; AAH07075.1; -; mRNA.
DR   EMBL; A01592; CAA00182.1; -; Unassigned_DNA.
DR   PIR; A53136; HBHU.
DR   UniGene; Hs.523443; -.
DR   PDB; 1A00; X-ray; B/D=3-147.
DR   PDB; 1A01; X-ray; B/D=3-147.
DR   PDB; 1A0U; X-ray; B/D=3-147.
DR   PDB; 1A0Z; X-ray; B/D=3-147.
DR   PDB; 1A3N; X-ray; B/D=1-147.
DR   PDB; 1A3O; X-ray; B/D=1-147.
DR   PDB; 1ABW; X-ray; B/D=3-147.
DR   PDB; 1ABY; X-ray; B/D=3-147.
DR   PDB; 1AJ9; X-ray; B=1-147.
DR   PDB; 1B86; X-ray; B/D=1-147.
DR   PDB; 1BAB; X-ray; B/D=1-147.
DR   PDB; 1BBB; X-ray; B/D=1-147.
DR   PDB; 1BIJ; X-ray; B/D=1-147.
DR   PDB; 1BUW; X-ray; B/D=-.
DR   PDB; 1BZ0; X-ray; B/D=1-147.
DR   PDB; 1BZ1; X-ray; B/D=1-147.
DR   PDB; 1BZZ; X-ray; B/D=1-147.
DR   PDB; 1C7B; X-ray; B/D=3-147.
DR   PDB; 1C7C; X-ray; B/D=3-147.
DR   PDB; 1C7D; X-ray; B/D=3-147.
DR   PDB; 1CBL; X-ray; A/B/C/D=1-147.
DR   PDB; 1CBM; X-ray; A/B/C/D=1-147.
DR   PDB; 1CLS; X-ray; B/D=1-147.
DR   PDB; 1CMY; X-ray; B/D=1-147.
DR   PDB; 1COH; X-ray; B/D=1-147.
DR   PDB; 1DKE; X-ray; B/D=1-147.
DR   PDB; 1DXT; X-ray; B/D=1-147.
DR   PDB; 1DXU; X-ray; B/D=3-147.
DR   PDB; 1DXV; X-ray; B/D=3-147.
DR   PDB; 1FN3; X-ray; B/D=1-147.
DR   PDB; 1G9V; X-ray; B/D=1-147.
DR   PDB; 1GBU; X-ray; B/D=1-147.
DR   PDB; 1GBV; X-ray; B/D=1-147.
DR   PDB; 1GLI; X-ray; B/D=3-147.
DR   PDB; 1GZX; X-ray; B/D=1-147.
DR   PDB; 1HAB; X-ray; B/D=1-147.
DR   PDB; 1HAC; X-ray; B/D=1-147.
DR   PDB; 1HBA; X-ray; B/D=1-147.
DR   PDB; 1HBB; X-ray; B/D=1-147.
DR   PDB; 1HBS; X-ray; B/D/F/H=1-147.
DR   PDB; 1HCO; X-ray; B=1-147.
DR   PDB; 1HDB; X-ray; B/D=1-147.
DR   PDB; 1HGA; X-ray; B/D=1-147.
DR   PDB; 1HGB; X-ray; B/D=1-147.
DR   PDB; 1HGC; X-ray; B/D=1-147.
DR   PDB; 1HHO; X-ray; B=1-147.
DR   PDB; 1IRD; X-ray; B=1-147.
DR   PDB; 1J3Y; X-ray; B/D/F/H=1-147.
DR   PDB; 1J3Z; X-ray; B/D/F/H=1-147.
DR   PDB; 1J40; X-ray; B/D/F/H=1-147.
DR   PDB; 1J41; X-ray; B/D/F/H=1-147.
DR   PDB; 1J7S; X-ray; B/D=3-147.
DR   PDB; 1J7W; X-ray; B/D=3-147.
DR   PDB; 1J7Y; X-ray; B/D=3-147.
DR   PDB; 1JY7; X-ray; B/D/Q/S/V/X=1-147.
DR   PDB; 1K0Y; X-ray; B/D=1-147.
DR   PDB; 1K1K; X-ray; B=1-147.
DR   PDB; 1KD2; X-ray; B/D=1-147.
DR   PDB; 1LFL; X-ray; B/D/Q/S=1-147.
DR   PDB; 1LFQ; X-ray; B=1-147.
DR   PDB; 1LFT; X-ray; B=1-147.
DR   PDB; 1LFV; X-ray; B=1-147.
DR   PDB; 1LFY; X-ray; B=1-147.
DR   PDB; 1LFZ; X-ray; B=1-147.
DR   PDB; 1LJW; X-ray; B=1-147.
DR   PDB; 1M9P; X-ray; B/D=1-147.
DR   PDB; 1MKO; X-ray; B/D=1-147.
DR   PDB; 1NEJ; X-ray; B/D=1-147.
DR   PDB; 1NIH; X-ray; B/D=1-147.
DR   PDB; 1NQP; X-ray; B/D=1-147.
DR   PDB; 1O1I; X-ray; B=1-147.
DR   PDB; 1O1J; X-ray; B/D=1-147.
DR   PDB; 1O1K; X-ray; B/D=1-147.
DR   PDB; 1O1L; X-ray; B/D=1-147.
DR   PDB; 1O1M; X-ray; B/D=1-147.
DR   PDB; 1O1N; X-ray; B/D=1-147.
DR   PDB; 1O1O; X-ray; B/D=1-147.
DR   PDB; 1O1P; X-ray; B/D=1-147.
DR   PDB; 1QI8; X-ray; B/D=3-147.
DR   PDB; 1QSH; X-ray; B/D=1-147.
DR   PDB; 1QSI; X-ray; B/D=1-147.
DR   PDB; 1QXD; X-ray; B/D=1-147.
DR   PDB; 1QXE; X-ray; B/D=1-147.
DR   PDB; 1R1X; X-ray; B=1-147.
DR   PDB; 1R1Y; X-ray; B/D=1-147.
DR   PDB; 1RPS; X-ray; B/D=1-147.
DR   PDB; 1RQ3; X-ray; B/D=1-147.
DR   PDB; 1RQ4; X-ray; B/D=1-147.
DR   PDB; 1RQA; X-ray; B/D=3-147.
DR   PDB; 1RVW; X-ray; B=1-147.
DR   PDB; 1SDK; X-ray; B/D=1-147.
DR   PDB; 1SDL; X-ray; B/D=1-147.
DR   PDB; 1THB; X-ray; B/D=1-147.
DR   PDB; 1UIW; X-ray; B/D/F/H=1-147.
DR   PDB; 1VWT; X-ray; B/D=1-147.
DR   PDB; 1XXT; X-ray; B/D=1-147.
DR   PDB; 1XY0; X-ray; B/D=1-147.
DR   PDB; 1XYE; X-ray; B/D=1-147.
DR   PDB; 1XZ2; X-ray; B/D=1-147.
DR   PDB; 1XZ4; X-ray; B/D=1-147.
DR   PDB; 1XZ5; X-ray; B/D=1-147.
DR   PDB; 1XZ7; X-ray; B/D=1-147.
DR   PDB; 1XZU; X-ray; B/D=1-147.
DR   PDB; 1XZV; X-ray; B/D=1-147.
DR   PDB; 1Y09; X-ray; B/D=1-147.
DR   PDB; 1Y0A; X-ray; B/D=1-147.
DR   PDB; 1Y0C; X-ray; B/D=1-147.
DR   PDB; 1Y0D; X-ray; B/D=1-147.
DR   PDB; 1Y0T; X-ray; B/D=3-147.
DR   PDB; 1Y0W; X-ray; B/D=3-147.
DR   PDB; 1Y22; X-ray; B/D=3-147.
DR   PDB; 1Y2Z; X-ray; B/D=3-147.
DR   PDB; 1Y31; X-ray; B/D=3-147.
DR   PDB; 1Y35; X-ray; B/D=3-147.
DR   PDB; 1Y45; X-ray; B/D=3-147.
DR   PDB; 1Y46; X-ray; B/D=3-147.
DR   PDB; 1Y4B; X-ray; B/D=3-147.
DR   PDB; 1Y4F; X-ray; B/D=3-147.
DR   PDB; 1Y4G; X-ray; B/D=3-147.
DR   PDB; 1Y4P; X-ray; B/D=3-147.
DR   PDB; 1Y4Q; X-ray; B/D=3-147.
DR   PDB; 1Y4R; X-ray; B/D=3-147.
DR   PDB; 1Y4V; X-ray; B/D=3-147.
DR   PDB; 1Y5F; X-ray; B/D=3-147.
DR   PDB; 1Y5J; X-ray; B/D=3-147.
DR   PDB; 1Y5K; X-ray; B/D=3-147.
DR   PDB; 1Y7C; X-ray; B/D=3-147.
DR   PDB; 1Y7D; X-ray; B/D=3-147.
DR   PDB; 1Y7G; X-ray; B/D=3-147.
DR   PDB; 1Y7Z; X-ray; B/D=3-147.
DR   PDB; 1Y83; X-ray; B/D=3-147.
DR   PDB; 1Y85; X-ray; B/D=1-146.
DR   PDB; 1Y8W; X-ray; B/D=1-147.
DR   PDB; 1YDZ; X-ray; B/D=1-147.
DR   PDB; 1YE0; X-ray; B/D=3-147.
DR   PDB; 1YE1; X-ray; B/D=3-147.
DR   PDB; 1YE2; X-ray; B/D=3-147.
DR   PDB; 1YEN; X-ray; B/D=3-147.
DR   PDB; 1YEO; X-ray; B/D=3-147.
DR   PDB; 1YEQ; X-ray; B/D=3-147.
DR   PDB; 1YEU; X-ray; B/D=3-147.
DR   PDB; 1YEV; X-ray; B/D=3-147.
DR   PDB; 1YFF; X-ray; B/D/F/H=1-147.
DR   PDB; 1YG5; X-ray; B/D=3-147.
DR   PDB; 1YGD; X-ray; B/D=3-147.
DR   PDB; 1YGF; X-ray; B/D=3-147.
DR   PDB; 1YH9; X-ray; B/D=1-147.
DR   PDB; 1YHE; X-ray; B/D=1-147.
DR   PDB; 1YHR; X-ray; B/D=1-147.
DR   PDB; 1YIE; X-ray; B/D=3-147.
DR   PDB; 1YIH; X-ray; B/D=3-147.
DR   PDB; 1YVQ; X-ray; B/D=1-147.
DR   PDB; 1YVT; X-ray; B=1-147.
DR   PDB; 1YZI; X-ray; B=1-147.
DR   PDB; 2D5Z; X-ray; B/D=1-147.
DR   PDB; 2D60; X-ray; B/D=1-147.
DR   PDB; 2DN1; X-ray; B=1-147.
DR   PDB; 2DN2; X-ray; B/D=1-147.
DR   PDB; 2DN3; X-ray; B=-.
DR   PDB; 2H35; NMR; B/D=-.
DR   PDB; 2HBC; X-ray; B=1-147.
DR   PDB; 2HBD; X-ray; B=1-147.
DR   PDB; 2HBE; X-ray; B=1-147.
DR   PDB; 2HBF; X-ray; B=1-147.
DR   PDB; 2HBS; X-ray; B/D/F/H=1-147.
DR   PDB; 2HCO; X-ray; B=1-147.
DR   PDB; 2HHD; X-ray; B/D=1-147.
DR   PDB; 2HHE; X-ray; B/D=4-147.
DR   PDB; 4HHB; X-ray; B/D=1-147.
DR   PDB; 6HBW; X-ray; B/D=1-147.
DR   IntAct; P68871; -.
DR   SWISS-2DPAGE; P68871; HUMAN.
DR   DOSAC-COBS-2DPAGE; P02023; HUMAN.
DR   HSC-2DPAGE; P68871; HUMAN.
DR   PMMA-2DPAGE; P68871; -.
DR   REPRODUCTION-2DPAGE; P68871; HUMAN.
DR   Siena-2DPAGE; P68871; -.
DR   Ensembl; ENSG00000188170; Homo sapiens.
DR   H-InvDB; HIX0009387; -.
DR   HGNC; HGNC:4827; HBB.
DR   MIM; 141900; gene+phenotype.
DR   MIM; 603903; phenotype.
DR   DrugBank; APRD01053; Iron Dextran.
DR   LinkHub; P68871; -.
DR   ArrayExpress; P68871; -.
DR   GermOnline; ENSG00000188170; Homo sapiens.
DR   RZPD-ProtExp; I0513; -.
DR   RZPD-ProtExp; RZPDo834D0222; -.
DR   RZPD-ProtExp; RZPDo834E0633; -.
DR   RZPD-ProtExp; RZPDo839B0670; -.
DR   GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB.
DR   GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB.
DR   GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
DR   GO; GO:0005344; F:oxygen transporter activity; NAS:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; IDA:UniProtKB.
DR   GO; GO:0030185; P:nitric oxide transport; NAS:UniProtKB.
DR   GO; GO:0015671; P:oxygen transport; TAS:UniProtKB.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynt...; NAS:UniProtKB.
DR   InterPro; IPR002337; Beta_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Disease mutation; Heme; Iron; Metal-binding; Oxygen transport;
KW   Polymorphism; S-nitrosylation; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000052976.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
FT   MOD_RES       2      2       N-acetylalanine (in variant Raleigh).
FT   MOD_RES      94     94       S-nitrosocysteine.
FT   MOD_RES     145    145       N6-acetyllysine.
FT   CARBOHYD      2      2       N-linked (Glc) (glycation); in Hb A1C.
FT   VARIANT       2      2       V -> A (in Raleigh; O(2) affinity down).
FT                                /FTId=VAR_002856.
FT   VARIANT       3      3       H -> L (in Graz).
FT                                /FTId=VAR_002857.
FT   VARIANT       3      3       H -> Q (in Okayama; O(2) affinity up).
FT                                /FTId=VAR_002858.
FT   VARIANT       3      3       H -> R (in Deer Lodge; O(2) affinity up).
FT                                /FTId=VAR_002859.
FT   VARIANT       3      3       H -> Y (in Fukuoka).
FT                                /FTId=VAR_002860.
FT   VARIANT       6      6       P -> R (in Warwickshire).
FT                                /FTId=VAR_002861.
FT   VARIANT       7      7       E -> A (in G-Makassar).
FT                                /FTId=VAR_002862.
FT   VARIANT       7      7       E -> K (in C).
FT                                /FTId=VAR_002864.
FT   VARIANT       7      7       E -> Q (in Machida).
FT                                /FTId=VAR_002865.
FT   VARIANT       7      7       E -> V (in S; sickle cell anemia;
FT                                dbSNP:rs334).
FT                                /FTId=VAR_002863.
FT   VARIANT       8      8       E -> G (in G-San Jose; mildly unstable).
FT                                /FTId=VAR_002866.
FT   VARIANT       8      8       E -> K (in G-Siriraj).
FT                                /FTId=VAR_002867.
FT   VARIANT       9      9       K -> E (in N-Timone).
FT                                /FTId=VAR_002868.
FT   VARIANT       9      9       K -> Q (in J-Luhe).
FT                                /FTId=VAR_002869.
FT   VARIANT       9      9       K -> T (in Rio Grande).
FT                                /FTId=VAR_002870.
FT   VARIANT      10     10       S -> C (in Porto Alegre; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002871.
FT   VARIANT      11     11       A -> D (in Ankara).
FT                                /FTId=VAR_002872.
FT   VARIANT      11     11       A -> V (in Iraq-Halabja).
FT                                /FTId=VAR_025393.
FT   VARIANT      12     12       V -> D (in Windsor; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002873.
FT   VARIANT      12     12       V -> I (in Hamilton).
FT                                /FTId=VAR_002874.
FT   VARIANT      14     14       A -> D (in J-Lens).
FT                                /FTId=VAR_002875.
FT   VARIANT      15     15       L -> P (in Saki; unstable).
FT                                /FTId=VAR_002876.
FT   VARIANT      15     15       L -> R (in Soegn; unstable).
FT                                /FTId=VAR_002877.
FT   VARIANT      16     16       W -> G (in Randwick; unstable).
FT                                /FTId=VAR_002878.
FT   VARIANT      16     16       W -> R (in Belfast; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002879.
FT   VARIANT      17     17       G -> D (in J-Baltimore/J-Trinidad/J-
FT                                Ireland/J-Georgia/N-New Haven).
FT                                /FTId=VAR_002880.
FT   VARIANT      17     17       G -> R (in D-Bushman).
FT                                /FTId=VAR_002881.
FT   VARIANT      18     18       K -> E (in Nagasaki).
FT                                /FTId=VAR_002882.
FT   VARIANT      18     18       K -> N (in J-Amiens).
FT                                /FTId=VAR_002883.
FT   VARIANT      18     18       K -> Q (in Nikosia).
FT                                /FTId=VAR_002884.
FT   VARIANT      19     19       V -> M (in Baden; slightly unstable).
FT                                /FTId=VAR_002885.
FT   VARIANT      20     20       N -> D (in Alamo).
FT                                /FTId=VAR_002886.
FT   VARIANT      20     20       N -> K (in D-Ouleh RABAH).
FT                                /FTId=VAR_002887.
FT   VARIANT      20     20       N -> S (in Malay).
FT                                /FTId=VAR_002888.
FT   VARIANT      21     21       V -> M (in Olympia; O(2) affinity up).
FT                                /FTId=VAR_002889.
FT   VARIANT      22     22       D -> G (in Connecticut; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002890.
FT   VARIANT      22     22       D -> H (in Karlskoga).
FT                                /FTId=VAR_002892.
FT   VARIANT      22     22       D -> N (in Cocody).
FT                                /FTId=VAR_002891.
FT   VARIANT      22     22       D -> Y (in Yusa).
FT                                /FTId=VAR_002893.
FT   VARIANT      23     23       E -> A (in G-Coushatta/G-Saskatoon/G-
FT                                Taegu/Hsin Chu).
FT                                /FTId=VAR_002894.
FT   VARIANT      23     23       E -> G (in G-Taipei).
FT                                /FTId=VAR_002895.
FT   VARIANT      23     23       E -> K (in E-Saskatoon; unstable).
FT                                /FTId=VAR_002896.
FT   VARIANT      23     23       E -> Q (in D-Iran).
FT                                /FTId=VAR_002897.
FT   VARIANT      23     23       E -> V (in D-Granada).
FT                                /FTId=VAR_002898.
FT   VARIANT      24     24       V -> D (in Strasbourg; O(2) affinity up).
FT                                /FTId=VAR_002899.
FT   VARIANT      24     24       V -> F (in Palmerston North; O(2)
FT                                affinity up; unstable).
FT                                /FTId=VAR_002900.
FT   VARIANT      24     24       V -> G (in Miyashiro; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002901.
FT   VARIANT      25     25       G -> D (in Moscva; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_002902.
FT   VARIANT      25     25       G -> R (in Riverdale-Bronx; O(2) affinity
FT                                up; unstable).
FT                                /FTId=VAR_002903.
FT   VARIANT      25     25       G -> V (in Savannah; unstable).
FT                                /FTId=VAR_002904.
FT   VARIANT      26     26       G -> D (in J-Auckland; unstable; O(2)
FT                                affinity down).
FT                                /FTId=VAR_002905.
FT   VARIANT      26     26       G -> R (in G-Taiwan Ami).
FT                                /FTId=VAR_002906.
FT   VARIANT      27     27       E -> K (in E).
FT                                /FTId=VAR_002907.
FT   VARIANT      27     27       E -> V (in Henri Mondor; slightly
FT                                unstable).
FT                                /FTId=VAR_002908.
FT   VARIANT      28     28       A -> D (in Volga/Drenthe; unstable).
FT                                /FTId=VAR_002909.
FT   VARIANT      28     28       A -> S (in Knossos).
FT                                /FTId=VAR_002910.
FT   VARIANT      28     28       A -> V (in Grange-blanche; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002911.
FT   VARIANT      29     29       L -> P (in Genova/Hyogo; unstable).
FT                                /FTId=VAR_002912.
FT   VARIANT      30     30       G -> D (in Lufkin; unstable).
FT                                /FTId=VAR_002913.
FT   VARIANT      31     31       R -> S (in Tacoma; unstable).
FT                                /FTId=VAR_002914.
FT   VARIANT      32     32       L -> P (in Yokohama; unstable).
FT                                /FTId=VAR_002915.
FT   VARIANT      33     33       L -> R (in Castilla; unstable).
FT                                /FTId=VAR_002916.
FT   VARIANT      33     33       L -> V (in Muscat; slightly unstable).
FT                                /FTId=VAR_002917.
FT   VARIANT      35     35       V -> D (in Santander; unstable).
FT                                /FTId=VAR_025394.
FT   VARIANT      35     35       V -> F (in Pitie-Salpetriere; O(2)
FT                                affinity up).
FT                                /FTId=VAR_002918.
FT   VARIANT      35     35       V -> L (in Nantes; increased oxygen
FT                                affinity).
FT                                /FTId=VAR_025395.
FT   VARIANT      36     36       Y -> F (in Philly; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002919.
FT   VARIANT      37     37       P -> R (in Sunnybrook).
FT                                /FTId=VAR_002920.
FT   VARIANT      37     37       P -> S (in North Chicago; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002921.
FT   VARIANT      37     37       P -> T (in Linkoping/Finlandia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_002922.
FT   VARIANT      38     38       W -> G (in Howick).
FT                                /FTId=VAR_002923.
FT   VARIANT      38     38       W -> R (in Rothschild; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002925.
FT   VARIANT      38     38       W -> S (in Hirose; O(2) affinity up).
FT                                /FTId=VAR_002924.
FT   VARIANT      39     39       T -> N (in Hinwil; O(2) affinity up).
FT                                /FTId=VAR_002926.
FT   VARIANT      40     40       Q -> E (in Vaasa; unstable).
FT                                /FTId=VAR_002927.
FT   VARIANT      40     40       Q -> K (in Alabama).
FT                                /FTId=VAR_002928.
FT   VARIANT      40     40       Q -> R (in Tianshui).
FT                                /FTId=VAR_002929.
FT   VARIANT      42     42       F -> Y (in Mequon).
FT                                /FTId=VAR_002930.
FT   VARIANT      43     43       F -> L (in Louisville; unstable).
FT                                /FTId=VAR_002931.
FT   VARIANT      44     44       E -> Q (in Hoshida/Chaya).
FT                                /FTId=VAR_002932.
FT   VARIANT      45     45       S -> C (in Mississippi).
FT                                /FTId=VAR_002933.
FT   VARIANT      46     46       F -> S (in Cheverly; unstable).
FT                                /FTId=VAR_002934.
FT   VARIANT      47     47       G -> E (in K-Ibadan).
FT                                /FTId=VAR_002935.
FT   VARIANT      48     48       D -> A (in Avicenna).
FT                                /FTId=VAR_002936.
FT   VARIANT      48     48       D -> G (in Gavello).
FT                                /FTId=VAR_002937.
FT   VARIANT      48     48       D -> Y (in Maputo).
FT                                /FTId=VAR_002938.
FT   VARIANT      49     49       L -> P (in Bab-Saadoum; slightly
FT                                unstable).
FT                                /FTId=VAR_002939.
FT   VARIANT      50     50       S -> F (in Las Palmas; slightly
FT                                unstable).
FT                                /FTId=VAR_002940.
FT   VARIANT      51     51       T -> K (in Edmonton).
FT                                /FTId=VAR_002941.
FT   VARIANT      52     52       P -> R (in Willamette; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002942.
FT   VARIANT      53     53       D -> A (in Ocho Rios).
FT                                /FTId=VAR_002943.
FT   VARIANT      53     53       D -> H (in Summer Hill).
FT                                /FTId=VAR_002944.
FT   VARIANT      55     55       V -> D (in Jacksonville; O(2) affinity
FT                                up; unstable).
FT                                /FTId=VAR_002945.
FT   VARIANT      56     56       M -> K (in Matera; unstable).
FT                                /FTId=VAR_002946.
FT   VARIANT      57     57       G -> R (in Hamadan).
FT                                /FTId=VAR_002947.
FT   VARIANT      58     58       N -> K (in G-ferrara; unstable).
FT                                /FTId=VAR_002948.
FT   VARIANT      59     59       P -> R (in Dhofar/Yukuhashi).
FT                                /FTId=VAR_002949.
FT   VARIANT      60     60       K -> E (in I-High Wycombe).
FT                                /FTId=VAR_002950.
FT   VARIANT      61     61       V -> A (in Collingwood; unstable).
FT                                /FTId=VAR_002951.
FT   VARIANT      62     62       K -> E (in N-Seatlle).
FT                                /FTId=VAR_002952.
FT   VARIANT      62     62       K -> M (in Bologna; O(2) affinity down).
FT                                /FTId=VAR_002953.
FT   VARIANT      62     62       K -> N (in Hikari).
FT                                /FTId=VAR_002954.
FT   VARIANT      63     63       A -> D (in J-Europa).
FT                                /FTId=VAR_002955.
FT   VARIANT      63     63       A -> P (in Duarte; unstable).
FT                                /FTId=VAR_002956.
FT   VARIANT      64     64       H -> Y (in M-Saskatoon; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002957.
FT   VARIANT      66     66       K -> M (in J-Antakya).
FT                                /FTId=VAR_002958.
FT   VARIANT      66     66       K -> N (in J-Sicilia).
FT                                /FTId=VAR_002959.
FT   VARIANT      66     66       K -> Q (in J-Cairo).
FT                                /FTId=VAR_002960.
FT   VARIANT      67     67       K -> T (in Chico; O(2) affinity down).
FT                                /FTId=VAR_002961.
FT   VARIANT      68     68       V -> A (in Sydney; unstable).
FT                                /FTId=VAR_002962.
FT   VARIANT      68     68       V -> M (in Alesha; unstable).
FT                                /FTId=VAR_002963.
FT   VARIANT      69     69       L -> H (in Brisbane; O(2) affinity up).
FT                                /FTId=VAR_002964.
FT   VARIANT      69     69       L -> P (in Mizuho; unstable).
FT                                /FTId=VAR_002965.
FT   VARIANT      70     70       G -> D (in Rambam).
FT                                /FTId=VAR_002966.
FT   VARIANT      70     70       G -> R (in Kenitra).
FT                                /FTId=VAR_002967.
FT   VARIANT      70     70       G -> S (in City of Hope).
FT                                /FTId=VAR_002968.
FT   VARIANT      71     71       A -> D (in Seattle; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_002969.
FT   VARIANT      72     72       F -> S (in Christchurch; unstable).
FT                                /FTId=VAR_002970.
FT   VARIANT      74     74       D -> G (in Tilburg; O(2) affinity down).
FT                                /FTId=VAR_002971.
FT   VARIANT      74     74       D -> V (in Mobile; O(2) affinity down).
FT                                /FTId=VAR_002972.
FT   VARIANT      74     74       D -> Y (in Vancouver; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002973.
FT   VARIANT      75     75       G -> R (in Aalborg; unstable).
FT                                /FTId=VAR_002974.
FT   VARIANT      75     75       G -> V (in Bushwick; unstable).
FT                                /FTId=VAR_002975.
FT   VARIANT      76     76       L -> P (in Atlanta; unstable).
FT                                /FTId=VAR_002976.
FT   VARIANT      76     76       L -> R (in Pasadena; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002977.
FT   VARIANT      77     77       A -> D (in J-Chicago).
FT                                /FTId=VAR_002978.
FT   VARIANT      78     78       H -> D (in J-Iran).
FT                                /FTId=VAR_002979.
FT   VARIANT      78     78       H -> R (in Costa Rica).
FT                                /FTId=VAR_002980.
FT   VARIANT      78     78       H -> Y (in Fukuyama).
FT                                /FTId=VAR_002981.
FT   VARIANT      79     79       L -> R (in Quin-hai).
FT                                /FTId=VAR_002982.
FT   VARIANT      80     80       D -> Y (in Tampa).
FT                                /FTId=VAR_002983.
FT   VARIANT      81     81       N -> K (in G-Szuhu/Gifu).
FT                                /FTId=VAR_002984.
FT   VARIANT      82     82       L -> H (in La Roche-sur-Yon; unstable and
FT                                O(2) affinity up).
FT                                /FTId=VAR_012663.
FT   VARIANT      82     82       L -> R (in Baylor; unstable).
FT                                /FTId=VAR_002985.
FT   VARIANT      83     83       K -> M (in Helsinki; O(2) affinity up).
FT                                /FTId=VAR_002986.
FT   VARIANT      83     83       K -> N (in Providence).
FT                                /FTId=VAR_012664.
FT   VARIANT      84     84       G -> D (in Pyrgos).
FT                                /FTId=VAR_025396.
FT   VARIANT      84     84       G -> R (in Muskegon).
FT                                /FTId=VAR_002987.
FT   VARIANT      85     85       T -> I (in Kofu).
FT                                /FTId=VAR_002988.
FT   VARIANT      87     87       A -> D (in Olomouc; O(2) affinity up).
FT                                /FTId=VAR_002989.
FT   VARIANT      88     88       T -> I (in Quebec-Chori).
FT                                /FTId=VAR_002990.
FT   VARIANT      88     88       T -> K (in D-Ibadan).
FT                                /FTId=VAR_002991.
FT   VARIANT      88     88       T -> P (in Valletta).
FT                                /FTId=VAR_002992.
FT   VARIANT      89     89       L -> P (in Santa Ana; unstable).
FT                                /FTId=VAR_002993.
FT   VARIANT      89     89       L -> R (in Boras; unstable).
FT                                /FTId=VAR_002994.
FT   VARIANT      90     90       S -> N (in Creteil; O(2) affinity up).
FT                                /FTId=VAR_002995.
FT   VARIANT      90     90       S -> R (in Vanderbilt; O(2) affinity up).
FT                                /FTId=VAR_002996.
FT   VARIANT      91     91       E -> D (in Pierre-Benite; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002997.
FT   VARIANT      91     91       E -> K (in Agenogi; O(2) affinity down).
FT                                /FTId=VAR_002998.
FT   VARIANT      92     92       L -> P (in Sabine; unstable).
FT                                /FTId=VAR_002999.
FT   VARIANT      92     92       L -> R (in Caribbean; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003000.
FT   VARIANT      93     93       H -> D (in J-Altgelds Gardens; unstable).
FT                                /FTId=VAR_003001.
FT   VARIANT      93     93       H -> N (in Isehara; unstable).
FT                                /FTId=VAR_003002.
FT   VARIANT      93     93       H -> P (in Newcastle and Duino;
FT                                associated with S-104 in Duino;
FT                                unstable).
FT                                /FTId=VAR_003003.
FT   VARIANT      93     93       H -> Q (in Istambul; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003004.
FT   VARIANT      94     94       C -> R (in Okazaki; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003005.
FT   VARIANT      95     95       D -> G (in Chandigarh).
FT                                /FTId=VAR_003006.
FT   VARIANT      95     95       D -> H (in Barcelona; O(2) affinity up).
FT                                /FTId=VAR_003007.
FT   VARIANT      95     95       D -> N (in Bunbury; O(2) affinity up).
FT                                /FTId=VAR_003008.
FT   VARIANT      96     96       K -> M (in J-Cordoba).
FT                                /FTId=VAR_003009.
FT   VARIANT      96     96       K -> N (in Detroit).
FT                                /FTId=VAR_003010.
FT   VARIANT      97     97       L -> P (in Debrousse; unstable; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003011.
FT   VARIANT      97     97       L -> V (in Regina; O(2) affinity up).
FT                                /FTId=VAR_003012.
FT   VARIANT      98     98       H -> L (in Wood; O(2) affinity up).
FT                                /FTId=VAR_003013.
FT   VARIANT      98     98       H -> P (in Nagoya; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003014.
FT   VARIANT      98     98       H -> Q (in Malmoe; O(2) affinity up).
FT                                /FTId=VAR_003015.
FT   VARIANT      98     98       H -> Y (in Moriguchi).
FT                                /FTId=VAR_003016.
FT   VARIANT      99     99       V -> G (in Nottingham; unstable).
FT                                /FTId=VAR_003017.
FT   VARIANT     100    100       D -> E (in Coimbra; O(2) affinity up).
FT                                /FTId=VAR_003018.
FT   VARIANT     101    101       P -> L (in Brigham; O(2) affinity up).
FT                                /FTId=VAR_003019.
FT   VARIANT     101    101       P -> R (in New Mexico).
FT                                /FTId=VAR_003020.
FT   VARIANT     102    102       E -> D (in Potomac; O(2) affinity up).
FT                                /FTId=VAR_003021.
FT   VARIANT     102    102       E -> G (in Alberta; O(2) affinity up).
FT                                /FTId=VAR_003022.
FT   VARIANT     102    102       E -> K (in British Columbia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003023.
FT   VARIANT     102    102       E -> Q (in Rush; unstable).
FT                                /FTId=VAR_003024.
FT   VARIANT     103    103       N -> S (in Beth Israel; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003025.
FT   VARIANT     103    103       N -> Y (in St Mande; O(2) affinity down).
FT                                /FTId=VAR_003026.
FT   VARIANT     104    104       F -> L (in Heathrow; O(2) affinity up).
FT                                /FTId=VAR_003027.
FT   VARIANT     105    105       R -> S (in Camperdown and Duino;
FT                                associated with P-92 in Duino; unstable).
FT                                /FTId=VAR_003028.
FT   VARIANT     105    105       R -> T (in Sherwood Forest).
FT                                /FTId=VAR_003029.
FT   VARIANT     108    108       G -> R (in Burke; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003030.
FT   VARIANT     109    109       N -> K (in Presbyterian; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003031.
FT   VARIANT     110    110       V -> M (in San Diego; O(2) affinity up).
FT                                /FTId=VAR_003032.
FT   VARIANT     111    111       L -> P (in Showa-Yakushiji).
FT                                /FTId=VAR_003033.
FT   VARIANT     112    112       V -> A (in Stanmore; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003034.
FT   VARIANT     113    113       C -> F (in Canterbury).
FT                                /FTId=VAR_025397.
FT   VARIANT     113    113       C -> R (in Indianapolis).
FT                                /FTId=VAR_003035.
FT   VARIANT     113    113       C -> Y (in Yahata).
FT                                /FTId=VAR_003036.
FT   VARIANT     115    115       L -> M (in Zengcheng).
FT                                /FTId=VAR_010144.
FT   VARIANT     115    115       L -> P (in Durham-N.C./Brescia; causes
FT                                beta-thalassemia).
FT                                /FTId=VAR_010145.
FT   VARIANT     116    116       A -> D (in Hradec Kralove; unstable;
FT                                causes severe beta-thalassemia).
FT                                /FTId=VAR_003037.
FT   VARIANT     116    116       A -> P (in Madrid; unstable).
FT                                /FTId=VAR_003038.
FT   VARIANT     117    117       H -> L (in Vexin; increased oxygen
FT                                affinity).
FT                                /FTId=VAR_025398.
FT   VARIANT     117    117       H -> Q (in Hafnia).
FT                                /FTId=VAR_003039.
FT   VARIANT     118    118       H -> P (in Saitama; unstable).
FT                                /FTId=VAR_003040.
FT   VARIANT     118    118       H -> R (in P-Galveston).
FT                                /FTId=VAR_003041.
FT   VARIANT     118    118       H -> Y (in Tsukumi).
FT                                /FTId=VAR_025399.
FT   VARIANT     120    120       G -> A (in Iowa).
FT                                /FTId=VAR_003042.
FT   VARIANT     121    121       K -> E (in Hijiyama).
FT                                /FTId=VAR_003043.
FT   VARIANT     121    121       K -> I (in Jianghua).
FT                                /FTId=VAR_003044.
FT   VARIANT     121    121       K -> Q (in Takamatsu).
FT                                /FTId=VAR_003045.
FT   VARIANT     122    122       E -> A (in D-Neath).
FT                                /FTId=VAR_003046.
FT   VARIANT     122    122       E -> G (in St Francis).
FT                                /FTId=VAR_003047.
FT   VARIANT     122    122       E -> K (in O-Arab).
FT                                /FTId=VAR_003049.
FT   VARIANT     122    122       E -> Q (in D-Los Angeles/D-Punjab/D-
FT                                Portugal/D-Chicago/D-Oak Ridge).
FT                                /FTId=VAR_003048.
FT   VARIANT     122    122       E -> V (in D-Camperdown/Beograd).
FT                                /FTId=VAR_003050.
FT   VARIANT     124    124       T -> I (in Villejuif; asymptomatic
FT                                variant).
FT                                /FTId=VAR_003051.
FT   VARIANT     125    125       P -> Q (in Ty Gard; O(2) affinity up).
FT                                /FTId=VAR_003053.
FT   VARIANT     125    125       P -> R (in Khartoum; unstable).
FT                                /FTId=VAR_003052.
FT   VARIANT     125    125       P -> S (in Tunis).
FT                                /FTId=VAR_003054.
FT   VARIANT     127    127       V -> A (in Beirut).
FT                                /FTId=VAR_003055.
FT   VARIANT     127    127       V -> E (in Hofu; unstable).
FT                                /FTId=VAR_003057.
FT   VARIANT     127    127       V -> G (in Dhonburi/Neapolis; unstable;
FT                                beta-thalassemia).
FT                                /FTId=VAR_003056.
FT   VARIANT     128    128       Q -> E (in Complutense).
FT                                /FTId=VAR_003058.
FT   VARIANT     128    128       Q -> K (in Brest; unstable).
FT                                /FTId=VAR_003059.
FT   VARIANT     129    129       A -> D (in J-Guantanamo; unstable).
FT                                /FTId=VAR_003060.
FT   VARIANT     130    130       A -> P (in Crete; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003061.
FT   VARIANT     130    130       A -> V (in La Desirade; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003062.
FT   VARIANT     131    131       Y -> D (in Wien; unstable).
FT                                /FTId=VAR_003063.
FT   VARIANT     131    131       Y -> S (in Nevers).
FT                                /FTId=VAR_003064.
FT   VARIANT     132    132       Q -> E (in Camden/Tokuchi/Motown).
FT                                /FTId=VAR_003065.
FT   VARIANT     132    132       Q -> K (in Shelby/Leslie/Deaconess;
FT                                unstable).
FT                                /FTId=VAR_003066.
FT   VARIANT     132    132       Q -> P (in Shangai; unstable).
FT                                /FTId=VAR_003067.
FT   VARIANT     132    132       Q -> R (in Sarrebourg; unstable).
FT                                /FTId=VAR_003068.
FT   VARIANT     133    133       K -> N (in Yamagata; O(2) affinity down).
FT                                /FTId=VAR_003069.
FT   VARIANT     133    133       K -> Q (in K-Woolwich).
FT                                /FTId=VAR_003070.
FT   VARIANT     134    134       V -> L (in Extredemura).
FT                                /FTId=VAR_003071.
FT   VARIANT     135    135       V -> E (in North Shore-Caracas;
FT                                unstable).
FT                                /FTId=VAR_003072.
FT   VARIANT     136    136       A -> E (in Beckman; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003073.
FT   VARIANT     136    136       A -> P (in Altdorf; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003074.
FT   VARIANT     137    137       G -> D (in Hope; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003075.
FT   VARIANT     139    139       A -> P (in Brockton; unstable).
FT                                /FTId=VAR_003076.
FT   VARIANT     140    140       N -> D (in Geelong; unstable).
FT                                /FTId=VAR_003077.
FT   VARIANT     140    140       N -> K (in Hinsdale; O(2) affinity down).
FT                                /FTId=VAR_003078.
FT   VARIANT     140    140       N -> S (in S-Wake; associated with V-6).
FT                                /FTId=VAR_025335.
FT   VARIANT     140    140       N -> Y (in Aurora; O(2) affinity up).
FT                                /FTId=VAR_003079.
FT   VARIANT     141    141       A -> D (in Himeji; unstable; O(2)
FT                                affinity down).
FT                                /FTId=VAR_003080.
FT   VARIANT     141    141       A -> T (in St Jacques: O(2) affinity up).
FT                                /FTId=VAR_003081.
FT   VARIANT     141    141       A -> V (in Puttelange; polycythemia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003082.
FT   VARIANT     142    142       L -> R (in Olmsted; unstable).
FT                                /FTId=VAR_003083.
FT   VARIANT     143    143       A -> D (in Ohio; O(2) affinity up).
FT                                /FTId=VAR_003084.
FT   VARIANT     144    144       H -> D (in Rancho Mirage).
FT                                /FTId=VAR_003085.
FT   VARIANT     144    144       H -> P (in Syracuse; O(2) affinity up).
FT                                /FTId=VAR_003087.
FT   VARIANT     144    144       H -> Q (in Little Rock; O(2) affinity
FT                                up).
FT                                /FTId=VAR_003086.
FT   VARIANT     144    144       H -> R (in Abruzzo; O(2) affinity up).
FT                                /FTId=VAR_003088.
FT   VARIANT     145    145       K -> E (in Mito; O(2) affinity up).
FT                                /FTId=VAR_003089.
FT   VARIANT     146    146       Y -> C (in Rainier; O(2) affinity up).
FT                                /FTId=VAR_003090.
FT   VARIANT     146    146       Y -> H (in Bethesda; O(2) affinity up).
FT                                /FTId=VAR_003091.
FT   VARIANT     147    147       H -> D (in Hiroshima; O(2) affinity up).
FT                                /FTId=VAR_003092.
FT   VARIANT     147    147       H -> L (in Cowtown; O(2) affinity up).
FT                                /FTId=VAR_003093.
FT   VARIANT     147    147       H -> P (in York; O(2) affinity up).
FT                                /FTId=VAR_003094.
FT   VARIANT     147    147       H -> Q (in Kodaira; O(2) affinity up).
FT                                /FTId=VAR_003095.
FT   HELIX         5     15
FT   TURN         20     22
FT   HELIX        23     34
FT   HELIX        36     41
FT   HELIX        43     45
FT   HELIX        51     56
FT   HELIX        58     76
FT   TURN         77     79
FT   HELIX        81     93
FT   TURN         94     96
FT   HELIX       101    118
FT   HELIX       119    121
FT   HELIX       124    141
FT   HELIX       143    145
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   HBB_PANPA               Reviewed;         147 AA.
AC   P68872; P02023; Q13852; Q14481; Q14510; Q9BX96; Q9UCP8; Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 20.
DE   Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin).
GN   Name=HBB;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-147.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; D93303; HBCZP.
DR   SMR; P68872; 2-147.
DR   InterPro; IPR002337; Beta_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000053056.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   HBB_PANTR               Reviewed;         147 AA.
AC   P68873; P02023; Q13852; Q14481; Q14510; Q28799; Q9BX96; Q9UCP8;
AC   Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 24.
DE   Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin).
GN   Name=HBB;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX   MEDLINE=85210896; PubMed=3999143; DOI=10.1016/0022-2836(85)90024-5;
RA   Savatier P., Trabuchet G., Faure C., Chebloune Y., Gouy M.,
RA   Verdier G., Nigon V.M.;
RT   "Evolution of the primate beta-globin gene region. High rate of
RT   variation in CpG dinucleotides and in short repeated sequences between
RT   man and chimpanzee.";
RL   J. Mol. Biol. 182:21-29(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   MEDLINE=66071496; PubMed=5855051;
RA   Rifkin D.B., Konigsberg W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous
CC       gene model prediction.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X02345; CAA26204.1; -; Genomic_DNA.
DR   PIR; B93303; HBCZ.
DR   SMR; P68873; 2-147.
DR   KEGG; hsa:3043; -.
DR   KEGG; ptr:450978; -.
DR   InterPro; IPR002337; Beta_haem.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin_like.
DR   InterPro; IPR012292; Globin_related.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   PROSITE; PS01033; GLOBIN; 1.
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000053060.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   LACI_ECOLI              Reviewed;         360 AA.
AC   P03023; O09196; P71309; Q2MC79; Q47338;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 3.
DT   20-MAR-2007, entry version 87.
DE   Lactose operon repressor.
GN   Name=lacI; OrderedLocusNames=b0345, JW0336;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=78246991; PubMed=355891; DOI=10.1038/274765a0;
RA   Farabaugh P.J.;
RT   "Sequence of the lacI gene.";
RL   Nature 274:765-769(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chen J., Matthews K.K.S.M.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Marsh S.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360.
RX   MEDLINE=76091932; PubMed=1107032;
RA   Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.;
RT   "Amino-acid sequence of lac repressor from Escherichia coli.
RT   Isolation, sequence analysis and sequence assembly of tryptic peptides
RT   and cyanogen-bromide fragments.";
RL   Eur. J. Biochem. 59:491-509(1975).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
RX   MEDLINE=73143730; PubMed=4571224;
RA   Platt T., Files J.G., Weber K.;
RT   "Lac repressor. Specific proteolytic destruction of the NH 2 -terminal
RT   region and loss of the deoxyribonucleic acid-binding activity.";
RL   J. Biol. Chem. 248:110-121(1973).
RN   [9]
RP   PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86.
RX   MEDLINE=74126378; PubMed=4594037;
RA   Ganem D., Miller J.H., Files J.G., Platt T., Weber K.;
RT   "Reinitiation of a lac repressor fragment at a condon other than
RT   AUG.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RX   MEDLINE=88230449; PubMed=3286877; DOI=10.1016/0022-2836(88)90237-9;
RA   Gordon A.J.E., Burns P.A., Fix D.F., Yatagai F., Allen F.L.,
RA   Horsfall M.J., Halliday J.A., Gray J., Bernelot-Moens C.,
RA   Glickman B.W.;
RT   "Missense mutation in the lacI gene of Escherichia coli. Inferences on
RT   the structure of the repressor protein.";
RL   J. Mol. Biol. 200:239-251(1988).
RN   [11]
RP   PROTEIN SEQUENCE OF 1-35.
RX   MEDLINE=96087076; PubMed=7498473; DOI=10.1016/0014-5793(95)01153-6;
RA   Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.;
RT   "Mechanism of Lac repressor switch-off: orientation of the Lac
RT   repressor DNA-binding domain is reversed upon inducer binding.";
RL   FEBS Lett. 375:27-30(1995).
RN   [12]
RP   MUTAGENESIS.
RX   MEDLINE=90183956; PubMed=2178920;
RA   Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B.,
RA   Mueller-Hill B.;
RT   "Mutant lac repressors with new specificities hint at rules for
RT   protein-DNA recognition.";
RL   EMBO J. 9:615-621(1990).
RN   [13]
RP   MUTAGENESIS.
RX   MEDLINE=94322386; PubMed=8046748; DOI=10.1006/jmbi.1994.1458;
RA   Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.;
RT   "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered
RT   Escherichia coli lac repressors reveals essential and non-essential
RT   residues, as well as 'spacers' which do not require a specific
RT   sequence.";
RL   J. Mol. Biol. 240:421-433(1994).
RN   [14]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE=91249837; PubMed=2040302;
RA   Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B.,
RA   Mueller-Hill B.;
RT   "A model of the lac repressor-operator complex based on physical and
RT   genetic data.";
RL   Eur. J. Biochem. 198:411-419(1991).
RN   [15]
RP   3D-STRUCTURE MODELING OF 1-56.
RX   MEDLINE=92020210; PubMed=1923807; DOI=10.1093/nar/19.19.5233;
RA   Shin J.A., Ebright R.H., Dervan P.B.;
RT   "Orientation of the Lac repressor DNA binding domain in complex with
RT   the left lac operator half site characterized by affinity cleaving.";
RL   Nucleic Acids Res. 19:5233-5236(1991).
RN   [16]
RP   STRUCTURE BY NMR.
RX   MEDLINE=89113344; PubMed=3064080;
RA   Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H.,
RA   Kaptein R.;
RT   "The interaction of lac repressor headpiece with its operator: an NMR
RT   view.";
RL   Protein Seq. Data Anal. 1:487-498(1988).
RN   [17]
RP   STRUCTURE BY NMR.
RX   MEDLINE=89302886; PubMed=2742823; DOI=10.1021/bi00433a037;
RA   Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H.,
RA   Kaptein R., Buck F., Fera B., Rueterjans H.;
RT   "H NMR study of a complex between the lac repressor headpiece and a 22
RT   base pair symmetric lac operator.";
RL   Biochemistry 28:2985-2991(1989).
RN   [18]
RP   STRUCTURE BY NMR OF 1-56.
RX   MEDLINE=96275660; PubMed=8683581; DOI=10.1006/jmbi.1996.0356;
RA   Slijper M., Bonvin A.M., Boelens R., Kaptein R.;
RT   "Refined structure of lac repressor headpiece (1-56) determined by
RT   relaxation matrix calculations from 2D and 3D NOE data: change of
RT   tertiary structure upon binding to the lac operator.";
RL   J. Mol. Biol. 259:761-773(1996).
RN   [19]
RP   STRUCTURE BY NMR OF 1-62.
RX   MEDLINE=20113476; PubMed=10647179; DOI=10.1016/S0969-2126(00)88339-2;
RA   Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R.,
RA   Kaptein R.;
RT   "The solution structure of Lac repressor headpiece 62 complexed to a
RT   symmetrical lac operator.";
RL   Structure 7:1483-1492(1999).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
RX   MEDLINE=96239623; PubMed=8638105;
RA   Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C.,
RA   Schumacher M.A., Brennan R.G., Lu P.;
RT   "Crystal structure of the lactose operon repressor and its complexes
RT   with DNA and inducer.";
RL   Science 271:1247-1254(1996).
CC   -!- FUNCTION: Repressor of the lactose operon. Binds allolactose as an
CC       inducer.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P00722:lacZ; NbExp=1; IntAct=EBI-909231, EBI-369998;
CC   -!- MISCELLANEOUS: Removing residues 1-59 results in loss of DNA-
CC       binding activity but retains tetrameric structure and inducer-
CC       binding activity. Deleting residues 340-360 results in loss of
CC       tetramer formation, but retains dimer formation, inducer-binding
CC       activity, and DNA-binding activity (if residues 1-59 are present).
CC   -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; V00294; CAA23569.1; -; Genomic_DNA.
DR   EMBL; X58469; CAA41383.1; -; Genomic_DNA.
DR   EMBL; U86347; AAB47270.1; ALT_INIT; Genomic_DNA.
DR   EMBL; J01636; AAA24052.1; -; Genomic_DNA.
DR   EMBL; U72488; AAB36549.1; -; Genomic_DNA.
DR   EMBL; U78872; AAB37348.1; -; Genomic_DNA.
DR   EMBL; U78873; AAB37351.1; -; Genomic_DNA.
DR   EMBL; U78874; AAB37354.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18069.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73448.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76127.1; -; Genomic_DNA.
DR   PIR; A93198; RPECL.
DR   PDB; 1CJG; NMR; A/B=1-62.
DR   PDB; 1EFA; X-ray; A/B/C=1-333.
DR   PDB; 1JWL; X-ray; A/B/C=1-333.
DR   PDB; 1JYE; X-ray; A=1-349.
DR   PDB; 1JYF; X-ray; A=1-349.
DR   PDB; 1L1M; NMR; A/B=1-62.
DR   PDB; 1LBG; X-ray; A/B/C/D=1-360.
DR   PDB; 1LBH; X-ray; A/B/C/D=1-360.
DR   PDB; 1LBI; X-ray; A/B/C/D=1-360.
DR   PDB; 1LCC; NMR; A=1-51.
DR   PDB; 1LCD; NMR; A=1-51.
DR   PDB; 1LQC; NMR; @=1-56.
DR   PDB; 1LTP; Model; L=62-323.
DR   PDB; 1TLF; X-ray; A/B/C/D=60-360.
DR   PDB; 2BJC; NMR; A/B=1-62.
DR   DIP; DIP:10079N; -.
DR   IntAct; P03023; -.
DR   ECO2DBASE; H039.0; 6TH EDITION.
DR   GenomeReviews; U00096_GR; b0345.
DR   GenomeReviews; AP009048_GR; JW0336.
DR   KEGG; ecj:JW0336; -.
DR   KEGG; eco:b0345; -.
DR   EchoBASE; EB0520; -.
DR   EcoGene; EG10525; lacI.
DR   BioCyc; EcoCyc:PD00763; -.
DR   LinkHub; P03023; -.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR010982; Lambda_DNA_bd.
DR   InterPro; IPR001761; Peripla_BP_Lac1.
DR   Pfam; PF00356; LacI; 1.
DR   Pfam; PF00532; Peripla_BP_1; 1.
DR   PRINTS; PR00036; HTHLACI.
DR   SMART; SM00354; HTH_LACI; 1.
DR   PROSITE; PS00356; HTH_LACI_1; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    360       Lactose operon repressor.
FT                                /FTId=PRO_0000107963.
FT   DOMAIN        1     58       HTH lacI-type.
FT   DNA_BIND      6     25       H-T-H motif.
FT   VARIANT     282    282       Y -> D (in T41 mutant).
FT   MUTAGEN      17     17       Y->H: Broadening of specificity.
FT   MUTAGEN      22     22       R->N: Recognizes an operator variant.
FT   CONFLICT    286    286       L -> S (in Ref. 1, 4 and 7).
FT   STRAND       63     69
FT   HELIX        74     89
FT   STRAND       93     98
FT   STRAND      101    103
FT   HELIX       104    115
FT   TURN        116    118
FT   STRAND      122    126
FT   HELIX       130    139
FT   TURN        140    142
FT   STRAND      145    150
FT   STRAND      154    156
FT   STRAND      158    161
FT   HELIX       163    177
FT   STRAND      181    186
FT   HELIX       192    207
FT   STRAND      213    217
FT   HELIX       222    234
FT   STRAND      240    246
FT   HELIX       247    259
FT   TURN        265    267
FT   STRAND      268    271
FT   HELIX       277    281
FT   STRAND      282    284
FT   STRAND      287    290
FT   HELIX       293    308
FT   STRAND      314    319
FT   STRAND      322    324
FT   HELIX       354    356
SQ   SEQUENCE   360 AA;  38590 MW;  347A8DEE92D736CB CRC64;
     MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ
     SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS
     GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ
     QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT
     AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS
     VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ
//
ID   LACY_ECOLI              Reviewed;         417 AA.
AC   P02920; Q2MC81;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-MAR-2007, entry version 78.
DE   Lactose permease (Lactose-proton symport).
GN   Name=lacY; OrderedLocusNames=b0343, JW0334;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Pastore J.C., Larigan J.D., Consler T.G., Kaback H.R.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   TOPOLOGY.
RX   PubMed=16453726;
RA   von Heijne G.;
RT   "The distribution of positively charged residues in bacterial inner
RT   membrane proteins correlates with the trans-membrane topology.";
RL   EMBO J. 5:3021-3027(1986).
RN   [7]
RP   TOPOLOGY.
RX   MEDLINE=90311318; PubMed=2164211;
RA   Calamia J., Manoil C.;
RT   "lac permease of Escherichia coli: topology and sequence elements
RT   promoting membrane insertion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4937-4941(1990).
RN   [8]
RP   TOPOLOGY.
RX   MEDLINE=96066665; PubMed=7578103; DOI=10.1021/bi00045a036;
RA   Ujwal M.L., Jung H., Bibi E., Manoil C., Altenbach C., Hubbell W.L.,
RA   Kaback H.R.;
RT   "Membrane topology of helices VII and XI in the lactose permease of
RT   Escherichia coli studied by lacY-phoA fusion analysis and site-
RT   directed spectroscopy.";
RL   Biochemistry 34:14909-14917(1995).
RN   [9]
RP   MUTAGENESIS.
RX   MEDLINE=91167519; PubMed=1848449; DOI=10.1016/0005-2736(91)90390-T;
RA   King S.C., Hansen C.L., Wilson T.H.;
RT   "The interaction between aspartic acid 237 and lysine 358 in the
RT   lactose carrier of Escherichia coli.";
RL   Biochim. Biophys. Acta 1062:177-186(1991).
RN   [10]
RP   MUTAGENESIS.
RX   MEDLINE=92355521; PubMed=1644770;
RA   Huang A.-M., Lee J.-I., King S.C., Wilson T.H.;
RT   "Amino acid substitution in the lactose carrier protein with the use
RT   of amber suppressors.";
RL   J. Bacteriol. 174:5436-5441(1992).
RN   [11]
RP   REVIEW.
RX   MEDLINE=90366577; PubMed=2203471; DOI=10.1016/0005-2728(90)90239-Z;
RA   Kaback H.R.;
RT   "The lac permease of Escherichia coli: a prototypic energy-transducing
RT   membrane protein.";
RL   Biochim. Biophys. Acta 1018:160-162(1990).
RN   [12]
RP   MASS SPECTROMETRY OF FORMYLATED FORM.
RX   MEDLINE=99415921; PubMed=10485888; DOI=10.1073/pnas.96.19.10695;
RA   Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G.,
RA   Faull K.F., Kaback H.R.;
RT   "Toward the bilayer proteome, electrospray ionization-mass
RT   spectrometry of large, intact transmembrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10695-10698(1999).
RN   [13]
RP   TOPOLOGY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF MUTANT GLY-154.
RX   MEDLINE=22776143; PubMed=12893935; DOI=10.1126/science.1088196;
RA   Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., Iwata S.;
RT   "Structure and mechanism of the lactose permease of Escherichia
RT   coli.";
RL   Science 301:610-615(2003).
CC   -!- FUNCTION: Responsible for transport of beta-galactosides into the
CC       cell, with the concomitant import of a proton (symport system).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; multi-pass membrane
CC       protein.
CC   -!- MASS SPECTROMETRY: MW=47357; METHOD=Electrospray; RANGE=1-417;
CC       NOTE=Ref.12.
CC   -!- SIMILARITY: Belongs to the lacY/rafB permease family.
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DR   EMBL; J01636; AAA24054.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23571.1; -; Genomic_DNA.
DR   EMBL; X56095; CAA39575.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18067.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73446.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76125.1; -; Genomic_DNA.
DR   PIR; A03418; GREC.
DR   PDB; 1M2U; Model; A=1-417.
DR   PDB; 1PV6; X-ray; A/B=1-417.
DR   PDB; 1PV7; X-ray; A/B=1-417.
DR   PDB; 2CFP; X-ray; A=1-417.
DR   PDB; 2CFQ; X-ray; A=1-417.
DR   DIP; DIP:10080N; -.
DR   GenomeReviews; U00096_GR; b0343.
DR   GenomeReviews; AP009048_GR; JW0334.
DR   KEGG; ecj:JW0334; -.
DR   KEGG; eco:b0343; -.
DR   EchoBASE; EB0521; -.
DR   EcoGene; EG10526; lacY.
DR   BioCyc; EcoCyc:LACY-MONOMER; -.
DR   LinkHub; P02920; -.
DR   InterPro; IPR000576; LacY_symport.
DR   InterPro; IPR007114; MFS.
DR   Pfam; PF01306; LacY_symp; 1.
DR   PRINTS; PR00174; LACYSMPORT.
DR   TIGRFAMs; TIGR00882; 2A0105; 1.
DR   PROSITE; PS00896; LACY_1; 1.
DR   PROSITE; PS00897; LACY_2; 1.
DR   PROSITE; PS50850; MFS; 1.
KW   3D-structure; Complete proteome; Formylation; Inner membrane;
KW   Membrane; Sugar transport; Symport; Transmembrane; Transport.
FT   CHAIN         1    417       Lactose permease.
FT                                /FTId=PRO_0000196184.
FT   TOPO_DOM      1      7       Cytoplasmic.
FT   TRANSMEM      8     34       1.
FT   TOPO_DOM     35     41       Periplasmic.
FT   TRANSMEM     42     70       2.
FT   TOPO_DOM     71     74       Cytoplasmic.
FT   TRANSMEM     75    100       3.
FT   TOPO_DOM    101    104       Periplasmic.
FT   TRANSMEM    105    129       4.
FT   TOPO_DOM    130    140       Cytoplasmic.
FT   TRANSMEM    141    163       5.
FT   TOPO_DOM    164    166       Periplasmic.
FT   TRANSMEM    167    186       6.
FT   TOPO_DOM    187    220       Cytoplasmic.
FT   TRANSMEM    221    249       7.
FT   TOPO_DOM    250    253       Periplasmic.
FT   TRANSMEM    254    278       8.
FT   TOPO_DOM    279    288       Cytoplasmic.
FT   TRANSMEM    289    308       9.
FT   TOPO_DOM    309    311       Periplasmic.
FT   TRANSMEM    312    334       10.
FT   TOPO_DOM    335    346       Cytoplasmic.
FT   TRANSMEM    347    374       11.
FT   TOPO_DOM    375    377       Periplasmic.
FT   TRANSMEM    378    398       12.
FT   TOPO_DOM    399    417       Cytoplasmic.
FT   SITE        126    126       Substrate binding.
FT   SITE        144    144       Substrate binding.
FT   SITE        269    269       Substrate binding and proton
FT                                translocation.
FT   SITE        302    302       Proton translocation.
FT   SITE        322    322       Proton translocation.
FT   SITE        325    325       Proton translocation.
FT   MOD_RES       1      1       N-formylmethionine; partial.
FT   MUTAGEN     237    237       D->N,G: Defect in melibiose transport.
FT   MUTAGEN     358    358       K->T: Defect in melibiose transport.
FT   TURN          2      4
FT   HELIX         8     12
FT   TURN         13     16
FT   HELIX        17     23
FT   TURN         24     28
FT   HELIX        31     38
FT   HELIX        42     54
FT   TURN         55     57
FT   HELIX        60     67
FT   HELIX        68     70
FT   HELIX        76     79
FT   TURN         80     83
FT   STRAND       84     87
FT   HELIX        88     93
FT   HELIX        96     99
FT   TURN        100    102
FT   HELIX       105    109
FT   TURN        114    120
FT   HELIX       121    135
FT   HELIX       140    142
FT   HELIX       144    164
FT   HELIX       168    171
FT   HELIX       173    177
FT   HELIX       178    183
FT   STRAND      201    203
FT   HELIX       210    216
FT   HELIX       220    231
FT   TURN        232    235
FT   HELIX       236    242
FT   HELIX       245    249
FT   STRAND      251    254
FT   HELIX       257    267
FT   HELIX       270    276
FT   HELIX       279    286
FT   HELIX       289    307
FT   HELIX       312    320
FT   HELIX       322    324
FT   HELIX       326    340
FT   TURN        343    345
FT   HELIX       346    349
FT   HELIX       351    356
FT   HELIX       357    399
FT   STRAND      408    411
FT   TURN        414    416
SQ   SEQUENCE   417 AA;  46503 MW;  24A8062F628CDA32 CRC64;
     MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA AISLFSLLFQ
     PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ YNILVGSIVG GIYLGFCFNA
     GAPAVEAFIE KVSRRSNFEF GRARMFGCVG WALCASIVGI MFTINNQFVF WLGSGCALIL
     AVLLFFAKTD APSSATVANA VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD
     QQFANFFTSF FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS
     VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY LVCFCFFKQL
     AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL SGPGPLSLLR RQVNEVA
//
ID   BGAL_ECOLI              Reviewed;        1024 AA.
AC   P00722; Q2MC80;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 83.
DE   Beta-galactosidase (EC 3.2.1.23) (Lactase).
GN   Name=lacZ; OrderedLocusNames=b0344, JW0335;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84028567; PubMed=6313347;
RA   Kalnins A., Otto K., Ruether U., Mueller-Hill B.;
RT   "Sequence of the lacZ gene of Escherichia coli.";
RL   EMBO J. 2:593-597(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-1024.
RX   MEDLINE=78218239; PubMed=97298;
RA   Fowler A.V., Zabin I.;
RT   "Amino acid sequence of beta-galactosidase. XI. Peptide ordering
RT   procedures and the complete sequence.";
RL   J. Biol. Chem. 253:5521-5525(1978).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476.
RX   MEDLINE=80188189; PubMed=6246435; DOI=10.1038/285038a0;
RA   Calos M.P., Miller J.H.;
RT   "Molecular consequences of deletion formation mediated by the
RT   transposon Tn9.";
RL   Nature 285:38-41(1980).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024.
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [8]
RP   ACTIVE SITE REGIONS.
RX   MEDLINE=83290932; PubMed=6411710;
RA   Fowler A.V., Smith P.J.;
RT   "The active site regions of lacZ and ebg beta-galactosidases are
RT   homologous.";
RL   J. Biol. Chem. 258:10204-10207(1983).
RN   [9]
RP   ACTIVE SITE GLU-462.
RX   MEDLINE=84108409; PubMed=6420154;
RA   Herrchen M., Legler G.;
RT   "Identification of an essential carboxylate group at the active site
RT   of lacZ beta-galactosidase from Escherichia coli.";
RL   Eur. J. Biochem. 138:527-531(1984).
RN   [10]
RP   ACTIVE SITE GLU-538.
RX   MEDLINE=92283812; PubMed=1350782;
RA   Gebler J.C., Aebersold R., Withers S.G.;
RT   "Glu-537, not Glu-461, is the nucleophile in the active site of (lac
RT   Z) beta-galactosidase from Escherichia coli.";
RL   J. Biol. Chem. 267:11126-11130(1992).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   MEDLINE=94277211; PubMed=8008071; DOI=10.1038/369761a0;
RA   Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.;
RT   "Three-dimensional structure of beta-galactosidase from E. coli.";
RL   Nature 369:761-766(1994).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=21590184; PubMed=11732897; DOI=10.1021/bi011727i;
RA   Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L.,
RA   Withers S.G., Matthews B.W.;
RT   "A structural view of the action of Escherichia coli (lacZ) beta-
RT   galactosidase.";
RL   Biochemistry 40:14781-14794(2001).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P03023:lacI; NbExp=1; IntAct=EBI-369998, EBI-909231;
CC       P0ACA1:yibF; NbExp=1; IntAct=EBI-369998, EBI-1133142;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC   -!- WEB RESOURCE: NAME=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/BG/".
CC   -!- WEB RESOURCE: NAME=ProZyme technical fact sheet;
CC       URL="http://www.prozyme.com/pdf/bg11.pdf".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J01636; AAA24053.1; -; Genomic_DNA.
DR   EMBL; V00296; CAA23573.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18068.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73447.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76126.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23570.1; -; Genomic_DNA.
DR   PIR; A90981; GBEC.
DR   PDB; 1BGL; X-ray; A/B/C/D/E/F/G/H=1-1024.
DR   PDB; 1BGM; X-ray; I/J/K/L/M/N/O/P=-.
DR   PDB; 1DP0; X-ray; A/B/C/D=10-1024.
DR   PDB; 1F49; X-ray; A/B/C/D/E/F/G/H=1-1024.
DR   PDB; 1F4A; X-ray; A/B/C/D=4-1024.
DR   PDB; 1F4H; X-ray; A/B/C/D=4-1024.
DR   PDB; 1GHO; X-ray; I/J/K/L/M/N/O/P=1-1024.
DR   PDB; 1HN1; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JYN; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JYV; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JYW; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JYX; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JYY; X-ray; A/B/C/D/E/F/G/H=1-1024.
DR   PDB; 1JYZ; X-ray; I/J/K/L/M/N/O/P=1-1024.
DR   PDB; 1JZ0; X-ray; A/B/C/D/E/F/G/H=1-1024.
DR   PDB; 1JZ1; X-ray; I/J/K/L/M/N/O/P=1-1024.
DR   PDB; 1JZ2; X-ray; A/B/C/D=1-1024.
DR   PDB; 1JZ3; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JZ4; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JZ5; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JZ6; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JZ7; X-ray; A/B/C/D=10-1024.
DR   PDB; 1JZ8; X-ray; A/B/C/D=10-1024.
DR   PDB; 1PX3; X-ray; A/B/C/D=10-1024.
DR   PDB; 1PX4; X-ray; A/B/C/D=10-1024.
DR   IntAct; P00722; -.
DR   ECO2DBASE; E123.0; 6TH EDITION.
DR   GenomeReviews; U00096_GR; b0344.
DR   GenomeReviews; AP009048_GR; JW0335.
DR   KEGG; ecj:JW0335; -.
DR   KEGG; eco:b0344; -.
DR   EchoBASE; EB0522; -.
DR   EcoGene; EG10527; lacZ.
DR   BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -.
DR   LinkHub; P00722; -.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR008979; Gal_bd.
DR   InterPro; IPR011013; Gal_mut_like.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_carb-bd.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR004199; Glyco_hydro_42_D5.
DR   InterPro; IPR013781; Glyco_hydro_cat.
DR   Gene3D; G3DSA:2.70.98.10; Glyco_hydro_42_5; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Glycosidase; Hydrolase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   1024       Beta-galactosidase.
FT                                /FTId=PRO_0000057650.
FT   ACT_SITE    462    462       Proton donor.
FT   ACT_SITE    538    538       Nucleophile.
FT   HELIX        15     17
FT   STRAND       22     25
FT   STRAND       36     38
FT   HELIX        39     44
FT   STRAND       51     53
FT   STRAND       56     65
FT   HELIX        66     68
FT   HELIX        72     75
FT   STRAND       82     87
FT   HELIX        90     93
FT   STRAND       99    104
FT   STRAND      120    129
FT   HELIX       131    135
FT   STRAND      136    144
FT   STRAND      146    154
FT   STRAND      157    163
FT   STRAND      169    172
FT   TURN        174    176
FT   STRAND      179    191
FT   HELIX       193    197
FT   STRAND      201    204
FT   STRAND      212    217
FT   STRAND      219    231
FT   STRAND      235    248
FT   STRAND      254    262
FT   STRAND      265    274
FT   STRAND      288    297
FT   STRAND      303    306
FT   STRAND      309    317
FT   STRAND      322    330
FT   STRAND      335    338
FT   STRAND      341    344
FT   STRAND      351    355
FT   TURN        361    363
FT   HELIX       369    381
FT   STRAND      386    388
FT   HELIX       397    405
FT   STRAND      408    412
FT   STRAND      420    422
FT   TURN        423    428
FT   HELIX       430    432
FT   HELIX       433    447
FT   STRAND      453    457
FT   HELIX       466    478
FT   TURN        488    490
FT   STRAND      491    493
FT   STRAND      497    499
FT   STRAND      513    515
FT   HELIX       520    524
FT   STRAND      533    539
FT   HELIX       549    558
FT   STRAND      562    568
FT   STRAND      575    578
FT   STRAND      584    587
FT   TURN        589    592
FT   HELIX       599    602
FT   HELIX       616    623
FT   STRAND      626    632
FT   STRAND      635    640
FT   STRAND      651    658
FT   STRAND      661    669
FT   STRAND      677    681
FT   STRAND      689    702
FT   STRAND      707    709
FT   STRAND      713    725
FT   STRAND      739    742
FT   STRAND      744    751
FT   STRAND      754    759
FT   TURN        760    762
FT   STRAND      764    770
FT   STRAND      776    783
FT   HELIX       790    793
FT   HELIX       806    813
FT   TURN        814    817
FT   STRAND      819    829
FT   STRAND      831    844
FT   STRAND      847    859
FT   STRAND      864    872
FT   STRAND      880    889
FT   STRAND      893    903
FT   STRAND      914    921
FT   HELIX       922    925
FT   STRAND      938    946
FT   STRAND      949    962
FT   HELIX       964    969
FT   HELIX       973    975
FT   STRAND      980    990
FT   STRAND      998   1000
FT   HELIX      1005   1007
FT   STRAND     1012   1021
SQ   SEQUENCE   1024 AA;  116483 MW;  9D295EF4CEF90B08 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
     TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
     LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
     GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//
ID   THGA_ECOLI              Reviewed;         203 AA.
AC   P07464; P77862; Q2MC82;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   20-MAR-2007, entry version 71.
DE   Galactoside O-acetyltransferase (EC 2.3.1.18) (GAT) (Thiogalactoside
DE   acetyltransferase).
GN   Name=lacA; OrderedLocusNames=b0342, JW0333;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=85200082; PubMed=3922433; DOI=10.1016/S0300-9084(85)80235-2;
RA   Fowler A.V., Hediger M.A., Musso R.E., Zabin I.;
RT   "The amino acid sequence of thiogalactoside transacetylase of
RT   Escherichia coli.";
RL   Biochimie 67:101-108(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86016712; PubMed=3901000;
RA   Hediger M.A., Johnson D.F., Nierlich D.P., Zabin I.;
RT   "DNA sequence of the lactose operon: the lacA gene and the
RT   transcriptional termination region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6414-6418(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   MEDLINE=21936195; PubMed=11937062; DOI=10.1016/S0969-2126(02)00741-4;
RA   Wang X.G., Olsen L.R., Roderick S.L.;
RT   "Structure of the lac operon galactoside acetyltransferase.";
RL   Structure 10:581-588(2002).
CC   -!- FUNCTION: May assist cellular detoxification by acetylating non-
CC       metabolizable pyranosides, thereby preventing their reentry into
CC       the cell.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + a beta-D-galactoside = CoA + a 6-
CC       acetyl-beta-D-galactoside.
CC   -!- PATHWAY: Lactose biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus of this protein is heterogeneous because the
CC       initiator methionine is only partially cleaved.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; J01636; AAA24055.1; -; Genomic_DNA.
DR   EMBL; X51872; CAA36162.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18066.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73445.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76124.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23572.1; -; Genomic_DNA.
DR   PIR; A94061; XXECTG.
DR   PDB; 1KQA; X-ray; A/B/C=1-203.
DR   PDB; 1KRR; X-ray; A/B/C=1-203.
DR   PDB; 1KRU; X-ray; A/B/C=1-203.
DR   PDB; 1KRV; X-ray; A/B/C=1-203.
DR   DIP; DIP:10078N; -.
DR   IntAct; P07464; -.
DR   GenomeReviews; U00096_GR; b0342.
DR   GenomeReviews; AP009048_GR; JW0333.
DR   KEGG; ecj:JW0333; -.
DR   KEGG; eco:b0342; -.
DR   EchoBASE; EB0519; -.
DR   EcoGene; EG10524; lacA.
DR   BioCyc; EcoCyc:GALACTOACETYLTRAN-MONOMER; -.
DR   GO; GO:0008870; F:galactoside O-acetyltransferase activity; IEA:EC.
DR   InterPro; IPR001451; Hexapep_transf.
DR   InterPro; IPR011004; Trimer_LpxA_like.
DR   Pfam; PF00132; Hexapep; 3.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
KW   3D-structure; Acyltransferase; Complete proteome;
KW   Direct protein sequencing; Lactose biosynthesis; Repeat; Transferase.
FT   CHAIN         1    203       Galactoside O-acetyltransferase.
FT                                /FTId=PRO_0000068696.
FT   HELIX         5     11
FT   HELIX        22     37
FT   HELIX        44     54
FT   STRAND       55     57
FT   STRAND       68     71
FT   STRAND       76     78
FT   STRAND       88     91
FT   STRAND       96     98
FT   STRAND      109    114
FT   TURN        119    121
FT   STRAND      127    129
FT   STRAND      132    134
FT   STRAND      172    175
FT   TURN        176    179
FT   STRAND      180    184
FT   HELIX       187    189
SQ   SEQUENCE   203 AA;  22799 MW;  31C7FEA0B0150D70 CRC64;
     MNMPMTERIR AGKLFTDMCE GLPEKRLRGK TLMYEFNHSH PSEVEKRESL IKEMFATVGE
     NAWVEPPVYF SYGSNIHIGR NFYANFNLTI VDDYTVTIGD NVLIAPNVTL SVTGHPVHHE
     LRKNGEMYSF PITIGNNVWI GSHVVINPGV TIGDNSVIGA GSIVTKDIPP NVVAAGVPCR
     VIREINDRDK HYYFKDYKVE SSV
//
ID   12S1_ARATH              Reviewed;         472 AA.
AC   P15455; Q9FFH7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   31-OCT-2006, entry version 58.
DE   12S seed storage protein CRA1 precursor [Contains: 12S seed storage
DE   protein CRA1 alpha chain (12S seed storage protein CRA1 acidic chain);
DE   12S seed storage protein CRA1 beta chain (12S seed storage protein
DE   CRA1 basic chain)].
GN   Name=CRA1; OrderedLocusNames=At5g44120; ORFNames=MLN1.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Landsberg erecta;
RA   Pang P.P., Pruitt R.E., Meyerowitz E.M.;
RT   "Molecular cloning, genome organization, expression and evolution of
RT   12S seed storage protein genes of Arabidopsis thaliana.";
RL   Plant Mol. Biol. 11:805-820(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned
RT   P1 clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RX   MEDLINE=94108489; PubMed=8281187;
RX   DOI=10.1046/j.1365-313X.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
RA   Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
RA   Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
RA   de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
RA   Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
CC   -!- FUNCTION: This is a seed storage protein.
CC   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a
CC       basic chain derived from a single precursor and linked by a
CC       disulfide bond.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences;
CC       Name=1;
CC         IsoId=P15455-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins)
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M37247; AAA32777.1; -; Genomic_DNA.
DR   EMBL; X14312; CAA32493.1; -; Genomic_DNA.
DR   EMBL; AB005239; BAB10979.1; -; Genomic_DNA.
DR   EMBL; AY070730; AAL50071.1; -; mRNA.
DR   EMBL; Z17590; CAA79005.1; -; mRNA.
DR   PIR; S08509; S08509.
DR   UniGene; At.20540; -.
DR   HSSP; P04776; 1FXZ.
DR   GenomeReviews; BA000015_GR; AT5G44120.
DR   KEGG; ath:At5g44120; -.
DR   TAIR; At5g44120; -.
DR   ArrayExpress; P15455; -.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR011051; Cupin_RmlC_type.
DR   InterPro; IPR006044; Seedstore11s_pln.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
KW   Alternative splicing; Seed storage protein; Signal; Storage protein.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    282       12S seed storage protein CRA1 alpha chain
FT                                (By similarity).
FT                                /FTId=PRO_0000031999.
FT   CHAIN       283    472       12S seed storage protein CRA1 beta chain
FT                                (By similarity).
FT                                /FTId=PRO_0000032000.
FT   DISULFID    112    289       Interchain (between alpha and beta
FT                                chains) (Potential).
FT   CONFLICT    167    167       E -> Q (in Ref. 1).
FT   CONFLICT    356    356       V -> E (in Ref. 1).
SQ   SEQUENCE   472 AA;  52595 MW;  700B468E4D251994 CRC64;
     MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW
     DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS
     EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH
     QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN
     QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP
     SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE
     AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR
     TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA
//
ID   OPSD_HUMAN              Reviewed;         348 AA.
AC   P08100; Q16414; Q2M249;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   20-MAR-2007, entry version 91.
DE   Rhodopsin (Opsin-2).
GN   Name=RHO; Synonyms=OPN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84272729; PubMed=6589631;
RA   Nathans J., Hogness D.S.;
RT   "Isolation and nucleotide sequence of the gene encoding human
RT   rhodopsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RG   The German cDNA consortium;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
RX   PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5;
RA   Bennett J., Beller B., Sun D., Kariko K.;
RT   "Sequence analysis of the 5.34-kb 5' flanking region of the human
RT   rhodopsin-encoding gene.";
RL   Gene 167:317-320(1995).
RN   [6]
RP   REVIEW ON RP4 VARIANTS.
RX   MEDLINE=94004905; PubMed=8401533;
RA   Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A.,
RA   Bhattacharya S.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 2:249-255(1993).
RN   [7]
RP   VARIANT RP4 HIS-23.
RX   MEDLINE=90136922; PubMed=2137202; DOI=10.1038/343364a0;
RA   Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S.,
RA   Yandell D.W., Sandberg M.A., Berson E.L.;
RT   "A point mutation of the rhodopsin gene in one form of retinitis
RT   pigmentosa.";
RL   Nature 343:364-366(1990).
RN   [8]
RP   VARIANTS RP4.
RX   MEDLINE=91051574; PubMed=2239971;
RA   Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G.,
RA   Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M.,
RA   Watty A., Ludwig M., Schinzel A., Samanns C., Gal A.,
RA   Bhattacharya S.S., Humphries P.;
RT   "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin
RT   proline-->histidine substitution (codon 23) in pedigrees from
RT   Europe.";
RL   Am. J. Hum. Genet. 47:941-945(1990).
RN   [9]
RP   VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347.
RX   MEDLINE=91015273; PubMed=2215617;
RA   Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E.,
RA   Reichel E., Sandberg M.A., Berson E.L.;
RT   "Mutations within the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   N. Engl. J. Med. 323:1302-1307(1990).
RN   [10]
RP   VARIANT RP4 ILE-255 DEL.
RX   MEDLINE=91090106; PubMed=1985460;
RA   Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C.,
RA   Bhattacharya S.S.;
RT   "A 3-bp deletion in the rhodopsin gene in a family with autosomal
RT   dominant retinitis pigmentosa.";
RL   Am. J. Hum. Genet. 48:26-30(1991).
RN   [11]
RP   VARIANT RP4 ARG-347.
RX   MEDLINE=92120672; PubMed=1840561;
RA   Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E.,
RA   Schinzel A.;
RT   "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant
RT   retinitis pigmentosa.";
RL   Genomics 11:468-470(1991).
RN   [12]
RP   VARIANTS RP4.
RX   MEDLINE=91319709; PubMed=1862076;
RA   Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H.,
RA   Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G.,
RA   Gouras P., Nathans J.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991).
RN   [13]
RP   VARIANTS RP4.
RX   MEDLINE=92021049; PubMed=1833777;
RA   Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.;
RT   "Mutation spectrum of the rhodopsin gene among patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991).
RN   [14]
RP   VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
RX   MEDLINE=91377732; PubMed=1897520;
RA   Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.;
RT   "Identification of novel rhodopsin mutations associated with retinitis
RT   pigmentosa by GC-clamped denaturing gradient gel electrophoresis.";
RL   Am. J. Hum. Genet. 49:699-706(1991).
RN   [15]
RP   VARIANT RP4 ARG-207.
RX   MEDLINE=93258325; PubMed=1302614; DOI=10.1093/hmg/1.9.769;
RA   Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M.,
RA   Sharpe E., Humphries P.;
RT   "Autosomal dominant retinitis pigmentosa: a novel mutation in the
RT   rhodopsin gene in the original 3q linked family.";
RL   Hum. Mol. Genet. 1:769-771(1992).
RN   [16]
RP   VARIANTS RP4 MET-17 AND LEU-347.
RX   MEDLINE=93004784; PubMed=1391967;
RA   Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M.,
RA   Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A.,
RA   Kanai A.;
RT   "Point mutations of rhodopsin gene found in Japanese families with
RT   autosomal dominant retinitis pigmentosa (ADRP).";
RL   Jpn. J. Hum. Genet. 37:125-132(1992).
RN   [17]
RP   VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND
RP   VARIANTS ALA-51; ILE-104 AND MET-209.
RX   MEDLINE=93304432; PubMed=8317502;
RA   Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C.,
RA   Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R.,
RA   Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.;
RT   "Identification of novel rhodopsin mutations responsible for retinitis
RT   pigmentosa: implications for the structure and function of
RT   rhodopsin.";
RL   Am. J. Hum. Genet. 53:80-89(1993).
RN   [18]
RP   VARIANT RP4 SER-15.
RX   MEDLINE=93357759; PubMed=8353500; DOI=10.1093/hmg/2.6.813;
RA   Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P.,
RA   Duvigneau C., Gal A.;
RT   "Autosomal dominant 'sector' retinitis pigmentosa due to a point
RT   mutation predicting an Asn-15-Ser substitution of rhodopsin.";
RL   Hum. Mol. Genet. 2:813-814(1993).
RN   [19]
RP   VARIANT CSNBAD1 GLU-292.
RX   MEDLINE=93364423; PubMed=8358437; DOI=10.1038/ng0793-280;
RA   Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.;
RT   "Heterozygous missense mutation in the rhodopsin gene as a cause of
RT   congenital stationary night blindness.";
RL   Nat. Genet. 4:280-283(1993).
RN   [20]
RP   VARIANTS RP4.
RX   MEDLINE=94375083; PubMed=8088850; DOI=10.1006/geno.1994.1301;
RA   Vaithinathan R., Berson E.L., Dryja T.P.;
RT   "Further screening of the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   Genomics 21:461-463(1994).
RN   [21]
RP   VARIANT RP4 THR-44.
RX   MEDLINE=94357587; PubMed=8076945; DOI=10.1007/BF00208284;
RA   Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C.,
RA   Carballo M.;
RT   "Identification of a novel rhodopsin mutation (Met-44-Thr) in a
RT   simplex case of retinitis pigmentosa.";
RL   Hum. Genet. 94:283-286(1994).
RN   [22]
RP   VARIANTS RP4 PHE-110; PRO-131 AND VAL-164.
RX   MEDLINE=95072600; PubMed=7981701; DOI=10.1093/hmg/3.7.1203;
RA   Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S.,
RA   Humphries P., Gal A.;
RT   "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1203-1203(1994).
RN   [23]
RP   VARIANT RP4 GLN-171.
RX   MEDLINE=95078852; PubMed=7987326; DOI=10.1093/hmg/3.8.1421;
RA   Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P.,
RA   Cabeza J.C.;
RT   "Identification of a new mutation at codon 171 of rhodopsin gene
RT   causing autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1421-1421(1994).
RN   [24]
RP   VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
RX   MEDLINE=95078858; PubMed=7987331; DOI=10.1093/hmg/3.8.1433;
RA   Souied E., Gerber S., Rozet J.M., Bonneau D., Dufier J.-L., Ghazi I.,
RA   Philip N., Soubrane G., Coscas G., Munnich A.;
RT   "Five novel missense mutations of the rhodopsin gene in autosomal
RT   dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1433-1434(1994).
RN   [25]
RP   VARIANTS RP4 ARG-40 AND LYS-216.
RX   MEDLINE=94362717; PubMed=8081400;
RA   Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A.,
RA   Bhattacharya S.;
RT   "Two new rhodopsin transversion mutations (L40R; M216K) in families
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 3:409-410(1994).
RN   [26]
RP   VARIANT RP4 LEU-345.
RX   MEDLINE=94321123; PubMed=8045708;
RA   Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.;
RT   "Autosomal dominant retinitis pigmentosa in a large family: a clinical
RT   and molecular genetic study.";
RL   Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994).
RN   [27]
RP   VARIANT ARRP LYS-150.
RX   MEDLINE=95078913; PubMed=7987385; DOI=10.1038/ng0994-10;
RA   Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R.,
RA   Orth U., Oehlmann R., Gal A.;
RT   "Missense rhodopsin mutation in a family with recessive RP.";
RL   Nat. Genet. 8:10-11(1994).
RN   [28]
RP   VARIANT RP4 ALA-347.
RX   MEDLINE=95359993; PubMed=7633434; DOI=10.1093/hmg/4.4.775;
RA   Macke J.P., Hennessey J.C., Nathans J.;
RT   "Rhodopsin mutation proline347-to-alanine in a family with autosomal
RT   dominant retinitis pigmentosa indicates an important role for proline
RT   at position 347.";
RL   Hum. Mol. Genet. 4:775-776(1995).
RN   [29]
RP   VARIANT CSNBAD1 ASP-90.
RX   MEDLINE=95148641; PubMed=7846071;
RA   Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K.,
RA   Alpern M.;
RT   "Dark-light: model for nightblindness from the human rhodopsin Gly-
RT   90-->Asp mutation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995).
RN   [30]
RP   VARIANT RP4 TRP-135.
RX   MEDLINE=96142043; PubMed=8554077;
RA   Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S.,
RA   Munnich A., Kaplan J.;
RT   "Retinitis punctata albescens associated with the Arg135Trp mutation
RT   in the rhodopsin gene.";
RL   Am. J. Ophthalmol. 121:19-25(1996).
RN   [31]
RP   VARIANT RP4 ARG-109.
RX   MEDLINE=98112414; PubMed=9452035;
RA   Goliath R., Bardien S., September A., Martin R., Ramesar R.,
RA   Greenberg J.;
RT   "Rhodopsin mutation G109R in a family with autosomal dominant
RT   retinitis pigmentosa.";
RL   Hum. Mutat. Suppl. 1:S40-S41(1998).
RN   [32]
RP   VARIANT CSNBAD1 ILE-94.
RX   MEDLINE=99103467; PubMed=9888392;
RX   DOI=10.1002/(SICI)1098-1004(1999)13:1<75::AID-HUMU9>3.0.CO;2-4;
RA   Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N.,
RA   Findlay J.B.C., Humphries P., Kenna P.F.;
RT   "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing
RT   autosomal dominant congenital stationary night blindness.";
RL   Hum. Mutat. 13:75-81(1999).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=495 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC       vision in dim light.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- DISEASE: Defects in RHO are the cause of retinitis pigmentosa 4
CC       (RP4) [MIM:180380]; a form of autosomal dominant retinitis
CC       pigmentosa. Retinitis pigmentosa (RP) [MIM:268000] leads to
CC       degeneration of retinal photoreceptor cells. Patients typically
CC       have night vision blindness and loss of midperipheral visual
CC       field. As their condition progresses, they lose their far
CC       peripheral visual field and eventually central vision as well.
CC   -!- DISEASE: Defects in RHO are a cause of autosomal recessive
CC       retinitis pigmentosa (ARRP) [MIM:268000].
CC   -!- DISEASE: Defects in RHO are a cause of autosomal dominant
CC       congenital stationary night blindness 1 (CSNBAD1) [MIM:610445];
CC       also known as rhodopsin-related congenital stationary night
CC       blindness. Congenital stationary night blindness is a
CC       nonprogressive retinal disorder characterized by impaired night
CC       vision and ocular symptoms such as myopia, hyperopia, nystagmus
CC       and reduced visual acuity.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -!- WEB RESOURCE: NAME=RHO; NOTE=Rhodopsin mutations page;
CC       URL="http://mol.ophth.uiowa.edu/MOL_WWW/Rhotab.html".
CC   -!- WEB RESOURCE: NAME=Mutations of the RHO gene;
CC       NOTE=Retina International's Scientific Newsletter;
CC       URL="http://www.retina-international.com/sci-news/rhomut.htm".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=RHO".
CC   -----------------------------------------------------------------------
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DR   EMBL; U49742; AAC31763.1; -; Genomic_DNA.
DR   EMBL; AB065668; BAC05894.1; -; Genomic_DNA.
DR   EMBL; BX537381; CAD97623.1; -; mRNA.
DR   EMBL; BC112104; AAI12105.1; -; mRNA.
DR   EMBL; BC112106; AAI12107.1; -; mRNA.
DR   EMBL; U16824; AAA97436.1; -; Genomic_DNA.
DR   EMBL; S81166; AAB35906.1; -; Genomic_DNA.
DR   PIR; A41200; OOHU.
DR   UniGene; Hs.247565; -.
DR   HSSP; P02699; 1EDS.
DR   SMR; P08100; 1-348.
DR   GlycoSuiteDB; P08100; -.
DR   Ensembl; ENSG00000163914; Homo sapiens.
DR   KEGG; hsa:6010; -.
DR   HGNC; HGNC:10012; RHO.
DR   MIM; 180380; gene+phenotype.
DR   MIM; 268000; phenotype.
DR   MIM; 610445; phenotype.
DR   ArrayExpress; P08100; -.
DR   GermOnline; ENSG00000163914; Homo sapiens.
DR   RZPD-ProtExp; RZPDo834D0247; -.
DR   RZPD-ProtExp; T1321; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS:ProtInc.
DR   GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
DR   GO; GO:0016056; P:rhodopsin mediated signaling; TAS:ProtInc.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000732; Rhodopsin.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Acetylation; Chromophore; Disease mutation;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphorylation; Photoreceptor protein; Polymorphism;
KW   Receptor; Retinal protein; Retinitis pigmentosa; Sensory transduction;
KW   Transducer; Transmembrane; Vision.
FT   CHAIN         1    348       Rhodopsin.
FT                                /FTId=PRO_0000197677.
FT   TOPO_DOM      1     36       Extracellular.
FT   TRANSMEM     37     61       1 (Potential).
FT   TOPO_DOM     62     73       Cytoplasmic.
FT   TRANSMEM     74     98       2 (Potential).
FT   TOPO_DOM     99    113       Extracellular.
FT   TRANSMEM    114    133       3 (Potential).
FT   TOPO_DOM    134    152       Cytoplasmic.
FT   TRANSMEM    153    176       4 (Potential).
FT   TOPO_DOM    177    202       Extracellular.
FT   TRANSMEM    203    230       5 (Potential).
FT   TOPO_DOM    231    252       Cytoplasmic.
FT   TRANSMEM    253    276       6 (Potential).
FT   TOPO_DOM    277    284       Extracellular.
FT   TRANSMEM    285    309       7 (Potential).
FT   TOPO_DOM    310    348       Cytoplasmic.
FT   BINDING     296    296       Retinal chromophore (covalent).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   LIPID       322    322       S-palmitoyl cysteine (By similarity).
FT   LIPID       323    323       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    110    187       By similarity.
FT   VARIANT       4      4       T -> K (in RP4).
FT                                /FTId=VAR_004765.
FT   VARIANT      15     15       N -> S (in RP4).
FT                                /FTId=VAR_004766.
FT   VARIANT      17     17       T -> M (in RP4).
FT                                /FTId=VAR_004767.
FT   VARIANT      23     23       P -> H (in RP4; most common variant).
FT                                /FTId=VAR_004768.
FT   VARIANT      23     23       P -> L (in RP4).
FT                                /FTId=VAR_004769.
FT   VARIANT      28     28       Q -> H (in RP4).
FT                                /FTId=VAR_004770.
FT   VARIANT      40     40       L -> R (in RP4).
FT                                /FTId=VAR_004771.
FT   VARIANT      44     44       M -> T (in RP4).
FT                                /FTId=VAR_004772.
FT   VARIANT      45     45       F -> L (in RP4).
FT                                /FTId=VAR_004773.
FT   VARIANT      46     46       L -> R (in RP4).
FT                                /FTId=VAR_004774.
FT   VARIANT      51     51       G -> A (effect not known).
FT                                /FTId=VAR_004775.
FT   VARIANT      51     51       G -> R (in RP4).
FT                                /FTId=VAR_004776.
FT   VARIANT      51     51       G -> V (in RP4).
FT                                /FTId=VAR_004777.
FT   VARIANT      53     53       P -> R (in RP4).
FT                                /FTId=VAR_004778.
FT   VARIANT      58     58       T -> R (in RP4).
FT                                /FTId=VAR_004779.
FT   VARIANT      68     71       Missing (in RP4).
FT                                /FTId=VAR_004780.
FT   VARIANT      87     87       V -> D (in RP4).
FT                                /FTId=VAR_004781.
FT   VARIANT      89     89       G -> D (in RP4).
FT                                /FTId=VAR_004782.
FT   VARIANT      90     90       G -> D (in CSNBAD1).
FT                                /FTId=VAR_004783.
FT   VARIANT      94     94       T -> I (in CSNBAD1).
FT                                /FTId=VAR_004784.
FT   VARIANT     104    104       V -> I.
FT                                /FTId=VAR_004785.
FT   VARIANT     106    106       G -> R (in RP4).
FT                                /FTId=VAR_004786.
FT   VARIANT     106    106       G -> W (in RP4).
FT                                /FTId=VAR_004787.
FT   VARIANT     109    109       G -> R (in RP4).
FT                                /FTId=VAR_004788.
FT   VARIANT     110    110       C -> F (in RP4).
FT                                /FTId=VAR_004789.
FT   VARIANT     110    110       C -> Y (in RP4).
FT                                /FTId=VAR_004790.
FT   VARIANT     114    114       G -> D (in RP4).
FT                                /FTId=VAR_004791.
FT   VARIANT     125    125       L -> R (in RP4).
FT                                /FTId=VAR_004792.
FT   VARIANT     127    127       S -> F (in RP4).
FT                                /FTId=VAR_004793.
FT   VARIANT     131    131       L -> P (in RP4).
FT                                /FTId=VAR_004794.
FT   VARIANT     135    135       R -> G (in RP4).
FT                                /FTId=VAR_004795.
FT   VARIANT     135    135       R -> L (in RP4).
FT                                /FTId=VAR_004796.
FT   VARIANT     135    135       R -> W (in RP4).
FT                                /FTId=VAR_004797.
FT   VARIANT     140    140       C -> S (in RP4).
FT                                /FTId=VAR_004798.
FT   VARIANT     150    150       E -> K (in ARRP).
FT                                /FTId=VAR_004799.
FT   VARIANT     164    164       A -> E (in RP4).
FT                                /FTId=VAR_004800.
FT   VARIANT     164    164       A -> V (in RP4).
FT                                /FTId=VAR_004801.
FT   VARIANT     167    167       C -> R (in RP4).
FT                                /FTId=VAR_004802.
FT   VARIANT     171    171       P -> L (in RP4).
FT                                /FTId=VAR_004803.
FT   VARIANT     171    171       P -> Q (in RP4).
FT                                /FTId=VAR_004804.
FT   VARIANT     171    171       P -> S (in RP4).
FT                                /FTId=VAR_004805.
FT   VARIANT     178    178       Y -> C (in RP4).
FT                                /FTId=VAR_004806.
FT   VARIANT     178    178       Y -> N (in RP4).
FT                                /FTId=VAR_004807.
FT   VARIANT     181    181       E -> K (in RP4).
FT                                /FTId=VAR_004808.
FT   VARIANT     182    182       G -> S (in RP4).
FT                                /FTId=VAR_004809.
FT   VARIANT     186    186       S -> P (in RP4).
FT                                /FTId=VAR_004810.
FT   VARIANT     188    188       G -> E (in RP4).
FT                                /FTId=VAR_004811.
FT   VARIANT     188    188       G -> R (in RP4).
FT                                /FTId=VAR_004812.
FT   VARIANT     190    190       D -> G (in RP4).
FT                                /FTId=VAR_004814.
FT   VARIANT     190    190       D -> N (in RP4).
FT                                /FTId=VAR_004813.
FT   VARIANT     190    190       D -> Y (in RP4).
FT                                /FTId=VAR_004815.
FT   VARIANT     207    207       M -> R (in RP4).
FT                                /FTId=VAR_004816.
FT   VARIANT     209    209       V -> M (effect not known).
FT                                /FTId=VAR_004817.
FT   VARIANT     211    211       H -> P (in RP4).
FT                                /FTId=VAR_004818.
FT   VARIANT     211    211       H -> R (in RP4).
FT                                /FTId=VAR_004819.
FT   VARIANT     216    216       M -> K (in RP4).
FT                                /FTId=VAR_004820.
FT   VARIANT     220    220       F -> C (in RP4).
FT                                /FTId=VAR_004821.
FT   VARIANT     222    222       C -> R (in RP4).
FT                                /FTId=VAR_004822.
FT   VARIANT     255    255       Missing (in RP4).
FT                                /FTId=VAR_004823.
FT   VARIANT     264    264       Missing (in RP4).
FT                                /FTId=VAR_004824.
FT   VARIANT     267    267       P -> L (in RP4).
FT                                /FTId=VAR_004825.
FT   VARIANT     267    267       P -> R (in RP4).
FT                                /FTId=VAR_004826.
FT   VARIANT     292    292       A -> E (in CSNBAD1).
FT                                /FTId=VAR_004827.
FT   VARIANT     296    296       K -> E (in RP4).
FT                                /FTId=VAR_004828.
FT   VARIANT     297    297       S -> R (in RP4).
FT                                /FTId=VAR_004829.
FT   VARIANT     342    342       T -> M (in RP4).
FT                                /FTId=VAR_004830.
FT   VARIANT     345    345       V -> L (in RP4).
FT                                /FTId=VAR_004831.
FT   VARIANT     345    345       V -> M (in RP4).
FT                                /FTId=VAR_004832.
FT   VARIANT     347    347       P -> A (in RP4).
FT                                /FTId=VAR_004833.
FT   VARIANT     347    347       P -> L (in RP4; common variant).
FT                                /FTId=VAR_004834.
FT   VARIANT     347    347       P -> Q (in RP4).
FT                                /FTId=VAR_004835.
FT   VARIANT     347    347       P -> R (in RP4).
FT                                /FTId=VAR_004836.
FT   VARIANT     347    347       P -> S (in RP4).
FT                                /FTId=VAR_004837.
SQ   SEQUENCE   348 AA;  38893 MW;  6F4F6FCBA34265B2 CRC64;
     MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
     VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
     GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
     EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
     ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
     YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
//
ID   AMIC_PSEAE              Reviewed;         385 AA.
AC   P27017;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   20-MAR-2007, entry version 50.
DE   Aliphatic amidase expression-regulating protein.
GN   Name=amiC; OrderedLocusNames=PA3364;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=PAC;
RX   MEDLINE=91317707; PubMed=1907262;
RA   Wilson S.A., Drew R.E.;
RT   "Cloning and DNA sequence of amiC, a new gene regulating expression of
RT   the Pseudomonas aeruginosa aliphatic amidase, and purification of the
RT   amiC product.";
RL   J. Bacteriol. 173:4914-4921(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   CRYSTALLIZATION.
RX   MEDLINE=92106343; PubMed=1762155; DOI=10.1016/0022-2836(91)90579-U;
RA   Wilson S.A., Chayen N.E., Hemmings A.M., Drew R.E., Pearl L.H.;
RT   "Crystallization of and preliminary X-ray data for the negative
RT   regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa.";
RL   J. Mol. Biol. 222:869-871(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 27-28.
RX   MEDLINE=95112789; PubMed=7813419;
RA   Pearl L.H., O'Hara B.P., Drew R.E., Wilson S.A.;
RT   "Crystal structure of AmiC: the controller of transcription
RT   antitermination in the amidase operon of Pseudomonas aeruginosa.";
RL   EMBO J. 13:5810-5817(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIR.
RC   STRAIN=PAC1;
RX   MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175;
RA   O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E.,
RA   Pearl L.H.;
RT   "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-
RT   regulated transcription antitermination complex.";
RL   EMBO J. 18:5175-5186(1999).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC   STRAIN=PAC1;
RX   MEDLINE=20175740; PubMed=10708652; DOI=10.1093/protein/13.2.129;
RA   O'Hara B.P., Wilson S.A., Lee A.W., Roe S.M., Siligardi G., Drew R.E.,
RA   Pearl L.H.;
RT   "Structural adaptation to selective pressure for altered ligand
RT   specificity in the Pseudomonas aeruginosa amide receptor, AmiC.";
RL   Protein Eng. 13:129-132(2000).
CC   -!- FUNCTION: Negatively regulates the expression of the aliphatic
CC       amidase operon. AmiC functions by inhibiting the action of amiR at
CC       the protein level. It exhibits protein kinase activity.
CC   -!- SUBUNIT: Homodimer. Forms a complex with amiR.
CC   -!- DOMAIN: Consists of two beta-alpha-beta domains with a central
CC       cleft in which the amide binds.
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DR   EMBL; X13776; CAA32024.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06752.1; -; Genomic_DNA.
DR   PIR; C83226; C83226.
DR   PDB; 1PEA; X-ray; @=1-385.
DR   PDB; 1QNL; X-ray; A=1-385.
DR   PDB; 1QO0; X-ray; A/B=1-385.
DR   IntAct; P27017; -.
DR   GenomeReviews; AE004091_GR; PA3364.
DR   KEGG; pae:PA3364; -.
DR   BioCyc; PAER287:PA3364-MONOMER; -.
DR   LinkHub; P27017; -.
DR   InterPro; IPR000709; Leu_Ile_Val_bd.
DR   PRINTS; PR00337; LEUILEVALBP.
KW   3D-structure; Complete proteome; Direct protein sequencing; Kinase;
KW   Repressor; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    385       Aliphatic amidase expression-regulating
FT                                protein.
FT                                /FTId=PRO_0000064581.
FT   VARIANT     106    106       T -> N (in strain: PAC181; butyramide
FT                                inducible phenotype).
FT   CONFLICT     27     28       QR -> HA (in Ref. 1).
FT   CONFLICT    186    186       V -> L (in Ref. 1).
FT   CONFLICT    263    263       A -> P (in Ref. 1).
FT   CONFLICT    305    305       S -> N (in Ref. 1).
FT   CONFLICT    319    319       C -> D (in Ref. 1).
FT   CONFLICT    383    383       A -> P (in Ref. 1).
FT   STRAND        8     12
FT   STRAND       15     17
FT   HELIX        20     38
FT   TURN         39     42
FT   STRAND       49     53
FT   HELIX        59     71
FT   STRAND       77     80
FT   HELIX        84     96
FT   STRAND      100    103
FT   STRAND      116    118
FT   HELIX       123    125
FT   HELIX       127    135
FT   TURN        136    138
FT   STRAND      140    149
FT   HELIX       150    165
FT   STRAND      169    176
FT   HELIX       182    195
FT   STRAND      198    203
FT   HELIX       208    220
FT   STRAND      228    232
FT   HELIX       235    238
FT   HELIX       243    246
FT   STRAND      250    254
FT   HELIX       262    272
FT   HELIX       283    302
FT   HELIX       307    314
FT   STRAND      319    321
FT   STRAND      324    328
FT   TURN        330    332
FT   STRAND      335    337
FT   STRAND      340    344
FT   STRAND      350    355
FT   HELIX       368    370
SQ   SEQUENCE   385 AA;  42807 MW;  33924B6C36017B79 CRC64;
     MGSHQERPLI GLLFSETGVT ADIERSQRYG ALLAVEQLNR EGGVGGRPIE TLSQDPGGDP
     DRYRLCAEDF IRNRGVRFLV GCYMSHTRKA VMPVVERADA LLCYPTPYEG FEYSPNIVYG
     GPAPNQNSAP LAAYLIRHYG ERVVFIGSDY IYPRESNHVM RHLYRQHGGT VLEEIYIPLY
     PSDDDVQRAV ERIYQARADV VFSTVVGTGT AELYRAIARR YGDGRRPPIA SLTTSEAEVA
     KMESDVAEGQ VVVAPYFSSI DTAASRAFVQ ACHGFFPENA TITAWAEAAY WQTLLLGRAA
     QAAGSWRVED VQRHLYDICI DAPQGPVRVE RQNNHSRLSS RIAEIDARGV FQVRWQSPEP
     IRPDPYVVVH NLDDWSASMG GGALP
//
ID   AMIR_PSEAE              Reviewed;         196 AA.
AC   P10932;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   20-MAR-2007, entry version 55.
DE   Aliphatic amidase regulator.
GN   Name=amiR; OrderedLocusNames=PA3363;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAC433;
RX   MEDLINE=89211409; PubMed=2495988; DOI=10.1016/0014-5793(89)80249-2;
RA   Lowe N., Rice P.M., Drew R.E.;
RT   "Nucleotide sequence of the aliphatic amidase regulator gene (amiR) of
RT   Pseudomonas aeruginosa.";
RL   FEBS Lett. 246:39-43(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=95286483; PubMed=7539417;
RA   Wilson S.A., Drew R.E.;
RT   "Transcriptional analysis of the amidase operon from Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 177:3052-3057(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIC.
RC   STRAIN=PAC1;
RX   MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175;
RA   O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E.,
RA   Pearl L.H.;
RT   "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-
RT   regulated transcription antitermination complex.";
RL   EMBO J. 18:5175-5186(1999).
CC   -!- FUNCTION: Positive controlling element of amiE, the gene for
CC       aliphatic amidase. Acts as a transcriptional antitermination
CC       factor. It is thought to allow RNA polymerase read through a rho-
CC       independent transcription terminator between the amiE promoter and
CC       gene.
CC   -!- SUBUNIT: Forms a complex with amiC.
CC   -!- SIMILARITY: Contains 1 ANTAR domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X13776; CAA32023.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06751.1; -; Genomic_DNA.
DR   PIR; B83226; B83226.
DR   PIR; S03884; S03884.
DR   PDB; 1QO0; X-ray; D/E=1-196.
DR   IntAct; P10932; -.
DR   GenomeReviews; AE004091_GR; PA3363.
DR   KEGG; pae:PA3363; -.
DR   BioCyc; PAER287:PA3363-MONOMER; -.
DR   InterPro; IPR005561; AmiR_NasR_reg.
DR   InterPro; IPR011006; CheY_like.
DR   InterPro; IPR008327; Res_reg_antiterm.
DR   Pfam; PF03861; ANTAR; 1.
DR   PIRSF; PIRSF036382; RR_antiterm; 1.
DR   PROSITE; PS50921; ANTAR; 1.
KW   3D-structure; Complete proteome; Transcription;
KW   Transcription antitermination; Transcription regulation.
FT   CHAIN         1    196       Aliphatic amidase regulator.
FT                                /FTId=PRO_0000064582.
FT   DOMAIN      129    190       ANTAR.
FT   CONFLICT     48     48       S -> A (in Ref. 1).
FT   CONFLICT     64     64       R -> G (in Ref. 1).
FT   CONFLICT    141    141       E -> D (in Ref. 1).
FT   CONFLICT    154    154       A -> V (in Ref. 1).
FT   CONFLICT    170    170       Y -> H (in Ref. 1).
FT   HELIX         3      8
FT   HELIX         9     12
FT   STRAND       14     19
FT   HELIX        23     35
FT   STRAND       38     42
FT   STRAND       54     59
FT   HELIX        65     75
FT   STRAND       81     86
FT   HELIX        91    100
FT   STRAND      103    109
FT   HELIX       112    114
FT   HELIX       115    160
FT   HELIX       164    175
FT   TURN        176    179
FT   HELIX       182    189
SQ   SEQUENCE   196 AA;  21903 MW;  306A4F30E8E4C6C0 CRC64;
     MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPESFD VPVDVVFTSI
     FQNRHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV
     SARRISEEMA KLKQKTEQLQ ERIAGQARIN QAKALLMQRH GWDEREAHQY LSREAMKRRE
     PILKIAQELL GNEPSA
//
ID   GCN4_YEAST              Reviewed;         281 AA.
AC   P03069; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0; Q96UT3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-MAR-2007, entry version 82.
DE   General control protein GCN4 (Amino acid biosynthesis regulatory
DE   protein).
GN   Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85038531; PubMed=6387704;
RA   Hinnebusch A.G.;
RT   "Evidence for translational regulation of the activator of general
RT   amino acid control in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84298088; PubMed=6433345;
RA   Thireos G., Penn M.D., Greer H.;
RT   "5' untranslated sequences are required for the translational control
RT   of a yeast regulatory gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62;
RP   ALA-82; ALA-91; ALA-125 AND GLU-196.
RC   STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC   CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX   PubMed=15087486; DOI=10.1093/nar/gkh529;
RA   Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA   Souciet J.-L.;
RT   "Differential evolution of the Saccharomyces cerevisiae DUP240
RT   paralogs and implication of recombination in phylogeny.";
RL   Nucleic Acids Res. 32:2069-2078(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
RX   PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x;
RA   Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.;
RT   "Construction of dimeric F(ab) useful in blood group serology.";
RL   Transfusion 42:257-264(2002).
RN   [6]
RP   DOMAINS.
RX   MEDLINE=87002456; PubMed=3530496; DOI=10.1016/0092-8674(86)90070-X;
RA   Hope I.A., Struhl K.;
RT   "Functional dissection of a eukaryotic transcriptional activator
RT   protein, GCN4 of yeast.";
RL   Cell 46:885-894(1986).
RN   [7]
RP   DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113
RP   AND 120-TRP--PHE-124.
RX   PubMed=7862116;
RA   Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H.,
RA   Hinnebusch A.G.;
RT   "The transcriptional activator GCN4 contains multiple activation
RT   domains that are critically dependent on hydrophobic amino acids.";
RL   Mol. Cell. Biol. 15:1220-1233(1995).
RN   [8]
RP   PHOSPHORYLATION AT THR-165.
RX   PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002;
RA   Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
RT   "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
RL   Mol. Cell. Biol. 22:5395-5404(2002).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
RX   MEDLINE=92054531; PubMed=1948029;
RA   O'Shea E.K., Klemm J.D., Kim P.S., Alber T.;
RT   "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
RT   coiled coil.";
RL   Science 254:539-544(1991).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
RX   MEDLINE=93113690; PubMed=1473154; DOI=10.1016/S0092-8674(05)80070-4;
RA   Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.;
RT   "The GCN4 basic region leucine zipper binds DNA as a dimer of
RT   uninterrupted alpha helices: crystal structure of the protein-DNA
RT   complex.";
RL   Cell 71:1223-1237(1992).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
RX   MEDLINE=99057965; PubMed=9837709; DOI=10.1006/jmbi.1998.2214;
RA   Eckert D.M., Malashkevich V.N., Kim P.S.;
RT   "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried
RT   polar residues.";
RL   J. Mol. Biol. 284:859-865(1998).
RN   [12]
RP   STRUCTURE BY NMR OF 237-281.
RX   MEDLINE=91367802; PubMed=1891459; DOI=10.1093/protein/4.5.519;
RA   Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H.,
RA   Gibson T.;
RT   "The solution structure of a leucine-zipper motif peptide.";
RL   Protein Eng. 4:519-529(1991).
CC   -!- FUNCTION: Is a transcription factor that is responsible for the
CC       activation of more than 30 genes required for amino acid or for
CC       purine biosynthesis in response to amino acid or purine
CC       starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-
CC       3'.
CC   -!- SUBUNIT: Binds DNA as a dimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal
CC       activation domain (NTAD) and the central acidic activation domain
CC       (CAAD) respectively, which can function independently to promote
CC       high-level transcription of the target genes.
CC   -!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation
CC       of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase
CC       complex SCF(Cdc4).
CC   -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; K02205; AAA34640.1; -; Genomic_DNA.
DR   EMBL; K02649; AAA65521.1; -; Genomic_DNA.
DR   EMBL; AJ585686; CAE52206.1; -; Genomic_DNA.
DR   EMBL; AJ585687; CAE52207.1; -; Genomic_DNA.
DR   EMBL; AJ585688; CAE52208.1; -; Genomic_DNA.
DR   EMBL; AJ585689; CAE52209.1; -; Genomic_DNA.
DR   EMBL; AJ585690; CAE52210.1; -; Genomic_DNA.
DR   EMBL; AJ585691; CAE52211.1; -; Genomic_DNA.
DR   EMBL; AJ585692; CAE52212.1; -; Genomic_DNA.
DR   EMBL; AJ585693; CAE52213.1; -; Genomic_DNA.
DR   EMBL; AJ585694; CAE52214.1; -; Genomic_DNA.
DR   EMBL; AJ585695; CAE52215.1; -; Genomic_DNA.
DR   EMBL; AJ585696; CAE52216.1; -; Genomic_DNA.
DR   EMBL; AJ585697; CAE52217.1; -; Genomic_DNA.
DR   EMBL; AJ585698; CAE52218.1; -; Genomic_DNA.
DR   EMBL; AJ585699; CAE52219.1; -; Genomic_DNA.
DR   EMBL; AJ585700; CAE52220.1; -; Genomic_DNA.
DR   EMBL; AJ585701; CAE52221.1; -; Genomic_DNA.
DR   EMBL; AJ585702; CAE52222.1; -; Genomic_DNA.
DR   EMBL; AJ585703; CAE52223.1; -; Genomic_DNA.
DR   EMBL; AJ585704; CAE52224.1; -; Genomic_DNA.
DR   EMBL; AF416613; AAL09032.1; -; mRNA.
DR   EMBL; U18530; AAB64486.1; -; Genomic_DNA.
DR   PIR; A03605; RGBYA2.
DR   PDB; 1CE9; X-ray; A/B/C/D=251-281.
DR   PDB; 1DGC; X-ray; A=220-281.
DR   PDB; 1FAV; X-ray; A=-.
DR   PDB; 1GCL; X-ray; A/B/C/D=249-281.
DR   PDB; 1GCM; X-ray; A/B/C=249-281.
DR   PDB; 1GK6; X-ray; A/B=-.
DR   PDB; 1GZL; X-ray; A/B=-.
DR   PDB; 1IHQ; NMR; A/B=-.
DR   PDB; 1IJ0; X-ray; A/B/C=249-281.
DR   PDB; 1IJ1; X-ray; A/B/C=249-281.
DR   PDB; 1IJ2; X-ray; A/B/C=249-281.
DR   PDB; 1IJ3; X-ray; A/B/C=249-281.
DR   PDB; 1KQL; X-ray; A/B=255-281.
DR   PDB; 1LD4; EM; E/F/G/H/I/J/K/L=225-281.
DR   PDB; 1LLM; X-ray; C/D=-.
DR   PDB; 1NKN; X-ray; A/B/C/D=-.
DR   PDB; 1PIQ; X-ray; A=249-279.
DR   PDB; 1RB1; X-ray; A/B/C=249-281.
DR   PDB; 1RB4; X-ray; A/B/C=249-281.
DR   PDB; 1RB5; X-ray; A/B/C=249-281.
DR   PDB; 1RB6; X-ray; A/B/C=249-281.
DR   PDB; 1SWI; X-ray; A/B/C=249-281.
DR   PDB; 1TMZ; NMR; A/B=-.
DR   PDB; 1UNT; X-ray; A/B=249-281.
DR   PDB; 1UNU; X-ray; A/B=249-281.
DR   PDB; 1UNV; X-ray; A/B=249-281.
DR   PDB; 1UNW; X-ray; A/B=249-281.
DR   PDB; 1UNX; X-ray; A/B=249-281.
DR   PDB; 1UNY; X-ray; A/B=249-281.
DR   PDB; 1UNZ; X-ray; A/B=249-281.
DR   PDB; 1UO0; X-ray; A/B=249-281.
DR   PDB; 1UO1; X-ray; A/B=249-281.
DR   PDB; 1UO2; X-ray; A/B=249-281.
DR   PDB; 1UO3; X-ray; A/B=249-281.
DR   PDB; 1UO4; X-ray; A/B=249-281.
DR   PDB; 1UO5; X-ray; A/B=249-281.
DR   PDB; 1W5G; X-ray; A/B=249-281.
DR   PDB; 1W5H; X-ray; A/B=249-281.
DR   PDB; 1W5I; X-ray; A/B=249-281.
DR   PDB; 1W5J; X-ray; A/B/C/D=249-281.
DR   PDB; 1W5K; X-ray; A/B/C/D=249-281.
DR   PDB; 1W5L; X-ray; A/B=249-281.
DR   PDB; 1YSA; X-ray; C/D=226-281.
DR   PDB; 1ZII; X-ray; A/B=249-281.
DR   PDB; 1ZIJ; X-ray; A/B/C=249-281.
DR   PDB; 1ZIK; X-ray; A/B=249-281.
DR   PDB; 1ZIL; X-ray; A/B=249-281.
DR   PDB; 1ZIM; X-ray; A/B/C=249-281.
DR   PDB; 1ZTA; NMR; @=247-281.
DR   PDB; 2B1F; X-ray; A/B/C/D=251-281.
DR   PDB; 2B22; X-ray; A=251-281.
DR   PDB; 2BNI; X-ray; A/B/C/D=249-281.
DR   PDB; 2DGC; X-ray; A=220-281.
DR   PDB; 2ZTA; X-ray; A/B=249-281.
DR   DIP; DIP:591N; -.
DR   TRANSFAC; T00321; -.
DR   Ensembl; YEL009C; Saccharomyces cerevisiae.
DR   GenomeReviews; U00092_GR; YEL009C.
DR   KEGG; sce:YEL009C; -.
DR   CYGD; YEL009c; -.
DR   SGD; S000000735; GCN4.
DR   BioCyc; SCER-S28-01:SCER-S28-01-001585-MONOMER; -.
DR   LinkHub; P03069; -.
DR   GermOnline; YEL009C; Saccharomyces cerevisiae.
DR   GO; GO:0005634; C:nucleus; IPI:SGD.
DR   GO; GO:0003700; F:transcription factor activity; IDA:SGD.
DR   GO; GO:0008652; P:amino acid biosynthetic process; TAS:SGD.
DR   GO; GO:0006990; P:unfolded protein response, positive regulat...; IMP:SGD.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
KW   3D-structure; Activator; Amino-acid biosynthesis; Complete proteome;
KW   DNA-binding; Nuclear protein; Phosphorylation; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    281       General control protein GCN4.
FT                                /FTId=PRO_0000076490.
FT   DOMAIN      253    274       Leucine-zipper.
FT   DNA_BIND    231    249       Basic motif.
FT   REGION       89    100       Required for transcriptional activation.
FT   REGION      106    125       Required for transcriptional activation.
FT   MOD_RES     165    165       Phosphothreonine (by PHO85).
FT   VARIANT      24     24       S -> P (in strain: CLIB 219).
FT   VARIANT      62     62       P -> S (in strain: CLIB 630 haplotype
FT                                Ha2).
FT   VARIANT      82     82       T -> A (in strain: CLIB 556 haplotype
FT                                Ha1).
FT   VARIANT      91     91       D -> A (in strain: CLIB 95, CLIB 219,
FT                                CLIB 382, CLIB 388, CLIB 410, CLIB 413,
FT                                CLIB 556, CLIB 630, K1, R12, R13
FT                                haplotype Ha2, Sigma 1278B haplotype Ha1,
FT                                YIIc12 and YIIc17).
FT   VARIANT     125    125       D -> A (in strain: CLIB 556 haplotype
FT                                Ha1).
FT   VARIANT     196    196       D -> E (in strain: CLIB 388, CLIB 410,
FT                                CLIB 413, CLIB 630 haplotype Ha1, K1,
FT                                YIIc12 haplotype Ha2 and YIIc17 haplotype
FT                                Ha1).
FT   MUTAGEN      97     98       FF->AA: Reduces transcriptional
FT                                activation activity; when associated with
FT                                A-107; A-110; A-113; A-120; A-123 and A-
FT                                124.
FT   MUTAGEN     107    107       M->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-110; A-113; A-120; A-123 and A-124.
FT   MUTAGEN     110    110       Y->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-107; A-113; A-120; A-123 and A-124.
FT   MUTAGEN     113    113       L->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-107; A-110; A-120; A-123 and A-124.
FT   MUTAGEN     120    124       WTSLF->ATSAA: Reduces transcriptional
FT                                activation activity; when associated with
FT                                A-97; A-98; A-107; A-110 and A-113.
FT   CONFLICT    239    281       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
FT                                ER -> PGVLVRESCKE (in Ref. 2).
FT   HELIX       230    276
FT   HELIX       250    276
FT   HELIX       251    278
SQ   SEQUENCE   281 AA;  31310 MW;  2ED1B8E35D509578 CRC64;
     MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD
     TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW
     TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK
     KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR
     RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R
//
ID   FLAV_ANASO              Reviewed;         170 AA.
AC   P0A3E0; P11241;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 17.
DE   Flavodoxin.
GN   Name=isiB;
OS   Anabaena sp. (strain PCC 7119).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1168;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92074973; PubMed=1720613;
RA   Fillat M.F., Borrias W.E., Weisbeek P.J.;
RT   "Isolation and overexpression in Escherichia coli of the flavodoxin
RT   gene from Anabaena PCC 7119.";
RL   Biochem. J. 280:187-191(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-37.
RX   MEDLINE=90381288; PubMed=2119231; DOI=10.1016/0167-4838(90)90091-S;
RA   Fillat M.F., Edmondson D.E., Gomez-Moreno C.;
RT   "Structural and chemical properties of a flavodoxin from Anabaena PCC
RT   7119.";
RL   Biochim. Biophys. Acta 1040:301-307(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=99318886; PubMed=10388575; DOI=10.1006/jmbi.1999.2863;
RA   Fernandez-Recio J., Romero A., Sancho J.;
RT   "Energetics of a hydrogen bond (charged and neutral) and of a cation-
RT   pi interaction in apoflavodoxin.";
RL   J. Mol. Biol. 290:319-330(1999).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INTERACTION:
CC       P08165:FDXR (xeno); NbExp=3; IntAct=EBI-593907, EBI-593948;
CC       P10933:PETH (xeno); NbExp=1; IntAct=EBI-593907, EBI-931306;
CC       P21890:petH; NbExp=5; IntAct=EBI-593907, EBI-593915;
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; S68006; AAB20462.1; -; Genomic_DNA.
DR   PDB; 1DX9; X-ray; A/B/C/D=1-170.
DR   PDB; 1FTG; X-ray; @=3-170.
DR   PDB; 1OBO; X-ray; A/B=3-170.
DR   PDB; 1OBV; X-ray; A=3-170.
DR   PDB; 1QHE; X-ray; A=3-170.
DR   IntAct; P0A3E0; -.
DR   LinkHub; P0A3E0; -.
DR   GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; TAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0010106; P:cellular response to iron ion starvation; TAS:UniProtKB.
DR   GO; GO:0006118; P:electron transport; IDA:UniProtKB.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171600.
FT   DOMAIN        5    165       Flavodoxin-like.
FT   STRAND        3      8
FT   STRAND       11     13
FT   HELIX        14     26
FT   TURN         28     30
FT   STRAND       31     35
FT   TURN         36     38
FT   HELIX        41     46
FT   STRAND       48     57
FT   TURN         58     60
FT   HELIX        64     70
FT   HELIX        71     75
FT   STRAND       82     88
FT   TURN         91     96
FT   HELIX       100    111
FT   STRAND      137    143
FT   TURN        145    147
FT   HELIX       149    151
FT   HELIX       152    167
SQ   SEQUENCE   170 AA;  18964 MW;  069E8DEBA9E33302 CRC64;
     MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI
     GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY
     WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL
//
ID   FLAV_ANASP              Reviewed;         170 AA.
AC   P0A3D9; P11241;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 21.
DE   Flavodoxin.
GN   Name=isiB; OrderedLocusNames=alr2405;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89296496; PubMed=2500643; DOI=10.1093/nar/17.11.4384;
RA   Leonhardt K.G., Straus N.A.;
RT   "Sequence of the flavodoxin gene from Anabaena variabilis 7120.";
RL   Nucleic Acids Res. 17:4384-4384(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [3]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91104858; PubMed=2125478; DOI=10.1021/bi00493a014;
RA   Stockman B.J., Krezel A.M., Markley J.L., Leonhardt K.G., Straus N.A.;
RT   "Hydrogen-1, carbon-13, and nitrogen-15 NMR spectroscopy of Anabaena
RT   7120 flavodoxin: assignment of beta-sheet and flavin binding site
RT   resonances and analysis of protein-flavin interactions.";
RL   Biochemistry 29:9600-9609(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=93271891; PubMed=1303762;
RA   Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J.,
RA   Markley J.L., Sundaralingam M.;
RT   "Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at
RT   2-A resolution.";
RL   Protein Sci. 1:1413-1427(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=15299298; DOI=10.1107/S0907444994011716;
RA   Burkhart B.M., Ramakrishnan B., Yan H., Reedstrom R.J., Markley J.L.,
RA   Straus N.A., Sundaralingam M.;
RT   "Structure of the trigonal form of recombinant oxidized flavodoxin
RT   from Anabaena 7120 at 1.40-A resolution.";
RL   Acta Crystallogr. D 51:318-330(1995).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X14577; CAA32720.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB74104.1; -; Genomic_DNA.
DR   PIR; AF2106; AF2106.
DR   PDB; 1FLV; X-ray; @=1-170.
DR   PDB; 1RCF; X-ray; @=1-170.
DR   GenomeReviews; BA000019_GR; alr2405.
DR   KEGG; ana:alr2405; -.
DR   LinkHub; P0A3D9; -.
DR   GO; GO:0009767; P:photosynthetic electron transport; NAS:UniProtKB.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171601.
FT   DOMAIN        5    165       Flavodoxin-like.
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     25
FT   TURN         26     28
FT   STRAND       31     35
FT   HELIX        41     46
FT   STRAND       48     53
FT   TURN         58     60
FT   HELIX        64     70
FT   HELIX        71     75
FT   STRAND       82     88
FT   TURN         91     96
FT   HELIX       100    111
FT   STRAND      137    143
FT   TURN        145    147
FT   HELIX       149    151
FT   HELIX       152    166
SQ   SEQUENCE   170 AA;  18964 MW;  069E8DEBA9E33302 CRC64;
     MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI
     GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY
     WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL
//
ID   FLAV_AQUAE              Reviewed;         185 AA.
AC   O67866;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   20-MAR-2007, entry version 42.
DE   Flavodoxin.
GN   Name=fldA; Synonyms=floX; OrderedLocusNames=aq_2096;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AE000657; AAC07825.1; -; Genomic_DNA.
DR   PIR; F70479; F70479.
DR   PDB; 2ARK; X-ray; A/B/C/D/E/F=1-185.
DR   GenomeReviews; AE000657_GR; aq_2096.
DR   KEGG; aae:aq_2096; -.
DR   BioCyc; AAEO63363:AQ_2096-MONOMER; -.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Transport.
FT   CHAIN         1    185       Flavodoxin.
FT                                /FTId=PRO_0000171602.
FT   DOMAIN        4    159       Flavodoxin-like.
FT   STRAND        2      8
FT   STRAND       11     13
FT   HELIX        14     27
FT   STRAND       32     38
FT   TURN         39     41
FT   HELIX        44     49
FT   STRAND       51     58
FT   HELIX        66     74
FT   HELIX        76     78
FT   TURN         79     81
FT   STRAND       87     97
FT   HELIX       101    114
FT   STRAND      122    127
FT   STRAND      130    141
FT   HELIX       145    165
FT   HELIX       172    178
FT   HELIX       180    182
SQ   SEQUENCE   185 AA;  20444 MW;  7C138666D5B89281 CRC64;
     MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN
     MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF
     GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP
     ARFVD
//
ID   FLS1_ARATH              Reviewed;         336 AA.
AC   Q96330; O04730; O04731; O04732; O04830; O04831; O04832;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   23-JAN-2007, entry version 50.
DE   Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23)
DE   (EC 1.14.11.9) (FLS 1).
GN   Name=FLS1; OrderedLocusNames=At5g08640; ORFNames=MAH20.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   MEDLINE=97267154; PubMed=9112784; DOI=10.1104/pp.113.4.1437;
RA   Pelletier M.K., Murrell J.R., Shirley B.W.;
RT   "Characterization of flavonol synthase and leucoanthocyanidin
RT   dioxygenase genes in Arabidopsis. Further evidence for differential
RT   regulation of 'early' and 'late' genes.";
RL   Plant Physiol. 113:1437-1445(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RA   Hartmann U., Weisshaar B.;
RT   "Isolation of an Arabidopsis clone encoding flavonol synthase.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98069011; PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II.
RT   Sequence features of the regions of 1,044,062 bp covered by thirteen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; U72631; AAB17393.1; -; Genomic_DNA.
DR   EMBL; U84258; AAC69362.1; -; Genomic_DNA.
DR   EMBL; U84259; AAC69363.1; -; mRNA.
DR   EMBL; U84260; AAB41504.1; -; mRNA.
DR   EMBL; AB006697; BAB10013.1; -; Genomic_DNA.
DR   EMBL; AY058068; AAL24176.1; -; mRNA.
DR   EMBL; BT000494; AAN18063.1; -; mRNA.
DR   EMBL; AY086328; AAM64397.1; -; mRNA.
DR   UniGene; At.8771; -.
DR   HSSP; Q96323; 1GP6.
DR   GenomeReviews; BA000015_GR; AT5G08640.
DR   KEGG; ath:At5g08640; -.
DR   TAIR; At5g08640; -.
DR   ArrayExpress; Q96330; -.
DR   GermOnline; AT5G08640; Arabidopsis thaliana.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    336       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067291.
FT   METAL       221    221       Iron (By similarity).
FT   METAL       223    223       Iron (By similarity).
FT   METAL       277    277       Iron (By similarity).
SQ   SEQUENCE   336 AA;  38282 MW;  3283E3AFE603D2A9 CRC64;
     MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV
     VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ
     KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG
     LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV
     FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK
     IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD
//
ID   FLAV_AZOCH              Reviewed;         180 AA.
AC   P23001; P35708;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   23-JAN-2007, entry version 48.
DE   Flavodoxin-B (FldB).
GN   Name=nifF;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8765738;
RA   Peelen S., Wijmenga S., Erbel P.J., Robson R.L., Eady R.R.,
RA   Vervoort J.;
RT   "Possible role of a short extra loop of the long-chain flavodoxin from
RT   Azotobacter chroococcum in electron transfer to nitrogenase: complete
RT   1H, 15N and 13C backbone assignments and secondary solution structure
RT   of the flavodoxin.";
RL   J. Biomol. NMR 7:315-330(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=MCD 1155;
RX   MEDLINE=91315397; PubMed=1859358;
RA   Bagby S., Barker P.D., Hill H.A.O., Sanghera G.S., Dunbar B.,
RA   Ashby G.A., Eady R.R., Thorneley R.N.F.;
RT   "Direct electrochemistry of two genetically distinct flavodoxins
RT   isolated from Azotobacter chroococcum grown under nitrogen-fixing
RT   conditions.";
RL   Biochem. J. 277:313-319(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M73019; AAB36613.1; -; Genomic_DNA.
DR   HSSP; P11241; 1OBO.
DR   SMR; P23001; 2-180.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Direct protein sequencing; Electron transport; Flavoprotein; FMN;
KW   Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    180       Flavodoxin-B.
FT                                /FTId=PRO_0000171603.
FT   DOMAIN        4    173       Flavodoxin-like.
SQ   SEQUENCE   180 AA;  19524 MW;  A19BE720B93F551D CRC64;
     MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDAVNVNRV SAEDFAQYQF LILGTPTLGE
     GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENFLDA MGELHSFFTE
     RGAKVVGAWS TDGYEFEGST AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL
//
ID   FLAV_AZOVI              Reviewed;         180 AA.
AC   P00324;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 61.
DE   Flavodoxin-2.
GN   Name=nifF;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89123097; PubMed=2644218;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A.,
RA   Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88087273; PubMed=3121629;
RA   Bennett L., Jacobson M., Dean D.R.;
RT   "Isolation, sequencing, and mutagenesis of the nifF gene encoding
RT   flavodoxin from Azotobacter vinelandii.";
RL   J. Biol. Chem. 263:1364-1369(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-180.
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
RX   MEDLINE=77242321; PubMed=889809; DOI=10.1021/bi00635a005;
RA   Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.;
RT   "Complete amino acid sequence of azotoflavin, a flavodoxin from
RT   Azotobacter vinelandii.";
RL   Biochemistry 16:3525-3537(1977).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-21, AND MASS SPECTROMETRY.
RC   STRAIN=OP / UW136;
RX   MEDLINE=96276406; PubMed=8694750;
RA   Gangeswaran R., Eady R.R.;
RT   "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in
RT   electron donation to purified assimilatory nitrate reductase.";
RL   Biochem. J. 317:103-108(1996).
RN   [5]
RP   STRUCTURE BY NMR.
RC   STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617;
RX   MEDLINE=98180401; PubMed=9521106;
RA   Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A.,
RA   van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.;
RT   "Apparent local stability of the secondary structure of Azotobacter
RT   vinelandii holoflavodoxin II as probed by hydrogen exchange:
RT   implications for redox potential regulation and flavodoxin folding.";
RL   Protein Sci. 7:306-317(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SUBUNIT: Monomer.
CC   -!- MASS SPECTROMETRY: MW=19533; MW_ERR=5; METHOD=Electrospray;
CC       RANGE=2-180; NOTE=Ref.4.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M20568; AAA64735.1; -; Genomic_DNA.
DR   EMBL; J03519; AAA22154.1; -; Genomic_DNA.
DR   PIR; A29935; FXAVEP.
DR   PDB; 1YOB; X-ray; A/B=1-180.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    180       Flavodoxin-2.
FT                                /FTId=PRO_0000171605.
FT   DOMAIN        4    173       Flavodoxin-like.
FT   STRAND        3      7
FT   STRAND       10     12
FT   HELIX        13     22
FT   TURN         27     29
FT   HELIX        36     38
FT   HELIX        41     45
FT   STRAND       48     55
FT   TURN         58     60
FT   HELIX        65     67
FT   HELIX        74     81
FT   STRAND       90     96
FT   TURN         99    101
FT   TURN        103    107
FT   HELIX       108    118
FT   TURN        119    121
FT   STRAND      123    125
FT   STRAND      141    151
FT   TURN        153    155
FT   HELIX       157    159
FT   HELIX       160    171
FT   HELIX       172    175
SQ   SEQUENCE   180 AA;  19663 MW;  8B1B43F23AB5E8B4 CRC64;
     MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDALNVNRV SAEDFAQYQF LILGTPTLGE
     GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENYLDA LGELYSFFKD
     RGAKIVGSWS TDGYEFESSE AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL
//
ID   FLAV_BACSU              Reviewed;         158 AA.
AC   O34737;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   31-OCT-2006, entry version 48.
DE   Probable flavodoxin-1.
GN   Name=ykuN; OrderedLocusNames=BSU14150;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Scanlan E., Devine K.M.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AJ222587; CAA10877.1; -; Genomic_DNA.
DR   EMBL; Z99111; CAB13288.1; -; Genomic_DNA.
DR   PIR; C69866; C69866.
DR   HSSP; P00323; 1J9E.
DR   GenomeReviews; AL009126_GR; BSU14150.
DR   KEGG; bsu:BG13298; -.
DR   SubtiList; BG13298; ykuN.
DR   BioCyc; BSUB1423:BSU1417-MONOMER; -.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    158       Probable flavodoxin-1.
FT                                /FTId=PRO_0000171607.
FT   DOMAIN        4    144       Flavodoxin-like.
SQ   SEQUENCE   158 AA;  17793 MW;  FECE71BF6E552D3F CRC64;
     MAKALITYAS MSGNTEDIAF IIKDTLQEYE LDIDCVEIND MDASCLTSYD YVLIGTYTWG
     DGDLPYEAED FFEEVKQIQL NGLKTACFGS GDYSYPKFCE AVNLFNVMLQ EAGAAVYQET
     LKIELAPETD EDVESCRAFA RGFLAWADYM NKEKIHVS
//
ID   FLAV_CHOCR              Reviewed;         173 AA.
AC   P14070;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   20-MAR-2007, entry version 53.
DE   Flavodoxin.
OS   Chondrus crispus (Carragheen).
OC   Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae;
OC   Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=90088453; PubMed=2597140;
RA   Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.;
RT   "The amino acid sequence of a flavodoxin from the eukaryotic red alga
RT   Chondrus crispus.";
RL   Biochem. J. 263:981-984(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-34.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   MEDLINE=90368796; PubMed=2394748;
RA   Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.;
RT   "Tertiary structure of oxidized flavodoxin from an eukaryotic red alga
RT   Chondrus crispus at 2.35-A resolution. Localization of charged
RT   residues and implication for interaction with electron transfer
RT   partners.";
RL   J. Biol. Chem. 265:15804-15812(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=92292160; PubMed=1602481; DOI=10.1016/0022-2836(92)90400-E;
RA   Fukuyama K., Matsubara H., Rogers L.J.;
RT   "Crystal structure of oxidized flavodoxin from a red alga Chondrus
RT   crispus refined at 1.8-A resolution. Description of the flavin
RT   mononucleotide binding site.";
RL   J. Mol. Biol. 225:775-789(1992).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   PIR; S06648; S06648.
DR   PDB; 2FCR; X-ray; @=1-173.
DR   LinkHub; P14070; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    173       Flavodoxin.
FT                                /FTId=PRO_0000171612.
FT   DOMAIN        2    168       Flavodoxin-like.
FT   CONFLICT     29     29       D -> S (in Ref. 2).
FT   CONFLICT     33     33       D -> S (in Ref. 2).
FT   STRAND        2      6
FT   STRAND        9     11
FT   HELIX        12     24
FT   HELIX        25     27
FT   HELIX        34     36
FT   HELIX        40     45
FT   STRAND       47     54
FT   HELIX        69     75
FT   HELIX        77     79
FT   STRAND       86     93
FT   TURN         95     97
FT   TURN        102    104
FT   HELIX       105    115
FT   STRAND      119    121
FT   HELIX       126    128
FT   STRAND      141    148
FT   TURN        149    151
FT   HELIX       156    171
SQ   SEQUENCE   173 AA;  18871 MW;  EF1F3A3554CA4166 CRC64;
     KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA
     DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP
     VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV
//
ID   FLAV_CLOSA              Reviewed;         160 AA.
AC   P18855;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   31-OCT-2006, entry version 39.
DE   Flavodoxin.
GN   Name=floX;
OS   Clostridium saccharobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=169679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91123180; PubMed=1991710;
RA   Santangelo J.D., Jones D.T., Woods D.R.;
RT   "Metronidazole activation and isolation of Clostridium acetobutylicum
RT   electron transport genes.";
RL   J. Bacteriol. 173:1088-1095(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -!- CAUTION: Was originally thought to originate from
CC       C.acetobutylicum.
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DR   EMBL; M36770; AAA23238.1; -; Genomic_DNA.
DR   HSSP; P00322; 2FVX.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    160       Flavodoxin.
FT                                /FTId=PRO_0000171614.
FT   DOMAIN        3    153       Flavodoxin-like.
SQ   SEQUENCE   160 AA;  17763 MW;  6153F8A1F0BCDC8D CRC64;
     MKISILYSSK TGKTERVAKL IEEGVKRSGN IEVKTMNLDA VDKKFLQESE GIIFGTPTYY
     ANISWEMKKW IDESSEFNLE GKLGAAFSTA NSIAGGSDIA LLTILNHLMV KGMLVYSGGV
     AFGKPKTHLG YVHINEIQEN EDENARIFGE RIANKVKQIF
//
ID   FLAV_CLOBE              Reviewed;         138 AA.
AC   P00322;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-MAR-2007, entry version 58.
DE   Flavodoxin.
OS   Clostridium beijerinckii (Clostridium MP).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1520;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=74277392; PubMed=4843142;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.;
RT   "The amino acid sequence of the Clostridium MP flavodoxin.";
RL   J. Biol. Chem. 249:4393-4396(1974).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM.
RX   MEDLINE=74277391; PubMed=4843141;
RA   Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G.,
RA   Smith W.W., Ludwig M.L.;
RT   "The structure of the oxidized form of clostridial flavodoxin at 1.9-A
RT   resolution.";
RL   J. Biol. Chem. 249:4383-4392(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=97178811; PubMed=9063874; DOI=10.1021/bi962180o;
RA   Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M.,
RA   Feng Y., Swenson R.P.;
RT   "Control of oxidation-reduction potentials in flavodoxin from
RT   Clostridium beijerinckii: the role of conformation changes.";
RL   Biochemistry 36:1259-1280(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   PDB; 1FLA; X-ray; @=1-138.
DR   PDB; 1FLD; X-ray; @=1-138.
DR   PDB; 1FLN; X-ray; @=1-138.
DR   PDB; 1FVX; X-ray; @=1-138.
DR   PDB; 2FAX; X-ray; @=1-138.
DR   PDB; 2FDX; X-ray; @=1-138.
DR   PDB; 2FLV; X-ray; @=1-138.
DR   PDB; 2FOX; X-ray; @=1-138.
DR   PDB; 2FVX; X-ray; @=1-138.
DR   PDB; 3NLL; X-ray; @=1-138.
DR   PDB; 4NLL; X-ray; @=1-138.
DR   PDB; 4NUL; X-ray; @=1-138.
DR   PDB; 5NLL; X-ray; @=1-138.
DR   PDB; 5NUL; X-ray; @=1-138.
DR   PDB; 5ULL; X-ray; @=1-138.
DR   PDB; 6NUL; X-ray; @=1-138.
DR   LinkHub; P00322; -.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    138       Flavodoxin.
FT                                /FTId=PRO_0000171613.
FT   DOMAIN        1    136       Flavodoxin-like.
FT   STRAND        2      6
FT   STRAND        8     10
FT   HELIX        11     25
FT   STRAND       31     34
FT   HELIX        35     37
FT   HELIX        40     43
FT   STRAND       47     53
FT   TURN         57     59
FT   TURN         63     65
FT   HELIX        66     73
FT   HELIX        74     76
FT   STRAND       81     93
FT   HELIX        94    105
FT   STRAND      115    120
FT   HELIX       122    124
FT   HELIX       125    136
SQ   SEQUENCE   138 AA;  15332 MW;  98BE3746EC000FF1 CRC64;
     MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV
     LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE
     PDEAEQDCIE FGKKIANI
//
ID   FLAV_DESDE              Reviewed;         148 AA.
AC   P26492;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   31-OCT-2006, entry version 37.
DE   Flavodoxin.
OS   Desulfovibrio desulfuricans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 29577 / CIP 107039 / LMG 7529 / NCIB 8307 / VKM B-1799;
RX   MEDLINE=91316149; PubMed=1859847; DOI=10.1016/0167-4781(91)90190-W;
RA   Helms L.R., Swenson R.P.;
RT   "Cloning and characterization of the flavodoxin gene from
RT   Desulfovibrio desulfuricans.";
RL   Biochim. Biophys. Acta 1089:417-419(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X59438; CAA42064.1; -; mRNA.
DR   PIR; S17000; FXDVD.
DR   HSSP; P00323; 1BU5.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171615.
FT   DOMAIN        4    145       Flavodoxin-like.
SQ   SEQUENCE   148 AA;  15694 MW;  1CE35B4B79817459 CRC64;
     MSKVLIVFGS STGNTESIAQ KLEELIAAGG HEVTLLNAAD ASAENLADGY DAVLFGCSAW
     GMEDLEMQDD FLSLFEEFNR IGLAGRKVAA FASGDQEYEH FCGAVPAIEE RAKELGATII
     AEGLKMEGDA SNDPEAVASF AEDVLKQL
//
ID   FLAV_DESGI              Reviewed;         146 AA.
AC   Q01095;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   31-OCT-2006, entry version 38.
DE   Flavodoxin.
OS   Desulfovibrio gigas.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759;
RX   MEDLINE=92329549; PubMed=1627649; DOI=10.1016/0167-4781(92)90034-W;
RA   Helms L.R., Swenson R.P.;
RT   "The primary structures of the flavodoxins from two strains of
RT   Desulfovibrio gigas. Cloning and nucleotide sequence of the structural
RT   genes.";
RL   Biochim. Biophys. Acta 1131:325-328(1992).
CC   -!- FUNCTION: Electron-transfer proteins that function in various
CC       electron transport systems in micro-organisms. Functionally
CC       interchangeable with ferredoxin.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X64766; CAA46013.1; -; Genomic_DNA.
DR   PIR; S24311; S24311.
DR   HSSP; P00323; 1BU5.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171617.
FT   DOMAIN        4    143       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15470 MW;  95D9E73B1FCF1403 CRC64;
     MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW
     GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV
     ASSLKIDGEP DSAEVLDWAR EVLARV
//
ID   FLAV_DESSA              Reviewed;         146 AA.
AC   P18086;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   20-MAR-2007, entry version 39.
DE   Flavodoxin.
OS   Desulfovibrio salexigens.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763;
RX   MEDLINE=90241257; PubMed=2334437; DOI=10.1016/0006-291X(90)92393-E;
RA   Helms L.R., Krey G.D., Swenson R.P.;
RT   "Identification, sequence determination, and expression of the
RT   flavodoxin gene from Desulfovibrio salexigens.";
RL   Biochem. Biophys. Res. Commun. 168:809-817(1990).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M35475; AAA23368.1; -; Genomic_DNA.
DR   PIR; A34640; A34640.
DR   HSSP; P00323; 1FX1.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171619.
FT   DOMAIN        4    143       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15812 MW;  BDE3651310E1F780 CRC64;
     MSKSLIVYGS TTGNTETAAE YVAEAFENKE IDVELKNVTD VSVADLGNGY DIVLFGCSTW
     GEEEIELQDD FIPLYDSLEN ADLKGKKVSV FGCGDSDYTY FCGAVDAIEE KLEKMGAVVI
     GDSLKIDGDP ERDEIVSWGS GIADKI
//
ID   FLAV_DESVH              Reviewed;         148 AA.
AC   P00323;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   20-MAR-2007, entry version 66.
DE   Flavodoxin.
GN   OrderedLocusNames=DVU_2680;
OS   Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB
OS   8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89008444; PubMed=3170590;
RA   Krey G.D., Vanin E.F., Swenson R.P.;
RT   "Cloning, nucleotide sequence, and expression of the flavodoxin gene
RT   from Desulfovibrio vulgaris (Hildenborough).";
RL   J. Biol. Chem. 263:15436-15443(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Curley G.P., Voordouw G.;
RT   "Cloning and sequencing of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris Hildenborough.";
RL   FEMS Microbiol. Lett. 49:295-299(1988).
RN   [3]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=77118626; PubMed=402366;
RA   Dubourdieu M., Fox J.L.;
RT   "Amino acid sequence of Desulfovibrio vulgaris flavodoxin.";
RL   J. Biol. Chem. 252:1453-1463(1977).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=91162643; PubMed=2002503; DOI=10.1016/0022-2836(91)90884-9;
RA   Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.;
RT   "Comparison of the crystal structures of a flavodoxin in its three
RT   oxidation states at cryogenic temperatures.";
RL   J. Mol. Biol. 218:195-208(1991).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=74087652; PubMed=4521211;
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H.;
RT   "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin
RT   at 2.0-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=73044810; PubMed=4508313;
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.;
RT   "Structure of the oxidized form of a flavodoxin at 2.5-A resolution:
RT   resolution of the phase ambiguity by anomalous scattering.";
RL   Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=99089597; PubMed=9874201;
RA   Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D.,
RA   Mayhew S.G., Higgins T.M.;
RT   "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough)
RT   apoflavodoxin-riboflavin complex.";
RL   Eur. J. Biochem. 258:362-371(1998).
RN   [9]
RP   STRUCTURE BY NMR.
RX   MEDLINE=93238683; PubMed=8477691;
RA   Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G.,
RA   Mueller F., Rueterjans H.;
RT   "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio
RT   vulgaris flavodoxin. Sequential assignments and identification of
RT   secondary structure elements.";
RL   Eur. J. Biochem. 213:167-184(1993).
RN   [10]
RP   STRUCTURE BY NMR.
RX   MEDLINE=96283837; PubMed=8681954;
RA   Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.;
RT   "NMR investigation of the solution conformation of oxidized flavodoxin
RT   from Desulfovibrio vulgaris. Determination of the tertiary structure
RT   and detection of protein-bound water molecules.";
RL   Eur. J. Biochem. 238:423-434(1996).
RN   [11]
RP   STRUCTURE BY NMR.
RX   MEDLINE=93237739; PubMed=8477184;
RA   Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A.,
RA   Swenson R.P.;
RT   "1H and 15N resonance assignments and solution secondary structure of
RT   oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear
RT   three-dimensional NMR spectroscopy.";
RL   J. Biomol. NMR 3:133-149(1993).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; J04033; AAA23367.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS97152.1; -; Genomic_DNA.
DR   PIR; A31991; FXDV.
DR   PDB; 1AKQ; X-ray; @=2-148.
DR   PDB; 1AKR; X-ray; @=2-148.
DR   PDB; 1AKT; X-ray; @=2-148.
DR   PDB; 1AKU; X-ray; @=2-148.
DR   PDB; 1AKV; X-ray; @=2-148.
DR   PDB; 1AKW; X-ray; @=2-148.
DR   PDB; 1AZL; X-ray; @=2-148.
DR   PDB; 1BU5; X-ray; A=2-148.
DR   PDB; 1C7E; X-ray; A/B=2-148.
DR   PDB; 1C7F; X-ray; A/B=2-148.
DR   PDB; 1F4P; X-ray; A=2-148.
DR   PDB; 1FX1; X-ray; @=1-148.
DR   PDB; 1I1O; X-ray; A=3-148.
DR   PDB; 1J8Q; X-ray; A=3-148.
DR   PDB; 1J9E; X-ray; A=3-148.
DR   PDB; 1J9G; X-ray; A=3-148.
DR   PDB; 1WSB; X-ray; A=1-148.
DR   PDB; 1WSW; X-ray; A=1-148.
DR   PDB; 1XT6; X-ray; A=3-148.
DR   PDB; 1XYV; X-ray; A=1-148.
DR   PDB; 1XYY; X-ray; A=1-148.
DR   PDB; 2FX2; X-ray; @=3-148.
DR   PDB; 3FX2; X-ray; @=3-148.
DR   PDB; 4FX2; X-ray; @=3-148.
DR   PDB; 5FX2; X-ray; @=3-148.
DR   GenomeReviews; AE017285_GR; DVU_2680.
DR   KEGG; dvu:DVU2680; -.
DR   TIGR; DVU_2680; -.
DR   BioCyc; DVUL882:DVU2680-MONOMER; -.
DR   LinkHub; P00323; -.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171620.
FT   DOMAIN        4    145       Flavodoxin-like.
FT   CONFLICT     28     28       D -> N (in Ref. 2).
FT   STRAND        3      9
FT   STRAND       11     13
FT   HELIX        14     29
FT   STRAND       32     37
FT   HELIX        38     40
FT   TURN         44     49
FT   STRAND       51     57
FT   STRAND       62     64
FT   TURN         69     71
FT   HELIX        72     76
FT   HELIX        78     80
FT   STRAND       87     94
FT   STRAND       98    100
FT   HELIX       103    114
FT   STRAND      124    128
FT   HELIX       130    133
FT   HELIX       134    145
SQ   SEQUENCE   148 AA;  15823 MW;  E07630E7047ABD3F CRC64;
     MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW
     GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV
     QDGLRIDGDP RAARDDIVGW AHDVRGAI
//
ID   FLAV_DESVM              Reviewed;         148 AA.
AC   P71165;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   31-OCT-2006, entry version 35.
DE   Flavodoxin.
OS   Desulfovibrio vulgaris (strain Miyazaki).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=Isolate F;
RX   MEDLINE=98230696; PubMed=9562622;
RA   Kitamura M., Sagara T., Taniguchi M., Ashida M., Ezoe K., Kohno K.,
RA   Kojima S., Ozawa K., Akutsu H., Kumagai I., Nakaya T.;
RT   "Cloning and expression of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris (Miyazaki F).";
RL   J. Biochem. 123:891-898(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; D88493; BAA13628.1; -; Genomic_DNA.
DR   HSSP; P00323; 1J9E.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171621.
FT   DOMAIN        4    145       Flavodoxin-like.
SQ   SEQUENCE   148 AA;  15656 MW;  9D321268D04D89B4 CRC64;
     MANVLIVYGS TTGNTAWVAE TVGRDIAEAG HSVEIRDAGQ VEAEGLCEGR DLVLFGCSTW
     GDDEIELQDD FIHLYESLEA TGAGKGRAAC FGCGDSSYTY FCGPVDAIEE RLSGLGADIV
     ADSLKIDGDP RTMRDDVSAW AGRVVTAL
//
ID   FLAV_ECO57              Reviewed;         176 AA.
AC   P61951; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 21.
DE   Flavodoxin-1.
GN   Name=fldA; OrderedLocusNames=Z0832, ECs0715;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE005174; AAG55007.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34138.1; -; Genomic_DNA.
DR   PIR; C85568; C85568.
DR   PIR; C90718; C90718.
DR   SMR; P61951; 2-176.
DR   GenomeReviews; BA000007_GR; ECs0715.
DR   GenomeReviews; AE005174_GR; Z0832.
DR   KEGG; ece:Z0832; -.
DR   KEGG; ecs:ECs0715; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171624.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ECOL6              Reviewed;         176 AA.
AC   P61950; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 21.
DE   Flavodoxin-1.
GN   Name=fldA; OrderedLocusNames=c_0771;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE014075; AAN79244.1; ALT_INIT; Genomic_DNA.
DR   SMR; P61950; 2-176.
DR   GenomeReviews; AE014075_GR; c_0771.
DR   KEGG; ecc:c0771; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171623.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ECOLI              Reviewed;         176 AA.
AC   P61949; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-MAR-2007, entry version 39.
DE   Flavodoxin-1.
GN   Name=fldA; OrderedLocusNames=b0684, JW0671;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RX   MEDLINE=91154129; PubMed=1999390;
RA   Osborne C., Chen L.-M., Matthews R.G.;
RT   "Isolation, cloning, mapping, and nucleotide sequencing of the gene
RT   encoding flavodoxin in Escherichia coli.";
RL   J. Bacteriol. 173:1729-1737(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RX   MEDLINE=95050480; PubMed=7961651;
RA   Jenkins C.M., Waterman M.R.;
RT   "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli
RT   support bovine cytochrome P450c17 hydroxylase activities.";
RL   J. Biol. Chem. 269:27401-27408(1994).
RN   [6]
RP   FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN.
RX   PubMed=9730838; DOI=10.1021/bi9808565;
RA   Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.;
RT   "The mechanism of adenosylmethionine-dependent activation of
RT   methionine synthase: a rapid kinetic analysis of intermediates in
RT   reductive methylation of Cob(II)alamin enzyme.";
RL   Biochemistry 37:12649-12658(1998).
RN   [7]
RP   STRUCTURE BY NMR.
RX   MEDLINE=97234567; PubMed=9119004;
RA   Ponstingl H., Otting G.;
RT   "NMR assignments, secondary structure and hydration of oxidized
RT   Escherichia coli flavodoxin.";
RL   Eur. J. Biochem. 244:384-399(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=98078562; PubMed=9416602;
RA   Hoover D.M., Ludwig M.L.;
RT   "A flavodoxin that is required for enzyme activation: the structure of
RT   oxidized flavodoxin from Escherichia coli at 1.8-A resolution.";
RL   Protein Sci. 6:2525-2537(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M59426; AAA23789.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73778.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35333.1; -; Genomic_DNA.
DR   PIR; A37319; A37319.
DR   PDB; 1AG9; X-ray; A/B=1-176.
DR   PDB; 1AHN; X-ray; @=1-176.
DR   IntAct; P61949; -.
DR   ECO2DBASE; A019.0; 6TH EDITION.
DR   GenomeReviews; U00096_GR; b0684.
DR   GenomeReviews; AP009048_GR; JW0671.
DR   KEGG; ecj:JW0671; -.
DR   KEGG; eco:b0684; -.
DR   EchoBASE; EB0314; -.
DR   EcoGene; EG10318; fldA.
DR   BioCyc; EcoCyc:FLAVODOXIN1-MONOMER; -.
DR   LinkHub; P61949; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171622.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   STRAND        3      7
FT   STRAND       10     12
FT   HELIX        13     25
FT   TURN         27     29
FT   STRAND       30     34
FT   HELIX        35     37
FT   HELIX        40     44
FT   STRAND       47     52
FT   TURN         57     59
FT   HELIX        63     72
FT   STRAND       81     87
FT   TURN         90     95
FT   HELIX        99    108
FT   TURN        109    112
FT   STRAND      132    134
FT   STRAND      137    143
FT   TURN        145    147
FT   TURN        149    151
FT   HELIX       152    167
FT   HELIX       169    172
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ENTAG              Reviewed;         177 AA.
AC   P28579;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   31-OCT-2006, entry version 40.
DE   Flavodoxin.
GN   Name=nifF;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OG   Plasmid pEA3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pantoea.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=333;
RX   MEDLINE=91217003; PubMed=1708766;
RA   Kreutzer R., Dayananda S., Klingmueller W.;
RT   "Cotranscription of the electron transport protein genes nifJ and nifF
RT   in Enterobacter agglomerans 333.";
RL   J. Bacteriol. 173:3252-3256(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=333;
RA   Schwickerath O.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M38221; AAA23385.1; -; Genomic_DNA.
DR   EMBL; X99694; CAA68010.1; -; Genomic_DNA.
DR   EMBL; X78558; CAA55301.1; -; Genomic_DNA.
DR   PIR; A39414; A39414.
DR   HSSP; P10340; 1D03.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Nitrogen fixation; Plasmid;
KW   Transport.
FT   CHAIN         1    177       Flavodoxin.
FT                                /FTId=PRO_0000171631.
FT   DOMAIN        4    173       Flavodoxin-like.
SQ   SEQUENCE   177 AA;  19581 MW;  3D54F95F7EC60B41 CRC64;
     MATIGIFFGS DTGQTRKVAK LIHQKLDGIA DAPLDVRRAT REQFLSYPVL LLGTPTLGDG
     ELPGVEAGSQ YDSWQEFTNT LSEADLTGKT VALFGLGDQL NYSKNFVSAM RILYDLVIAR
     GACVVGNWPR EGYKFSFSAA LLENNEFVGL PLDQENQYDL TEERIDSWLE KLKPAVL
//
ID   FLAV_HAEIN              Reviewed;         174 AA.
AC   P44562;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 50.
DE   Flavodoxin.
GN   Name=fldA; OrderedLocusNames=HI0191;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; L42023; AAC21860.1; -; Genomic_DNA.
DR   PIR; C64053; C64053.
DR   HSSP; P23243; 1AHN.
DR   SMR; P44562; 2-173.
DR   GenomeReviews; L42023_GR; HI0191.
DR   KEGG; hin:HI0191; -.
DR   TIGR; HI0191; -.
DR   BioCyc; HINF71421:HI0191-MONOMER; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    174       Flavodoxin.
FT                                /FTId=PRO_0000171633.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   174 AA;  19627 MW;  5E95E895F04BF3F8 CRC64;
     MAIVGLFYGS DTGNTENIAK QIQKQLGSDL IDIRDIAKSS KEDIEAYDFL LFGIPTWYYG
     EAQADWDDFF PTLEEIDFTD KLVGIFGCGD QEDYADYFCD AIGTVRDIIE PHGAIVVGNW
     PTEGYNFEAS KALLEDGTFI GLCIDEDRQP ELTAERVEKW CKQIYDEMCL AELA
//
ID   FLAV_HELPY              Reviewed;         164 AA.
AC   O25776;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   20-MAR-2007, entry version 46.
DE   Flavodoxin.
GN   Name=fldA; OrderedLocusNames=HP_1161;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE000511; AAD08207.1; -; Genomic_DNA.
DR   PIR; A64665; A64665.
DR   PDB; 2BMV; X-ray; A=1-164.
DR   GenomeReviews; AE000511_GR; HP_1161.
DR   KEGG; hpy:HP1161; -.
DR   TIGR; HP_1161; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Transport.
FT   CHAIN         1    164       Flavodoxin.
FT                                /FTId=PRO_0000171634.
FT   DOMAIN        4    160       Flavodoxin-like.
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     26
FT   STRAND       28     33
FT   HELIX        34     36
FT   HELIX        39     42
FT   STRAND       46     55
FT   TURN         56     58
FT   HELIX        62     68
FT   HELIX        74     77
FT   STRAND       79     86
FT   TURN         89     91
FT   TURN         96     98
FT   HELIX        99    107
FT   STRAND      110    112
FT   STRAND      116    118
FT   STRAND      133    139
FT   TURN        141    143
FT   HELIX       145    147
FT   HELIX       148    159
FT   TURN        160    162
SQ   SEQUENCE   164 AA;  17492 MW;  EBAD44D97964608C CRC64;
     MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VVDVAKASKE QFNSFTKVIL VAPTAGAGDL
     QTDWEDFLGT LEASDFATKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG
     YHFEASKAVE GGKFVGLVID EDNQDDLTDE RISKWVEQVK GSFA
//
ID   FLAV_KLEPN              Reviewed;         176 AA.
AC   O07026;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   31-OCT-2006, entry version 35.
DE   Flavodoxin.
GN   Name=fldA;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 13883 / DSM 30104 / IFO 14940 / NCIMB 13281 / NCTC 9633;
RX   MEDLINE=97417492; PubMed=9272865; DOI=10.1016/S0378-1119(97)00168-6;
RA   Achenbach L.A., Genova E.G.;
RT   "Transcriptional regulation of a second flavodoxin gene from
RT   Klebsiella pneumoniae.";
RL   Gene 194:235-240(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-176.
RC   STRAIN=ATCC 13883 / DSM 30104 / IFO 14940 / NCIMB 13281 / NCTC 9633;
RX   MEDLINE=97208874; PubMed=9055816; DOI=10.1016/S0378-1119(96)00642-7;
RA   Achenbach L.A., Yang W.;
RT   "The fur gene from Klebsiella pneumoniae: characterization, genomic
RT   organization and phylogenetic analysis.";
RL   Gene 185:201-207(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- INDUCTION: By low iron conditions and by heat shock. Iron
CC       regulation is mediated through the fur protein.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; U67169; AAB65080.1; -; Genomic_DNA.
DR   EMBL; L23871; AAB51076.1; -; Genomic_DNA.
DR   HSSP; P23243; 1AHN.
DR   SMR; O07026; 2-176.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    176       Flavodoxin.
FT                                /FTId=PRO_0000171636.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19765 MW;  C40E5F80287D3636 CRC64;
     MAIIGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAHDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTNERVEKW VKQVAEELHL EEIKNA
//
ID   FLS_MATIN               Reviewed;         291 AA.
AC   O04395;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   31-OCT-2006, entry version 40.
DE   Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23)
DE   (EC 1.14.11.9) (FLS) (Fragment).
OS   Matthiola incana (Common stock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Matthiola.
OX   NCBI_TaxID=3724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower bud, and Petal;
RA   Henkel J., Forkmann G.;
RT   "Cloning and expression of a flavonol synthase gene from common stock
RT   (Matthiola incana).";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; AF001391; AAB58800.1; -; mRNA.
DR   HSSP; Q96323; 1GP6.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN        <1    291       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067295.
FT   METAL       175    175       Iron (By similarity).
FT   METAL       177    177       Iron (By similarity).
FT   METAL       231    231       Iron (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   291 AA;  33430 MW;  6B8E4E3D2834720A CRC64;
     QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR
     SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA
     RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING
     LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT
     RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S
//
ID   FLAV_MEGEL              Reviewed;         137 AA.
AC   P00321;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-MAR-2007, entry version 50.
DE   Flavodoxin.
OS   Megasphaera elsdenii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Acidaminococcaceae;
OC   Megasphaera.
OX   NCBI_TaxID=907;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   MEDLINE=73197809; PubMed=4711610;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "The primary structure of Peptostreptococcus elsdenii flavodoxin.";
RL   J. Biol. Chem. 248:4354-4366(1973).
RN   [2]
RP   SEQUENCE REVISION TO 78-82.
RX   MEDLINE=74277393; PubMed=4843143;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "Correction of the amino acid sequence of Peptostreptococcus elsdenii
RT   flavodoxin.";
RL   J. Biol. Chem. 249:4397-4397(1974).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-41 AND 136-137.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   MEDLINE=72062407; PubMed=5126921; DOI=10.1021/bi00792a009;
RA   Tanaka M., Haniu M., Matsueda G., Yasunobu K.T., Mayhew S., Massey V.;
RT   "Amino- and carboxyl-terminal amino acid sequences of the
RT   Peptostreptococcus eisdenii and Clostridium pasteurianum
RT   flavodoxins.";
RL   Biochemistry 10:3041-3046(1971).
RN   [4]
RP   STRUCTURE BY NMR.
RX   MEDLINE=90276429; PubMed=2161759;
RA   van Mierlo C.P.M., Mueller F., Vervoort J.;
RT   "Secondary and tertiary structure characteristics of Megasphaera
RT   elsdenii flavodoxin in the reduced state as determined by two-
RT   dimensional 1H NMR.";
RL   Eur. J. Biochem. 189:589-600(1990).
RN   [5]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91071190; PubMed=2253614;
RA   van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F.,
RA   Berendsen H.J.C., de Vlieg J.;
RT   "Tertiary structure of two-electron reduced Megasphaera elsdenii
RT   flavodoxin and some implications, as determined by two-dimensional 1H-
RT   NMR and restrained molecular dynamics.";
RL   Eur. J. Biochem. 194:185-198(1990).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   PIR; A92137; FXME.
DR   PDB; 2FZ5; NMR; A=1-137.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    137       Flavodoxin.
FT                                /FTId=PRO_0000171639.
FT   DOMAIN        2    137       Flavodoxin-like.
FT   STRAND        2      6
FT   STRAND        9     11
FT   HELIX        12     26
FT   STRAND       31     35
FT   HELIX        41     45
FT   STRAND       48     53
FT   TURN         58     60
FT   HELIX        64     74
FT   HELIX        75     77
FT   STRAND       82     91
FT   HELIX        95    106
FT   STRAND      110    123
FT   HELIX       126    135
SQ   SEQUENCE   137 AA;  14550 MW;  86BD744412D6F869 CRC64;
     MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE
     ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM
     PDNAPECKEL GEAAAKA
//
ID   FLAV_NOSSM              Reviewed;          35 AA.
AC   P35707;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   31-OCT-2006, entry version 30.
DE   Flavodoxin (Fragment).
OS   Nostoc sp. (strain MAC).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=35822;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   HSSP; P11241; 1RCF.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Direct protein sequencing; Electron transport; Flavoprotein; FMN;
KW   Transport.
FT   CHAIN         1    >35       Flavodoxin.
FT                                /FTId=PRO_0000171640.
FT   DOMAIN        4    >35       Flavodoxin-like.
FT   NON_TER      35     35
SQ   SEQUENCE   35 AA;  3820 MW;  B6EEB5CA7A45DDA6 CRC64;
     SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID
//
ID   FLS_PETHY               Reviewed;         348 AA.
AC   Q07512;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   06-MAR-2007, entry version 43.
DE   Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23)
DE   (EC 1.14.11.9) (FLS).
GN   Name=FL;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Old Glory Blue; TISSUE=Petal;
RX   MEDLINE=94108485; PubMed=7904213;
RA   Holton T.A., Brugliera F., Tanaka Y.;
RT   "Cloning and expression of flavonol synthase from Petunia hybrida.";
RL   Plant J. 4:1003-1010(1993).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest level during the first
CC       stage of flower development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; Z22543; CAA80264.1; -; mRNA.
DR   PIR; S33510; S33510.
DR   HSSP; Q96323; 1GP6.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   InterPro; IPR002283; IPN_synth.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    348       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067296.
FT   METAL       234    234       Iron (By similarity).
FT   METAL       236    236       Iron (By similarity).
FT   METAL       290    290       Iron (By similarity).
SQ   SEQUENCE   348 AA;  39427 MW;  B39E1E4381DE6379 CRC64;
     MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL
     RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP
     GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR
     EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI
     TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR
     MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ
//
ID   FLAV_RHOCA              Reviewed;         182 AA.
AC   P52967;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 36.
DE   Flavodoxin.
GN   Name=nifF;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis;
RX   MEDLINE=96272272; PubMed=8682802;
RA   Gennaro G., Huebner P., Sandmeier U., Yakunin A.F., Hallenbeck P.C.;
RT   "Cloning, characterization, and regulation of nifF from Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 178:3949-3952(1996).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; L42290; AAC05792.1; -; Genomic_DNA.
DR   HSSP; P11241; 1OBO.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    182       Flavodoxin.
FT                                /FTId=PRO_0000171641.
FT   DOMAIN        4    173       Flavodoxin-like.
SQ   SEQUENCE   182 AA;  19820 MW;  95452D6EA538243E CRC64;
     MAKIGLFFGS DTGTTRKIAK QIKDMFDDEV MAKPLNVNRA DVADFMAYDF LILGTPTLGD
     GQLPGLSANA ASESWEEFLP RIADQDFSGK TIALFGLGDQ VTYPLEFVNA LFFLHEFFSD
     RGANVVGRWP AKGYGFEDSL AVVEGEFLGL ALDQDNQAAL TPERLKGWLS LIAADFGLVL
     PA
//
ID   FLS_SOLTU               Reviewed;         349 AA.
AC   Q41452;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   06-MAR-2007, entry version 40.
DE   Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23)
DE   (EC 1.14.11.9) (FLS).
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pistil;
RX   MEDLINE=97177800; PubMed=9025306;
RA   van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A.,
RA   Schrauwen J.A.M., Wullems G.J.;
RT   "Regulation of flavonol biosynthesis during anther and pistil
RT   development, and during pollen tube growth in Solanum tuberosum.";
RL   Plant J. 11:105-113(1997).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Temporally expressed during flower
CC       development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
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DR   EMBL; X92178; CAA63092.1; -; mRNA.
DR   PIR; T07373; T07373.
DR   HSSP; Q96323; 1GP6.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   InterPro; IPR005123; 2OG-FeII_Oase.
DR   InterPro; IPR002283; IPN_synth.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
KW   Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    349       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067297.
FT   METAL       238    238       Iron (By similarity).
FT   METAL       240    240       Iron (By similarity).
FT   METAL       291    291       Iron (By similarity).
SQ   SEQUENCE   349 AA;  39728 MW;  ADBBC3F6B10A0E05 CRC64;
     MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI
     DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI
     AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA
     KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD
     MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT
     RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ
//
ID   FLAV_SYNP2              Reviewed;         170 AA.
AC   P31158;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   23-JAN-2007, entry version 39.
DE   Flavodoxin.
GN   Name=isiB;
OS   Synechococcus sp. (strain PCC 7002) (Agmenellum quadruplicatum).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92407507; PubMed=1527503;
RA   Leonhardt K.G., Straus N.A.;
RT   "An iron stress operon involved in photosynthetic electron transport
RT   in the marine cyanobacterium Synechococcus sp. PCC 7002.";
RL   J. Gen. Microbiol. 138:1613-1621(1992).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: By iron stress.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M88253; AAA27318.1; -; Genomic_DNA.
DR   HSSP; P10340; 1OFV.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171643.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   170 AA;  18479 MW;  FFBB605F69E701BA CRC64;
     MSKIGLFFGT QTGNTEELAQ AIQAAFGGSD IVELFDVAEV DIEALRDFDQ LIIGCPTWNV
     GELQSDWEAL YDDLDDVDFS GKTIAYFGAG DQVGYADNFQ DAMGVLEEKI TSLGGKTVGQ
     WPTAGYDHSE SKAERDGKFV GLAIDEDNQP ELTAERIQAW VAQLKPAFGL
//
ID   FLAV_SYNP7              Reviewed;         170 AA.
AC   P10340; Q31MZ8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   20-MAR-2007, entry version 64.
DE   Flavodoxin.
GN   Name=isiB; OrderedLocusNames=Synpcc7942_1541;
OS   Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88086879; PubMed=3121586;
RA   Laudenbach D.E., Reith M.E., Straus N.A.;
RT   "Isolation, sequence analysis, and transcriptional studies of the
RT   flavodoxin gene from Anacystis nidulans R2.";
RL   J. Bacteriol. 170:258-265(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-56, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=83216115; PubMed=6406674; DOI=10.1016/S0022-2836(83)80277-0;
RA   Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D.,
RA   Tanaka M., Yasunobu K.T.;
RT   "Structure of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 165:737-753(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   MEDLINE=20079529; PubMed=10610791; DOI=10.1006/jmbi.1999.3151;
RA   Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M.,
RA   Ludwig M.L.;
RT   "Refined structures of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 294:711-724(1999).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX   MEDLINE=20079530; PubMed=10610792; DOI=10.1006/jmbi.1999.3152;
RA   Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H.,
RA   Pattridge K.A., Ludwig M.L.;
RT   "Comparisons of wild-type and mutant flavodoxins from Anacystis
RT   nidulans. Structural determinants of the redox potentials.";
RL   J. Mol. Biol. 294:725-743(1999).
RN   [6]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91329335; PubMed=1907844; DOI=10.1021/bi00245a008;
RA   Clubb R.T., Thanabal V., Osborne C., Wagner G.;
RT   "1H and 15N resonance assignments of oxidized flavodoxin from
RT   Anacystis nidulans with 3D NMR.";
RL   Biochemistry 30:7718-7730(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: By iron stress.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M19116; AAA22050.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57571.1; -; Genomic_DNA.
DR   PDB; 1CZH; X-ray; A=1-170.
DR   PDB; 1CZK; X-ray; A=1-170.
DR   PDB; 1CZL; X-ray; A=1-170.
DR   PDB; 1CZN; X-ray; A=1-170.
DR   PDB; 1CZO; X-ray; A=1-170.
DR   PDB; 1CZR; X-ray; A=1-170.
DR   PDB; 1CZU; X-ray; A=1-170.
DR   PDB; 1D03; X-ray; A=1-170.
DR   PDB; 1D04; X-ray; A=1-170.
DR   PDB; 1OFV; X-ray; @=1-170.
DR   GenomeReviews; CP000100_GR; Synpcc7942_1541.
DR   KEGG; syf:Synpcc7942_1541; -.
DR   LinkHub; P10340; -.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171644.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   CONFLICT     55     55       C -> S (in Ref. 3).
FT   STRAND        3      7
FT   STRAND       10     12
FT   HELIX        13     25
FT   TURN         28     30
FT   STRAND       31     35
FT   HELIX        36     38
FT   HELIX        41     46
FT   STRAND       48     53
FT   TURN         58     60
FT   HELIX        64     69
FT   HELIX        70     75
FT   STRAND       82     88
FT   TURN         91     96
FT   HELIX       100    110
FT   TURN        111    113
FT   STRAND      120    122
FT   STRAND      137    143
FT   TURN        145    147
FT   HELIX       149    151
FT   HELIX       152    167
SQ   SEQUENCE   170 AA;  18778 MW;  7291AEF23DCA0345 CRC64;
     MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY LIIGCPTWNV
     GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ DAMGILEEKI SSLGSQTVGY
     WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP DLTKNRIKTW VSQLKSEFGL
//
ID   FLAV_SYNY3              Reviewed;         170 AA.
AC   P27319;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   23-JAN-2007, entry version 49.
DE   Flavodoxin.
GN   Name=isiB; OrderedLocusNames=sll0248;
OS   Synechocystis sp. (strain PCC 6803).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94320780; PubMed=8045418; DOI=10.1016/0378-1119(94)90342-5;
RA   Poncelet M.G.M., Cassier-Chauvat C.J.S., Chauvat F.R.L.;
RT   "Sequence of the flavodoxin-encoding gene from the cyanobacterium
RT   Synechocystis PCC6803.";
RL   Gene 145:153-154(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-42.
RX   MEDLINE=92338182; PubMed=1633177; DOI=10.1016/0167-4838(92)90465-P;
RA   Bottin H., Lagoutte B.;
RT   "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp
RT   PCC 6803.";
RL   Biochim. Biophys. Acta 1101:48-56(1992).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) are -433 mV and -238 mV;
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; Z27091; CAA81614.1; -; Genomic_DNA.
DR   EMBL; L25881; AAA27288.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17947.1; -; Genomic_DNA.
DR   PIR; S38632; S38632.
DR   HSSP; P10340; 1OFV.
DR   SMR; P27319; 3-165.
DR   GenomeReviews; BA000022_GR; sll0248.
DR   KEGG; syn:sll0248; -.
DR   BioCyc; SSP1148:SLL0248-MONOMER; -.
DR   GO; GO:0009767; P:photosynthetic electron transport; NAS:UniProtKB.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    170       Flavodoxin.
FT                                /FTId=PRO_0000171645.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   CONFLICT      2      2       Missing (in Ref. 3).
FT   CONFLICT     40     40       A -> AA (in Ref. 3).
SQ   SEQUENCE   170 AA;  18822 MW;  B2937F347796BBD9 CRC64;
     MTKIGLFYGT QTGNTETIAE LIQKEMGGDS VVDMMDISQA DVDDFRQYSC LIIGCPTWNV
     GELQSDWEGF YDQLDEIDFN GKKVAYFGAG DQVGYADNFQ DAMGILEEKI SGLGGKTVGF
     WPTAGYDFDE SKAVKNGKFV GLALDEDNQP ELTELRVKTW VSEIKPILQS
//
ID   FLAV_TREPA              Reviewed;         146 AA.
AC   O83895;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   06-MAR-2007, entry version 37.
DE   Flavodoxin.
GN   Name=fldA; OrderedLocusNames=TP_0925;
OS   Treponema pallidum.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE000520; AAC65882.1; -; Genomic_DNA.
DR   PIR; F71263; F71263.
DR   HSSP; P00322; 2FVX.
DR   GenomeReviews; AE000520_GR; TP_0925.
DR   KEGG; tpa:TP0925; -.
DR   TIGR; TP_0925; -.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171646.
FT   DOMAIN        4    145       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15793 MW;  398A7D7C8530F2CE CRC64;
     MAKVAVIFWS GTGHTETMAR CIVEGLNVGG AKADLFSVMD FDVGTFDSYD RFAFGCSAAG
     SEELESSEFE PFFTSIEGRL SGKKVALFGS YEWAGEGEGG EWMVNWVERC KAAGADVFEG
     KGEIAYDDPS EEAQASCKAF GERFAR
//
ID   FLAV_TRIEI              Reviewed;         171 AA.
AC   O52659; Q114Y7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   12-DEC-2006, entry version 33.
DE   Flavodoxin.
GN   Name=fld; OrderedLocusNames=Tery_1666;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-146.
RA   Lin S., Carpenter E.J.;
RT   "Identification of a gene encoding flavodoxin in the marine
RT   cyanobacterium Trichodesmium.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; CP000393; ABG50937.1; -; Genomic_DNA.
DR   EMBL; AF044318; AAC02683.1; -; Genomic_DNA.
DR   HSSP; P11241; 1RCF.
DR   SMR; O52659; 1-144.
DR   GenomeReviews; CP000393_GR; Tery_1666.
DR   InterPro; IPR010086; Flav_long.
DR   InterPro; IPR001226; Flavodoxin.
DR   InterPro; IPR008254; Flavodoxin_1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    171       Flavodoxin.
FT                                /FTId=PRO_0000171647.
FT   DOMAIN        4    166       Flavodoxin-like.
FT   CONFLICT      4      4       I -> M (in Ref. 2; AAC02683).
FT   CONFLICT      8      8       V -> F (in Ref. 2; AAC02683).
FT   CONFLICT    130    130       E -> V (in Ref. 2; AAC02683).
SQ   SEQUENCE   171 AA;  18742 MW;  677F643438653126 CRC64;
     MSKIGLFVGT TTGKTEEAAE KIKEEFGGDD VVTIHDISEA SPEDFDGYQN VIIGCPTWDV
     GELQSDWSGF YSEELDNVKF TGKKVAYFGT GDQIGYADNF QDAMGILEEK ITGLGGTTIG
     SWSTEGYDHE DSKAVKNGKF VGLALDDDNQ ADLTDERIKE WVKQLKTEFG V
//
ID   PAX1_HUMAN              Reviewed;         440 AA.
AC   P15863; Q642X9; Q6NTC0; Q9Y558;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 3.
DT   23-JAN-2007, entry version 69.
DE   Paired box protein Pax-1 (HUP48).
GN   Name=PAX1; Synonyms=HUP48;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N.,
RA   Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S.,
RA   Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
RT   "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT   of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 1-142.
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [5]
RP   VARIANT HIS-45.
RX   MEDLINE=97016531; PubMed=8863157;
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
CC   -!- FUNCTION: This protein is a transcriptional activator. It may play
CC       a role in the formation of segmented structures of the embryo. May
CC       play an important role in the normal development of the vertebral
CC       column (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15863-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15863-2; Sequence=VSP_012986, VSP_012987;
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY740018; AAU21037.1; -; Genomic_DNA.
DR   EMBL; AL035562; CAB46996.1; -; Genomic_DNA.
DR   EMBL; BC069134; AAH69134.1; -; mRNA.
DR   EMBL; X15044; CAA33146.1; ALT_INIT; Genomic_DNA.
DR   PIR; S06961; S06961.
DR   UniGene; Hs.349082; -.
DR   HSSP; Q02548; 1K78.
DR   SMR; P15863; 8-130.
DR   TRANSFAC; T00398; -.
DR   Ensembl; ENSG00000125813; Homo sapiens.
DR   KEGG; hsa:5075; -.
DR   HGNC; HGNC:8615; PAX1.
DR   MIM; 167411; gene.
DR   ArrayExpress; P15863; -.
DR   GermOnline; ENSG00000125813; Homo sapiens.
DR   RZPD-ProtExp; T1074; -.
DR   GO; GO:0001501; P:skeletal development; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Activator; Alternative splicing; Developmental protein; DNA-binding;
KW   Nuclear protein; Paired box; Polymorphism; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    440       Paired box protein Pax-1.
FT                                /FTId=PRO_0000050172.
FT   DOMAIN        4    130       Paired.
FT   VAR_SEQ     330    361       PSREGSLPAPAARPRTPSVAYTDCPSRPRPPR -> REGTD
FT                                RKPPSSGSKAPDALSSLHGLPIPASTS (in isoform
FT                                2).
FT                                /FTId=VSP_012986.
FT   VAR_SEQ     362    440       Missing (in isoform 2).
FT                                /FTId=VSP_012987.
FT   VARIANT      45     45       Q -> H (in a patient with neural tube
FT                                defects, but not clearly linked to the
FT                                disease).
FT                                /FTId=VAR_003787.
FT   CONFLICT      1      1       M -> A (in Ref. 4).
SQ   SEQUENCE   440 AA;  46295 MW;  500B7155C81616F9 CRC64;
     MEQTYGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY
     NETGSILPGA IGGSKPRVTT PNVVKHIRDY KQGDPGIFAW EIRDRLLADG VCDKYNVPSV
     SSISRILRNK IGSLAQPGPY EASKQPPSQP TLPYNHIYQY PYPSPVSPTG AKMGSHPGVP
     GTAGHVSIPR SWPSAHSVSN ILGIRTFMEQ TGALAGSEGT AYSPKMEDWA GVNRTAFPAT
     PAVNGLEKPA LEADIKYTQS ASTLSAVGGF LPACAYPASN QHGVYSAPGG GYLAPGPPWP
     PAQGPPLAPP GAGVAVHGGE LAAAMTFKHP SREGSLPAPA ARPRTPSVAY TDCPSRPRPP
     RGSSPRTRAR RERQADPGAQ VCAAAPAIGT GRIGGLAEEE ASAGPRGARP ASPQAQPCLW
     PDPPHFLYWS GFLGFSELGF
//
ID   PAX2_HUMAN              Reviewed;         416 AA.
AC   Q02962; Q15105; Q15110; Q15837;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   20-FEB-2007, entry version 77.
DE   Paired box protein Pax-2.
GN   Name=PAX2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96299768; PubMed=8661132; DOI=10.1006/geno.1996.0350;
RA   Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A.,
RA   Eccles M.R.;
RT   "Genomic structure of the human PAX2 gene.";
RL   Genomics 35:258-261(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=92338102; PubMed=1378753;
RA   Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K., Goodfellow P.J.,
RA   Reeve A.E.;
RT   "Expression of the PAX2 gene in human fetal kidney and Wilms' tumor.";
RL   Cell Growth Differ. 3:279-289(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
RX   MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292;
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
RC   TISSUE=Kidney cortex;
RA   Ward T.A., Nebel A., Eccles M.R.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   VARIANTS RCS GLU-THR-75 INS AND SER-76.
RX   MEDLINE=98430997; PubMed=9760197; DOI=10.1007/s004390050798;
RA   Devriendt K., Matthijs G., van Damme B., van Caesbroeck D.,
RA   Eccles M.R., Vanrenterghem Y., Fryns J.-P., Leys A.;
RT   "Missense mutation and hexanucleotide duplication in the PAX2 gene in
RT   two unrelated families with renal-coloboma syndrome (MIM 120330).";
RL   Hum. Genet. 103:149-153(1998).
RN   [6]
RP   VARIANT VAL-334.
RX   MEDLINE=21113232; PubMed=11180607;
RX   DOI=10.1002/1098-1004(200102)17:2<155::AID-HUMU16>3.0.CO;2-9;
RA   Gelb A.C., Manligas G.S., Gharaybeh S., Schimmenti L.A.;
RT   "Identification of two novel polymorphisms (g.903C>T and g.1544C>T) in
RT   the PAX2 gene.";
RL   Hum. Mutat. 17:155-155(2001).
RN   [7]
RP   VARIANT OMN 39-GLN-ARG-40 DEL.
RX   MEDLINE=21105676; PubMed=11168927;
RX   DOI=10.1046/j.1523-1755.2001.059002457.x;
RA   Salomon R., Tellier A.-L., Attie-Bitach T., Amiel J., Vekemans M.,
RA   Lyonnet S., Dureau P., Niaudet P., Gubler M.-C., Broyer M.;
RT   "PAX2 mutations in oligomeganephronia.";
RL   Kidney Int. 59:457-462(2001).
CC   -!- FUNCTION: Probable transcription factor that may have a role in
CC       kidney cell differentiation. Has a critical role in the
CC       development of the urogenital tract, the eyes, and the CNS.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q02962-1; Sequence=Displayed;
CC       Name=2; Synonyms=Fetal kidney;
CC         IsoId=Q02962-2; Sequence=VSP_002346;
CC       Name=3;
CC         IsoId=Q02962-3; Sequence=VSP_002345;
CC   -!- TISSUE SPECIFICITY: Expressed in primitive cells of the kidney,
CC       ureter, eye, ear and central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Mainly in fetal kidney and juvenile
CC       nephrogenic rests.
CC   -!- DISEASE: Defects in PAX2 are the cause of renal-coloboma syndrome
CC       (RCS) [MIM:120330]; also known as papillorenal syndrome or optic
CC       nerve coloboma with renal disease. RCS is an autosomal dominant
CC       disease characterized by the association of renal hypoplasia,
CC       vesicoureteral reflux and dysplasia of the retina and optic disk.
CC   -!- DISEASE: Defects in PAX2 may be responsible for isolated renal
CC       hypoplasia as observed in oligomeganephronia (OMN). OMN is a rare
CC       congenital and usually sporadic anomaly characterized by bilateral
CC       renal hypoplasia, with a reduced number of enlarged nephrons and
CC       without urinary tract abnormalities.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: NAME=PAX2 mutation db;
CC       URL="http://www.hgu.mrc.ac.uk/Softdata/PAX2/".
CC   -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX2ID41642ch10q24.html".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=PAX2".
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DR   EMBL; U45255; AAC63385.1; -; Genomic_DNA.
DR   EMBL; U45245; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45246; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45247; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45248; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45249; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45250; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45251; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45253; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45254; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; M89470; AAA60024.1; -; mRNA.
DR   EMBL; L09747; AAC41711.1; -; Genomic_DNA.
DR   EMBL; L09748; AAC41711.1; JOINED; Genomic_DNA.
DR   EMBL; L09746; AAC41711.1; JOINED; Genomic_DNA.
DR   EMBL; L25597; AAA36417.1; -; mRNA.
DR   PIR; A49008; A49008.
DR   UniGene; Hs.155644; -.
DR   HSSP; Q02548; 1K78.
DR   SMR; Q02962; 19-142.
DR   TRANSFAC; T01823; -.
DR   Ensembl; ENSG00000075891; Homo sapiens.
DR   KEGG; hsa:5076; -.
DR   HGNC; HGNC:8616; PAX2.
DR   MIM; 120330; phenotype.
DR   MIM; 167409; gene.
DR   ArrayExpress; Q02962; -.
DR   GermOnline; ENSG00000075891; Homo sapiens.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Disease mutation; DNA-binding; Nuclear protein; Paired box;
KW   Polymorphism; Transcription; Transcription regulation.
FT   CHAIN         1    416       Paired box protein Pax-2.
FT                                /FTId=PRO_0000050175.
FT   DOMAIN       16    142       Paired.
FT   VAR_SEQ     206    228       Missing (in isoform 3).
FT                                /FTId=VSP_002345.
FT   VAR_SEQ     364    416       GSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRS
FT                                APAARAAAYDRH -> EAAVGPSSSLMSKPGRKLAEVPPCV
FT                                QPTGASSPATRTATPSTRPTTRLGDSATPPY (in
FT                                isoform 2).
FT                                /FTId=VSP_002346.
FT   VARIANT      39     40       Missing (in OMN; with bilateral
FT                                coloboma).
FT                                /FTId=VAR_012442.
FT   VARIANT      75     75       T -> TET (in RCS).
FT                                /FTId=VAR_003788.
FT   VARIANT      76     76       G -> S (in RCS).
FT                                /FTId=VAR_003789.
FT   VARIANT     334    334       A -> V.
FT                                /FTId=VAR_012443.
FT   CONFLICT     15     16       PG -> R (in Ref. 3).
SQ   SEQUENCE   416 AA;  44734 MW;  88A42F5D8307F80E CRC64;
     MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA
     EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND
     PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS
     QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL
     DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG
     MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRSAPAARA AAYDRH
//
ID   PAX3_HUMAN              Reviewed;         479 AA.
AC   P23760; Q16448;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   20-MAR-2007, entry version 86.
DE   Paired box protein Pax-3 (HUP2).
GN   Name=PAX3; Synonyms=HUP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 197-479.
RX   MEDLINE=95301273; PubMed=7782066; DOI=10.1016/0888-7543(95)80076-X;
RA   Macina R.A., Barr F.G., Galili N., Riethman H.C.;
RT   "Genomic organization of the human PAX3 gene: DNA sequence analysis of
RT   the region disrupted in alveolar rhabdomyosarcoma.";
RL   Genomics 26:1-8(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 30-195.
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-392, AND VARIANTS WS1 LEU-45
RP   AND ASP-99.
RX   MEDLINE=95072569; PubMed=7981674; DOI=10.1093/hmg/3.7.1069;
RA   Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E.,
RA   Kunze J., Sperling K., Strachan T., Read A.P.;
RT   "PAX3 gene structure and mutations: close analogies between
RT   Waardenburg syndrome and the Splotch mouse.";
RL   Hum. Mol. Genet. 3:1069-1074(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (PAX3A AND PAX3B).
RX   MEDLINE=94171226; PubMed=7545913; DOI=10.1007/BF00212021;
RA   Tsukamoto K., Nakamura Y., Niikawa N.;
RT   "Isolation of two isoforms of the PAX3 gene transcripts and their
RT   tissue-specific alternative expression in human adult tissues.";
RL   Hum. Genet. 93:270-274(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-319, AND CHROMOSOMAL TRANSLOCATION WITH
RP   NCOA1.
RX   PubMed=15313887; DOI=10.1158/0008-5472.CAN-04-0844;
RA   Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J.,
RA   Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.;
RT   "Gene expression signatures identify rhabdomyosarcoma subtypes and
RT   detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1.";
RL   Cancer Res. 64:5539-5545(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 56-74, AND VARIANT WS1 63-ALA--ILE-67 DEL.
RX   MEDLINE=92168113; PubMed=1347148; DOI=10.1038/355635a0;
RA   Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R.,
RA   Gruss P., Strachan T.;
RT   "Waardenburg's syndrome patients have mutations in the human homologue
RT   of the Pax-3 paired box gene.";
RL   Nature 355:635-636(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 265-319.
RA   Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.B.,
RA   Wilcox E.R.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   CHROMOSOMAL TRANSLOCATION WITH FOXO1A.
RX   MEDLINE=94100975; PubMed=8275086; DOI=10.1038/ng1193-230;
RA   Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S.,
RA   Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G.;
RT   "Fusion of a fork head domain gene to PAX3 in the solid tumour
RT   alveolar rhabdomyosarcoma.";
RL   Nat. Genet. 5:230-235(1993).
RN   [9]
RP   INTERACTION WITH DAXX.
RX   MEDLINE=99321757; PubMed=10393185; DOI=10.1093/emboj/18.13.3702;
RA   Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.;
RT   "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated
RT   repressor hDaxx.";
RL   EMBO J. 18:3702-3711(1999).
RN   [10]
RP   INVOLVEMENT IN WS1.
RX   PubMed=1303193; DOI=10.1093/hmg/1.4.243;
RA   Morell R., Friedman T.B., Moeljopawiro S., Hartono S., Asher J.H. Jr.;
RT   "A frameshift mutation in the HuP2 paired domain of the probable human
RT   homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1
RT   in an Indonesian family.";
RL   Hum. Mol. Genet. 1:243-247(1992).
RN   [11]
RP   VARIANT WS1 LEU-50.
RX   MEDLINE=92168114; PubMed=1347149; DOI=10.1038/355637a0;
RA   Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.;
RT   "An exonic mutation in the HuP2 paired domain gene causes
RT   Waardenburg's syndrome.";
RL   Nature 355:637-638(1992).
RN   [12]
RP   VARIANT WS1 ALA-81.
RX   MEDLINE=93258399; PubMed=8490648; DOI=10.1038/ng0193-26;
RA   Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R.,
RA   Strachan T.;
RT   "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and
RT   type 2.";
RL   Nat. Genet. 3:26-30(1993).
RN   [13]
RP   VARIANTS WS3 HIS-47 AND WS1 LEU-56.
RX   MEDLINE=93190976; PubMed=8447316;
RA   Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K.,
RA   Baldwin C.T.;
RT   "Mutations in the paired domain of the human PAX3 gene cause Klein-
RT   Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I
RT   (WS-I).";
RL   Am. J. Hum. Genet. 52:455-462(1993).
RN   [14]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE=95135456; PubMed=7833953;
RA   Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.;
RT   "A single base pair substitution within the paired box of PAX3 in an
RT   individual with Waardenburg syndrome type 1 (WS1).";
RL   Hum. Mutat. 4:227-228(1994).
RN   [15]
RP   VARIANTS WS1 PHE-265 AND GLY-271.
RX   MEDLINE=95126143; PubMed=7825605;
RA   Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B.,
RA   San Agustin T.B., Wilcox E.R.;
RT   "Further elucidation of the genomic structure of PAX3, and
RT   identification of two different point mutations within the PAX3
RT   homeobox that cause Waardenburg syndrome type 1 in two families.";
RL   Am. J. Hum. Genet. 56:75-83(1995).
RN   [16]
RP   VARIANT WS3 PHE-84.
RX   MEDLINE=95243235; PubMed=7726174;
RA   Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.;
RT   "Homozygosity for Waardenburg syndrome.";
RL   Am. J. Hum. Genet. 56:1173-1178(1995).
RN   [17]
RP   VARIANTS WS1 MET-60; GLU-85 AND SER-238.
RX   MEDLINE=96042708; PubMed=8533800;
RA   Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.;
RT   "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new
RT   mutations and review of the literature.";
RL   Am. J. Med. Genet. 58:115-122(1995).
RN   [18]
RP   VARIANTS WS1 MET-78; ALA-81; ASP-99; CYS-266; CYS-270; CYS-271 AND
RP   HIS-271, AND VARIANT LYS-315.
RX   MEDLINE=96154685; PubMed=8589691; DOI=10.1093/hmg/4.11.2131;
RA   Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D.,
RA   Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W.,
RA   Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R.,
RA   Read A.P.;
RT   "The mutational spectrum in Waardenburg syndrome.";
RL   Hum. Mol. Genet. 4:2131-2137(1995).
RN   [19]
RP   VARIANTS WS1 ARG-48; CYS-270 AND HIS-271, AND VARIANTS LYS-273 AND
RP   LYS-315.
RX   PubMed=8845842; DOI=10.1093/hmg/5.4.497;
RA   Pandya A., Xia X.-J., Landa B.L., Arnos K.S., Israel J., Lloyd J.,
RA   James A.L., Diehl S.R., Blanton S.H., Nance W.E.;
RT   "Phenotypic variation in Waardenburg syndrome: mutational
RT   heterogeneity, modifier genes or polygenic background?";
RL   Hum. Mol. Genet. 5:497-502(1996).
RN   [20]
RP   VARIANT CDHS LYS-47.
RX   MEDLINE=96263735; PubMed=8664898;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:1<30::AID-HUMU4>3.3.CO;2-H;
RA   Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.;
RT   "Missense mutation in the paired domain of PAX3 causes craniofacial-
RT   deafness-hand syndrome.";
RL   Hum. Mutat. 7:30-35(1996).
RN   [21]
RP   VARIANT LYS-315.
RX   MEDLINE=97016531; PubMed=8863157;
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
RN   [22]
RP   VARIANT WS1 PHE-59.
RX   MEDLINE=97220597; PubMed=9067759;
RX   DOI=10.1002/(SICI)1098-1004(1997)9:2<177::AID-HUMU11>3.3.CO;2-Z;
RA   Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K.,
RA   Fukushima Y., Jinno Y., Niikawa N.;
RT   "Three novel PAX3 mutations observed in patients with Waardenburg
RT   syndrome type 1.";
RL   Hum. Mutat. 9:177-180(1997).
RN   [23]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE=98112449; PubMed=9452070;
RA   Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "Identification of two PAX3 mutations causing Waardenburg syndrome,
RT   one within the paired domain (M62V) and the other downstream of the
RT   homeodomain (Q282X).";
RL   Hum. Mutat. Suppl. 1:S145-S147(1998).
RN   [24]
RP   VARIANT WS1 HIS-391.
RX   MEDLINE=98200183; PubMed=9541113;
RA   Carey M.L., Friedman T.B., Asher J.H. Jr., Innis J.W.;
RT   "Septo-optic dysplasia and WS1 in the proband of a WS1 family
RT   segregating for a novel mutation in PAX3 exon 7.";
RL   J. Med. Genet. 35:248-250(1998).
RN   [25]
RP   VARIANT LYS-315.
RX   MEDLINE=98250826; PubMed=9584079; DOI=10.1006/mcpr.1997.0149;
RA   Wang C., Kim E., Attaie A., Smith T.N., Wilcox E.R., Lalwani A.K.;
RT   "A PAX3 polymorphism (T315K) in a family exhibiting Waardenburg
RT   syndrome type 2.";
RL   Mol. Cell. Probes 12:55-57(1998).
RN   [26]
RP   VARIANT WS1 ASN-59.
RA   Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A.,
RA   Schwartz E.I.;
RT   "A novel missense mutation Ile59Asn in the PAX3 gene in a family with
RT   Waardenburg syndrome type I.";
RL   Hum. Mutat. 13:85-85(1999).
RN   [27]
RP   VARIANT WS3 CYS-270.
RA   Bottani A., Antonarakis S.E., Blouin J.-L.;
RL   Unpublished observations (MAY-1999).
RN   [28]
RP   VARIANT WS1 LEU-73.
RX   MEDLINE=20243823; PubMed=10779847;
RX   DOI=10.1076/1381-6810(200003)21:1;1-I;FT025;
RA   Sotirova V.N., Rezaie T.M., Khoshsorour M.M., Sarfarazi M.;
RT   "Identification of a novel mutation in the paired domain of PAX3 in an
RT   Iranian family with waardenburg syndrome type I.";
RL   Ophthalmic Genet. 21:25-28(2000).
RN   [29]
RP   VARIANT WS1 MET-60, AND VARIANT WS3 HIS-90.
RX   MEDLINE=22829208; PubMed=12949970; DOI=10.1002/ajmg.a.20260;
RA   Wollnik B., Tukel T., Uyguner O., Ghanbari A., Kayserili H.,
RA   Emiroglu M., Yuksel-Apak M.;
RT   "Homozygous and heterozygous inheritance of PAX3 mutations causes
RT   different types of Waardenburg syndrome.";
RL   Am. J. Med. Genet. A 122:42-45(2003).
CC   -!- FUNCTION: Probable transcription factor associated with
CC       development of alveolar rhabdomyosarcoma.
CC   -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX7. Interacts
CC       with DAXX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Pax3;
CC         IsoId=P23760-1; Sequence=Displayed;
CC       Name=Pax3A;
CC         IsoId=P23760-2; Sequence=VSP_002355, VSP_002356;
CC       Name=Pax3B;
CC         IsoId=P23760-3; Sequence=VSP_002357, VSP_002358;
CC   -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome
CC       type I (WS1) [MIM:193500]. WS1 is an autosomal dominant disorder
CC       characterized by wide bridge of nose owing to lateral displacement
CC       of the inner canthus of each eye (dystopia canthorum), pigmentary
CC       disturbances such as frontal white blaze of hair, heterochromia of
CC       irides, white eyelashes, leukoderma and sensorineural deafness.
CC       The syndrome shows variable clinical expression and some affected
CC       individuals do not manifest hearing impairment.
CC   -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome
CC       type III (WS3) [MIM:148820]; also known as Klein-Waardenburg
CC       syndrome or Waardenburg syndrome with upper limb anomalies or
CC       white forelock with malformations. WS3 is a very rare autosomal
CC       dominant disorder, which shares many of the characteristics of
CC       WS1. Patients additionally present with musculoskeletal
CC       abnormalities.
CC   -!- DISEASE: Defects in PAX3 are the cause of craniofacial-deafness-
CC       hand syndrome (CDHS) [MIM:122880]. CDHS is thought to be an
CC       autosomal dominant disease which comprises absence or hypoplasia
CC       of the nasal bones, hypoplastic maxilla, small and short nose with
CC       thin nares, limited movement of the wrist, short palpebral
CC       fissures, ulnar deviation of the fingers, hypertelorism and
CC       profound sensory-neural deafness.
CC   -!- DISEASE: A chromosomal aberration involving PAX3 is a cause of
CC       rhabdomyosarcoma 2 (RMS2) [MIM:268220]; also known as alveolar
CC       rhabdomyosarcoma. Translocation (2;13)(q35;q14) with FOXO1A. The
CC       resulting protein is a transcriptional activator.
CC   -!- DISEASE: A chromosomal aberration involving PAX3 is a cause of
CC       rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1
CC       generates the NCOA1-PAX3 oncogene consisting of the N-terminus
CC       part of PAX3 and the C-terminus part of NCOA1. The fusion protein
CC       acts as a transcriptional activator. Rhabdomyosarcoma is the most
CC       common soft tissue carcinoma in childhood, representing 5-8% of
CC       all malignancies in children.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX3ID70ch2q35.html".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=PAX3".
CC   -----------------------------------------------------------------------
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DR   EMBL; U12263; AAA80573.1; -; Genomic_DNA.
DR   EMBL; U12259; AAA80574.1; -; Genomic_DNA.
DR   EMBL; U12258; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; U12260; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; U12262; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; X15043; CAA33145.1; -; Genomic_DNA.
DR   EMBL; X15252; CAA33145.1; JOINED; Genomic_DNA.
DR   EMBL; X15253; CAA33145.1; JOINED; Genomic_DNA.
DR   EMBL; Z29972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z29973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z29974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S69369; AAB30167.1; -; mRNA.
DR   EMBL; S69370; AAB30168.1; -; mRNA.
DR   EMBL; S83614; AAB21476.1; -; Genomic_DNA.
DR   EMBL; L10614; AAA91849.1; -; Genomic_DNA.
DR   PIR; I54276; I54276.
DR   PIR; I68547; I68547.
DR   PIR; S06960; S06960.
DR   UniGene; Hs.42146; -.
DR   HSSP; P06601; 1FJL.
DR   SMR; P23760; 38-161, 218-277.
DR   TRANSFAC; T00679; -.
DR   TRANSFAC; T01812; -.
DR   TRANSFAC; T01813; -.
DR   Ensembl; ENSG00000135903; Homo sapiens.
DR   KEGG; hsa:5077; -.
DR   HGNC; HGNC:8617; PAX3.
DR   MIM; 122880; phenotype.
DR   MIM; 148820; phenotype.
DR   MIM; 193500; phenotype.
DR   MIM; 268220; phenotype.
DR   MIM; 606597; gene.
DR   LinkHub; P23760; -.
DR   ArrayExpress; P23760; -.
DR   GermOnline; ENSG00000135903; Homo sapiens.
DR   GO; GO:0003700; F:transcription factor activity; TAS:ProtInc.
DR   GO; GO:0006915; P:apoptosis; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00027; PAIREDBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Alternative splicing; Chromosomal rearrangement; Deafness;
KW   Developmental protein; Disease mutation; DNA-binding; Homeobox;
KW   Nuclear protein; Paired box; Polymorphism; Proto-oncogene;
KW   Transcription; Transcription regulation; Waardenburg syndrome.
FT   CHAIN         1    479       Paired box protein Pax-3.
FT                                /FTId=PRO_0000050178.
FT   DOMAIN       34    161       Paired.
FT   DNA_BIND    219    278       Homeobox.
FT   SITE        319    320       Breakpoint for translocation to form
FT                                PAX3-NCOA1 oncogene.
FT   VAR_SEQ     196    215       ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRA
FT                                SAS (in isoform Pax3A).
FT                                /FTId=VSP_002355.
FT   VAR_SEQ     196    206       ASAPQSDEGSD -> GKALVSGVSSH (in isoform
FT                                Pax3B).
FT                                /FTId=VSP_002357.
FT   VAR_SEQ     207    479       Missing (in isoform Pax3B).
FT                                /FTId=VSP_002358.
FT   VAR_SEQ     216    479       Missing (in isoform Pax3A).
FT                                /FTId=VSP_002356.
FT   VARIANT      45     45       F -> L (in WS1).
FT                                /FTId=VAR_003790.
FT   VARIANT      47     47       N -> H (in WS3).
FT                                /FTId=VAR_003791.
FT   VARIANT      47     47       N -> K (in CDHS).
FT                                /FTId=VAR_003792.
FT   VARIANT      48     48       G -> R (in WS1).
FT                                /FTId=VAR_017533.
FT   VARIANT      50     50       P -> L (in WS1; important hearing loss).
FT                                /FTId=VAR_003793.
FT   VARIANT      56     56       R -> L (in WS1; associated with
FT                                meningomyelocele).
FT                                /FTId=VAR_003794.
FT   VARIANT      59     59       I -> F (in WS1).
FT                                /FTId=VAR_003795.
FT   VARIANT      59     59       I -> N (in WS1).
FT                                /FTId=VAR_003796.
FT   VARIANT      60     60       V -> M (in WS1).
FT                                /FTId=VAR_003797.
FT   VARIANT      62     62       M -> V (in WS1).
FT                                /FTId=VAR_003798.
FT   VARIANT      63     67       Missing (in WS1).
FT                                /FTId=VAR_003799.
FT   VARIANT      73     73       S -> L (in WS1).
FT                                /FTId=VAR_013640.
FT   VARIANT      78     78       V -> M (in WS1).
FT                                /FTId=VAR_017534.
FT   VARIANT      81     81       G -> A (in WS1; originally classified as
FT                                Waardenburg syndrome type 2).
FT                                /FTId=VAR_003800.
FT   VARIANT      84     84       S -> F (in WS3).
FT                                /FTId=VAR_003801.
FT   VARIANT      85     85       K -> E (in WS1).
FT                                /FTId=VAR_003802.
FT   VARIANT      90     90       Y -> H (in WS3).
FT                                /FTId=VAR_017535.
FT   VARIANT      99     99       G -> D (in WS1).
FT                                /FTId=VAR_003803.
FT   VARIANT     238    238       F -> S (in WS1).
FT                                /FTId=VAR_003804.
FT   VARIANT     265    265       V -> F (in WS1).
FT                                /FTId=VAR_003805.
FT   VARIANT     266    266       W -> C (in WS1).
FT                                /FTId=VAR_017536.
FT   VARIANT     270    270       R -> C (in WS1 and WS3).
FT                                /FTId=VAR_013619.
FT   VARIANT     271    271       R -> C (in WS1).
FT                                /FTId=VAR_017537.
FT   VARIANT     271    271       R -> G (in WS1).
FT                                /FTId=VAR_003806.
FT   VARIANT     271    271       R -> H (in WS1; associated with Lys-273
FT                                in one family).
FT                                /FTId=VAR_017538.
FT   VARIANT     273    273       R -> K (associated with His-271 in one
FT                                Waardenburg syndrome type I family).
FT                                /FTId=VAR_017539.
FT   VARIANT     315    315       T -> K (in dbSNP:rs2234675).
FT                                /FTId=VAR_003807.
FT   VARIANT     391    391       Q -> H (in WS1).
FT                                /FTId=VAR_013641.
FT   CONFLICT    108    108       Missing (in Ref. 5).
SQ   SEQUENCE   479 AA;  52968 MW;  8AFCA674E3ACB4FE CRC64;
     MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE
     YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES
     EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER
     THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP
     TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR
     HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE
     PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF
//
ID   PAX4_HUMAN              Reviewed;         350 AA.
AC   O43316; O95161; Q6B0H0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   20-FEB-2007, entry version 61.
DE   Paired box protein Pax-4.
GN   Name=PAX4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98102804; PubMed=9439631; DOI=10.1006/bbrc.1997.7935;
RA   Matsushita T., Yamaoka T., Otsuka S., Moritani M., Matsumoto T.,
RA   Itakura M.;
RT   "Molecular cloning of mouse paired-box-containing gene (Pax-4) from an
RT   islet beta cell line and deduced sequence of human Pax-4.";
RL   Biochem. Biophys. Res. Commun. 242:176-180(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
RX   MEDLINE=98424228; PubMed=9753306;
RA   Tao T., Wasson J., Bernal-Mizrachi E., Behn P.S., Chayen S.,
RA   Duprat L., Meyer J., Glaser B., Permutt M.A.;
RT   "Isolation and characterization of the human PAX4 gene.";
RL   Diabetes 47:1650-1653(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ALTERNATIVE SPLICING (ISOFORM PAX4V).
RC   TISSUE=Insulinoma;
RX   MEDLINE=21164695; PubMed=11263967; DOI=10.1006/bbrc.2001.4552;
RA   Miyamoto T., Kakizawa T., Ichikawa K., Nishio S., Kajikawa S.,
RA   Hashizume K.;
RT   "Expression of dominant negative form of PAX4 in human insulinoma.";
RL   Biochem. Biophys. Res. Commun. 282:34-40(2001).
CC   -!- FUNCTION: Plays an important role in the differentiation and
CC       development of pancreatic islet beta cells. Transcriptional
CC       repressor that binds to a common element in the glucagon, insulin
CC       and somatostatin promoters. Competes with PAX6 for this same
CC       promoter binding site. The Pax4v isoform appears to be a dominant
CC       negative form antagonizing PAX4 transcriptional activity.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Pax4;
CC         IsoId=O43316-1; Sequence=Displayed;
CC       Name=Pax4V;
CC         IsoId=O43316-2; Sequence=VSP_002359, VSP_002360;
CC       Name=3;
CC         IsoId=O43316-3; Sequence=VSP_012925;
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
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DR   EMBL; AB008913; BAA24506.1; -; mRNA.
DR   EMBL; AF043978; AAD02289.1; ALT_INIT; mRNA.
DR   EMBL; BC074761; AAH74761.1; ALT_INIT; mRNA.
DR   PIR; JC5828; JC5828.
DR   UniGene; Hs.129706; -.
DR   HSSP; P26367; 6PAX.
DR   SMR; O43316; 7-135.
DR   TRANSFAC; T02982; -.
DR   KEGG; hsa:5078; -.
DR   HGNC; HGNC:8618; PAX4.
DR   MIM; 167413; gene.
DR   ArrayExpress; O43316; -.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00027; PAIREDBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Alternative splicing; Developmental protein; Differentiation;
KW   DNA-binding; Homeobox; Nuclear protein; Paired box; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    350       Paired box protein Pax-4.
FT                                /FTId=PRO_0000050180.
FT   DOMAIN        5    131       Paired.
FT   DNA_BIND    170    229       Homeobox.
FT   REGION      278    350       Transcription repression.
FT   VAR_SEQ     239    257       Missing (in isoform Pax4V).
FT                                /FTId=VSP_002359.
FT   VAR_SEQ     258    350       QSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKA
FT                                CLKPCWDCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAG
FT                                KATPTHFSHWP -> AVPWQCAHSSPACPGTTGSLLLSAVL
FT                                GNSTRKVSE (in isoform Pax4V).
FT                                /FTId=VSP_002360.
FT   VAR_SEQ     305    350       DCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAGKATPTH
FT                                FSHWP -> GHLPPQPNSLDSGLLCLPCPSSHCPLASLSGS
FT                                QALLWPGCPLLYGLE (in isoform 3).
FT                                /FTId=VSP_012925.
SQ   SEQUENCE   350 AA;  37833 MW;  2C2343AF16AEAAAC CRC64;
     MHQDGISSMN QLGGLFVNGR PLPLDTRQQI VRLAVSGMRP CDISRILKVS NGCVSKILGR
     YYRTGVLEPK GIGGSKPRLA TPPVVARIAQ LKGECPALFA WEIQRQLCAE GLCTQDKTPS
     VSSINRVLRA LQEDQGLPCT RLRSPAVLAP AVLTPHSGSE TPRGTHPGTG HRNRTIFSPS
     QAEALEKEFQ RGQYPDSVAR GKLATATSLP EDTVRVWFSN RRAKWRRQEK LKWEMQLPGA
     SQGLTVPRVA PGIISAQQSP GSVPTAALPA LEPLGPSCYQ LCWATAPERC LSDTPPKACL
     KPCWDCGSFL LPVIAPSCVD VAWPCLDASL AHHLIGGAGK ATPTHFSHWP
//
ID   PAX5_HUMAN              Reviewed;         391 AA.
AC   Q02548; O75933;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   20-MAR-2007, entry version 65.
DE   Paired box protein Pax-5 (B-cell-specific transcription factor)
DE   (BSAP).
GN   Name=PAX5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92387536; PubMed=1516825;
RA   Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P.,
RA   Maurer-Fogy I., Busslinger M.;
RT   "Pax-5 encodes the transcription factor BSAP and is expressed in B
RT   lymphocytes, the developing CNS, and adult testis.";
RL   Genes Dev. 6:1589-1607(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 62-197.
RX   MEDLINE=98416211; PubMed=9742255; DOI=10.1093/nar/26.19.4497;
RA   Verkoczy L.K., Berinstein N.L.;
RT   "Isolation of genes negatively or positively co-expressed with human
RT   recombination activating gene 1 (RAG1) by differential display PCR (DD
RT   RT-PCR).";
RL   Nucleic Acids Res. 26:4497-4507(1998).
RN   [3]
RP   INTERACTION WITH TLE4.
RX   MEDLINE=20271869; PubMed=10811620; DOI=10.1093/emboj/19.10.2292;
RA   Eberhard D., Jimenez G., Heavey B., Busslinger M.;
RT   "Transcriptional repression by Pax5 (BSAP) through interaction with
RT   corepressors of the Groucho family.";
RL   EMBO J. 19:2292-2303(2000).
CC   -!- FUNCTION: May play an important role in B-cell differentiation as
CC       well as neural development and spermatogenesis. Involved in the
CC       regulation of the CD19 gene, a B-lymphoid-specific target gene.
CC   -!- SUBUNIT: Interacts with DAXX (By similarity). Binds DNA as a
CC       monomer. Binds TLE4.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed at early B-cell differentiation, in
CC       the developing CNS and in adult testis.
CC   -!- PTM: O-glycosylated (Probable).
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX5ID62.htm".
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DR   EMBL; M96944; AAA58397.1; -; mRNA.
DR   EMBL; AF080573; AAC35286.1; -; mRNA.
DR   PIR; A44063; A44063.
DR   UniGene; Hs.591091; -.
DR   PDB; 1K78; X-ray; A/E/I=1-149.
DR   PDB; 1MDM; X-ray; A=1-149.
DR   IntAct; Q02548; -.
DR   TRANSFAC; T00070; -.
DR   Ensembl; ENSG00000196092; Homo sapiens.
DR   KEGG; hsa:5079; -.
DR   HGNC; HGNC:8619; PAX5.
DR   HPA; CAB001449; -.
DR   MIM; 167414; gene.
DR   LinkHub; Q02548; -.
DR   ArrayExpress; Q02548; -.
DR   GermOnline; ENSG00000196092; Homo sapiens.
DR   GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   3D-structure; Developmental protein; Differentiation; DNA-binding;
KW   Glycoprotein; Neurogenesis; Nuclear protein; Paired box;
KW   Spermatogenesis; Transcription; Transcription regulation.
FT   CHAIN         1    391       Paired box protein Pax-5.
FT                                /FTId=PRO_0000050183.
FT   DOMAIN       16    142       Paired.
FT   CONFLICT     99     99       I -> F (in Ref. 2).
FT   CONFLICT    141    143       TKV -> PKL (in Ref. 2).
FT   HELIX        35     46
FT   HELIX        51     58
FT   HELIX        62     75
FT   STRAND       89     91
FT   HELIX        93    105
FT   HELIX       111    120
FT   TURN        126    128
FT   HELIX       132    140
SQ   SEQUENCE   391 AA;  42149 MW;  DB37E6EACD9F993A CRC64;
     MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA
     ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS
     ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV
     FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP
     IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF
     PNPGLLGSPY YYSAAARGAA PPAAATAYDR H
//
ID   PAX6_HUMAN              Reviewed;         422 AA.
AC   P26367; Q6N006; Q99413;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   20-MAR-2007, entry version 91.
DE   Paired box protein Pax-6 (Oculorhombin) (Aniridia type II protein).
GN   Name=PAX6; Synonyms=AN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92103673; PubMed=1684738; DOI=10.1016/0092-8674(91)90284-6;
RA   Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T.,
RA   van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M.,
RA   Royer-Pokora B., Collins F.S., Swaroop A., Strong L.C., Saunders G.F.;
RT   "Positional cloning and characterization of a paired box- and
RT   homeobox-containing gene from the aniridia region.";
RL   Cell 67:1059-1074(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94258210; PubMed=1345175; DOI=10.1038/ng1192-232;
RA   Glaser T., Walton D.S., Maas R.L.;
RT   "Genomic structure, evolutionary conservation and aniridia mutations
RT   in the human PAX6 gene.";
RL   Nat. Genet. 2:232-239(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM PAX6).
RA   Liu J., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A).
RC   TISSUE=Cerebellum;
RG   The German cDNA consortium;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 5A).
RA   Wilkinson J.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   ALTERNATIVE SPLICING, AND DNA-BINDING.
RX   MEDLINE=95047352; PubMed=7958875;
RA   Epstein J.A., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L.;
RT   "Two independent and interactive DNA-binding subdomains of the Pax6
RT   paired domain are regulated by alternative splicing.";
RL   Genes Dev. 8:2022-2034(1994).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-136.
RX   PubMed=10346815;
RA   Xu H.E., Rould M.A., Xu W., Epstein J.A., Maas R.L., Pabo C.O.;
RT   "Crystal structure of the human Pax-6 paired domain-DNA complex
RT   reveals specific roles for the linker region and carboxyl-terminal
RT   subdomain in DNA binding.";
RL   Genes Dev. 13:1263-1275(1999).
RN   [9]
RP   REVIEW ON VARIANTS.
RX   MEDLINE=98141676; PubMed=9482572;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:2<93::AID-HUMU1>3.3.CO;2-J;
RA   Prosser J., van Heyningen V.;
RT   "PAX6 mutations reviewed.";
RL   Hum. Mutat. 11:93-108(1998).
RN   [10]
RP   VARIANT AN2 TRP-208.
RX   MEDLINE=93372853; PubMed=8364574; DOI=10.1093/hmg/2.7.915;
RA   Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D.,
RA   Fekete G., van Heyningen V.;
RT   "PAX6 mutations in aniridia.";
RL   Hum. Mol. Genet. 2:915-920(1993).
RN   [11]
RP   VARIANT PETERS ANOMALY GLY-26.
RX   MEDLINE=94214497; PubMed=8162071; DOI=10.1038/ng0294-168;
RA   Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D.,
RA   Adams R.J., Punnet H.H., van Heyningen V.;
RT   "Mutations at the PAX6 locus are found in heterogeneous anterior
RT   segment malformations including Peters' anomaly.";
RL   Nat. Genet. 6:168-173(1994).
RN   [12]
RP   VARIANTS FOVEAL HYPOPLASIA CYS-125 AND CYS-128.
RX   MEDLINE=96225435; PubMed=8640214; DOI=10.1038/ng0696-141;
RA   Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.;
RT   "PAX6 missense mutation in isolated foveal hypoplasia.";
RL   Nat. Genet. 13:141-142(1996).
RN   [13]
RP   VARIANT AN2 ARG-87, AND VARIANT GLY-26.
RX   MEDLINE=97227282; PubMed=9147640; DOI=10.1093/hmg/6.3.381;
RA   Tang H.K., Chao L.-Y., Saunders G.F.;
RT   "Functional analysis of paired box missense mutations in the PAX6
RT   gene.";
RL   Hum. Mol. Genet. 6:381-386(1997).
RN   [14]
RP   VARIANT AN2 22-PRO--ARG-26 DEL.
RX   MEDLINE=97428347; PubMed=9281415; DOI=10.1006/mcpr.1997.0117;
RA   Axton R., Hanson I.M., Love J., Seawright A., Prosser J.,
RA   van Heyningen V.;
RT   "Combined SSCP/heteroduplex analysis in the screening for PAX6
RT   mutations.";
RL   Mol. Cell. Probes 11:287-292(1997).
RN   [15]
RP   VARIANT AN2 TRP-18.
RX   MEDLINE=99006892; PubMed=9792406;
RX   DOI=10.1002/(SICI)1098-1004(1998)12:5<304::AID-HUMU3>3.3.CO;2-Y;
RA   Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V.,
RA   Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.;
RT   "Ten novel mutations found in Aniridia.";
RL   Hum. Mutat. 12:304-313(1998).
RN   [16]
RP   VARIANT EYE MALFORMATIONS ARG-422.
RX   MEDLINE=98199717; PubMed=9538891;
RA   Azuma N., Yamada M.;
RT   "Missense mutation at the C-terminus of the PAX6 gene in ocular
RT   anterior segment anomalies.";
RL   Invest. Ophthalmol. Vis. Sci. 39:828-830(1998).
RN   [17]
RP   VARIANTS AN2 SER-17; VAL-29; GLN-44 AND HIS-178.
RX   MEDLINE=99072581; PubMed=9856761;
RA   Azuma N., Hotta Y., Tanaka H., Yamada M.;
RT   "Missense mutations in the PAX6 gene in aniridia.";
RL   Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998).
RN   [18]
RP   VARIANT EYE MALFORMATIONS ASP-53.
RX   MEDLINE=99375017; PubMed=10441571; DOI=10.1086/302529;
RA   Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.;
RT   "Missense mutation in the alternative splice region of the PAX6 gene
RT   in eye anomalies.";
RL   Am. J. Hum. Genet. 65:656-663(1999).
RN   [19]
RP   ALTERNATIVE SPLICING, AND VARIANTS AN2 SER-42; LEU-53; PRO-63; GLU-79
RP   AND GLN-208.
RX   MEDLINE=99250762; PubMed=10234503; DOI=10.1038/sj.ejhg.5200308;
RA   Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.;
RT   "Mutational analysis of PAX6: 16 novel mutations including 5 missense
RT   mutations with a mild aniridia phenotype.";
RL   Eur. J. Hum. Genet. 7:274-286(1999).
RN   [20]
RP   VARIANTS AN2 PRO-33 AND PRO-43, VARIANT FOVEAL HYPOPLASIA VAL-64, AND
RP   VARIANT ECTOPIA PUPILLAE ASP-126.
RX   MEDLINE=99135896; PubMed=9931324; DOI=10.1093/hmg/8.2.165;
RA   Hanson I.M., Churchill A., Love J., Axton R., Moore T., Clarke M.,
RA   Meire F., van Heyningen V.;
RT   "Missense mutations in the most ancient residues of the PAX6 paired
RT   domain underlie a spectrum of human congenital eye malformations.";
RL   Hum. Mol. Genet. 8:165-172(1999).
RN   [21]
RP   VARIANTS AN2 SER-29; ARG-119 AND ALA-353.
RA   Wildhardt G.;
RL   Unpublished observations (APR-1999).
RN   [22]
RP   VARIANT AN2 37-ALA--PRO-39 DEL.
RA   Saunders G.F.;
RL   Unpublished observations (AUG-1999).
RN   [23]
RP   VARIANT NYSTAGMUS ARG-118.
RX   MEDLINE=20410622; PubMed=10955655; DOI=10.1007/s004170000124;
RA   Sonoda S., Isashiki Y., Tabata Y., Kimura K., Kakiuchi T., Ohba N.;
RT   "A novel PAX6 gene mutation (P118R) in a family with congenital
RT   nystagmus associated with a variant form of aniridia.";
RL   Graefes Arch. Clin. Exp. Ophthalmol. 238:552-558(2000).
RN   [24]
RP   VARIANTS AN2 GLN-375 AND ARG-422.
RX   MEDLINE=21205761; PubMed=11309364; DOI=10.1093/hmg/10.9.911;
RA   Singh S., Chao L.-Y., Mishra R., Davies J., Saunders G.F.;
RT   "Missense mutation at the C-terminus of PAX6 negatively modulates
RT   homeodomain function.";
RL   Hum. Mol. Genet. 10:911-918(2001).
RN   [25]
RP   VARIANT MORNING GLORY DISK ANOMALY SER-68, VARIANT OCULAR COLOBOMA
RP   SER-258, VARIANT PETERS ANOMALY PRO-363, AND VARIANTS OPTIC NERVE
RP   HYPOPLASIA/APLASIA ILE-292; ARG-378; VAL-381 AND ALA-391.
RX   MEDLINE=22633032; PubMed=12721955; DOI=10.1086/375555;
RA   Azuma N., Yamaguchi Y., Handa H., Tadokoro K., Asaka A., Kawase E.,
RA   Yamada M.;
RT   "Mutations of the PAX6 gene detected in patients with a variety of
RT   optic-nerve malformations.";
RL   Am. J. Hum. Genet. 72:1565-1570(2003).
CC   -!- FUNCTION: Transcription factor with important functions in the
CC       development of the eye, nose, central nervous system and pancreas.
CC       Required for the differentiation of pancreatic islet alpha cells
CC       (By similarity). Competes with PAX4 in binding to a common element
CC       in the glucagon, insulin and somatostatin promoters (By
CC       similarity). Isoform 5a appears to function as a molecular switch
CC       that specifies target genes.
CC   -!- INTERACTION:
CC       P63168:Dynll1 (xeno); NbExp=2; IntAct=EBI-747278, EBI-349121;
CC       Q9NSC5:HOMER3; NbExp=2; IntAct=EBI-747278, EBI-748420;
CC       Q96F44:TRIM11; NbExp=2; IntAct=EBI-747278, EBI-851809;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P26367-1; Sequence=Displayed;
CC       Name=5a; Synonyms=Pax6-5a;
CC         IsoId=P26367-2; Sequence=VSP_002366;
CC       Name=3; Synonyms=Pax6-5A,6*;
CC         IsoId=P26367-3; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Fetal eye, brain, spinal cord and olfactory
CC       epithelium. Isoform 5a is less abundant than the PAX6 shorter
CC       form.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing eye and brain.
CC   -!- DISEASE: Defects in PAX6 are the cause of aniridia type II (AN2)
CC       [MIM:106210]. AN2 is a bilateral panocular disorder characterized
CC       by complete or partial absence of the iris, absence of the fovea
CC       and malformations of the lens and anterior chamber. Severe age-
CC       related corneal degeneration is a frequent complication which
CC       contributes to a poor visual prognostis in aniridia. About one
CC       third of the cases are sporadic, and two thirds are familial, with
CC       autosomal dominant inheritance and high penetrance. Nearly one
CC       third of sporadic AN patients develop Wilms tumor in association
CC       with genitourinary anomalies and mental retardation (WAGR
CC       syndrome) as a consequence of heterozygous (sub)microscopic
CC       deletions of chromosome 11p13.
CC   -!- DISEASE: Defects in PAX6 are a cause of Peters anomaly
CC       [MIM:604229]. Peters anomaly consists of a central corneal
CC       leukoma, absence of the posterior corneal stroma and Descemet
CC       membrane, and a variable degree of iris and lenticular attachments
CC       to the central aspect of the posterior cornea.
CC   -!- DISEASE: Defects in PAX6 are a cause of ectopia pupillae
CC       [MIM:129750]. It is a congenital eye malformation in which the
CC       pupils are displaced from their normal central position.
CC   -!- DISEASE: Defects in PAX6 are a cause of foveal hypoplasia
CC       [MIM:136520]. Foveal hypoplasia can be isolated or associated with
CC       presenile cataract. Inheritance is autosomal dominant.
CC   -!- DISEASE: Defects in PAX6 are a cause of autosomal dominant
CC       keratitis [MIM:148190]. It is an eye disorder characterized by
CC       corneal opacification and vascularization, and by foveal
CC       hypoplasia.
CC   -!- DISEASE: Defects in PAX6 are a cause of ocular coloboma
CC       [MIM:120200]; also known as uveoretinal coloboma or coloboma of
CC       iris, choroid and retina. Ocular colobomas are a set of
CC       malformations resulting from abnormal morphogenesis of the optic
CC       cup and stalk, and the fusion of the fetal fissure (optic
CC       fissure). Severe colobomatous malformations may cause as much as
CC       10% of the childhood blindness. The clinical presentation of
CC       ocular coloboma is variable. Some individuals may present with
CC       minimal defects in the anterior iris leaf without other ocular
CC       defects. More complex malformations create a combination of iris,
CC       uveoretinal and/or optic nerve defects without or with
CC       microphthalmia or even anophthalmia.
CC   -!- DISEASE: Defects in PAX6 are a cause of coloboma of optic nerve
CC       [MIM:120430].
CC   -!- DISEASE: Defects in PAX6 are a cause of bilateral optic nerve
CC       hypoplasia [MIM:165550]; also known as bilateral optic nerve
CC       aplasia. Inheritance is autosomal dominant.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: NAME=Human PAX6 allelic variant database web site;
CC       URL="http://pax6.hgu.mrc.ac.uk/".
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=PAX6".
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DR   EMBL; M77844; AAA59963.1; -; mRNA.
DR   EMBL; M77844; AAA59962.1; -; mRNA.
DR   EMBL; M93650; AAA36416.1; -; mRNA.
DR   EMBL; AY047583; AAK95849.1; -; mRNA.
DR   EMBL; BX640762; CAE45868.1; -; mRNA.
DR   EMBL; Z95332; CAG38363.1; -; Genomic_DNA.
DR   EMBL; Z83307; CAG38363.1; JOINED; Genomic_DNA.
DR   EMBL; Z83307; CAG38087.1; -; Genomic_DNA.
DR   EMBL; Z95332; CAG38087.1; JOINED; Genomic_DNA.
DR   EMBL; BC011953; AAH11953.1; -; mRNA.
DR   PIR; A56674; A56674.
DR   UniGene; Hs.591993; -.
DR   PDB; 2CUE; NMR; A=211-277.
DR   PDB; 6PAX; X-ray; A=4-136.
DR   IntAct; P26367; -.
DR   TRANSFAC; T01122; -.
DR   TRANSFAC; T01814; -.
DR   Ensembl; ENSG00000007372; Homo sapiens.
DR   KEGG; hsa:5080; -.
DR   H-InvDB; HIX0009529; -.
DR   HGNC; HGNC:8620; PAX6.
DR   MIM; 106210; phenotype.
DR   MIM; 120200; phenotype.
DR   MIM; 120430; phenotype.
DR   MIM; 129750; phenotype.
DR   MIM; 136520; phenotype.
DR   MIM; 148190; phenotype.
DR   MIM; 165550; phenotype.
DR   MIM; 604229; phenotype.
DR   MIM; 607108; gene.
DR   ArrayExpress; P26367; -.
DR   GermOnline; ENSG00000007372; Homo sapiens.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:transcription factor activity; TAS:ProtInc.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0001654; P:eye development; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00027; PAIREDBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   3D-structure; Alternative splicing; Developmental protein;
KW   Differentiation; Disease mutation; DNA-binding; Homeobox;
KW   Nuclear protein; Paired box; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    422       Paired box protein Pax-6.
FT                                /FTId=PRO_0000050185.
FT   DOMAIN        4    130       Paired.
FT   DNA_BIND    210    269       Homeobox.
FT   COMPBIAS    131    209       Gln/Gly-rich.
FT   COMPBIAS    279    422       Pro/Ser/Thr-rich.
FT   VAR_SEQ      47     47       Q -> QTHADAKVQVLDNQN (in isoform 5a).
FT                                /FTId=VSP_002366.
FT   VARIANT      17     17       N -> S (in AN2).
FT                                /FTId=VAR_003808.
FT   VARIANT      18     18       G -> W (in AN2 and Peters anomaly).
FT                                /FTId=VAR_003809.
FT   VARIANT      22     26       Missing (in AN2; sporadic form).
FT                                /FTId=VAR_008693.
FT   VARIANT      26     26       R -> G (in Peters anomaly).
FT                                /FTId=VAR_003810.
FT   VARIANT      29     29       I -> S (in AN2; sporadic form).
FT                                /FTId=VAR_008694.
FT   VARIANT      29     29       I -> V (in AN2).
FT                                /FTId=VAR_003811.
FT   VARIANT      33     33       A -> P (in AN2; sporadic form).
FT                                /FTId=VAR_008695.
FT   VARIANT      37     39       Missing (in AN2; sporadic form).
FT                                /FTId=VAR_008696.
FT   VARIANT      42     42       I -> S (in AN2; mild).
FT                                /FTId=VAR_008697.
FT   VARIANT      43     43       S -> P (in AN2; sporadic form).
FT                                /FTId=VAR_008698.
FT   VARIANT      44     44       R -> Q (in AN2).
FT                                /FTId=VAR_003812.
FT   VARIANT      53     53       V -> D (in Peters anomaly, congenital
FT                                cataract and foveal hypoplasia; Japanese
FT                                pedigrees).
FT                                /FTId=VAR_008700.
FT   VARIANT      53     53       V -> L (in AN2; mild).
FT                                /FTId=VAR_008699.
FT   VARIANT      63     63       T -> P (in AN2; mild).
FT                                /FTId=VAR_008701.
FT   VARIANT      64     64       G -> V (in foveal hypoplasia; associated
FT                                with presenile cataract syndrome).
FT                                /FTId=VAR_008702.
FT   VARIANT      68     68       P -> S (in morning glory disk anomaly;
FT                                significant impairment of transcriptional
FT                                activation ability).
FT                                /FTId=VAR_017540.
FT   VARIANT      79     79       A -> E (in AN2; mild).
FT                                /FTId=VAR_008703.
FT   VARIANT      87     87       I -> R (in AN2; loss of activity).
FT                                /FTId=VAR_003813.
FT   VARIANT     118    118       P -> R (in nystagmus associated with a
FT                                variant form of aniridia).
FT                                /FTId=VAR_015065.
FT   VARIANT     119    119       S -> R (in AN2; sporadic form).
FT                                /FTId=VAR_008704.
FT   VARIANT     125    125       R -> C (in foveal hypoplasia; isolated).
FT                                /FTId=VAR_017541.
FT   VARIANT     126    126       V -> D (in ectopia pupillae).
FT                                /FTId=VAR_008705.
FT   VARIANT     128    128       R -> C (in foveal hypoplasia; isolated).
FT                                /FTId=VAR_003814.
FT   VARIANT     178    178       Q -> H (in AN2).
FT                                /FTId=VAR_003815.
FT   VARIANT     208    208       R -> Q (in AN2; mild).
FT                                /FTId=VAR_008706.
FT   VARIANT     208    208       R -> W (in AN2).
FT                                /FTId=VAR_003816.
FT   VARIANT     258    258       F -> S (in ocular coloboma; significant
FT                                impairment of transcriptional activation
FT                                ability).
FT                                /FTId=VAR_017542.
FT   VARIANT     292    292       S -> I (in bilateral optic nerve
FT                                hypoplasia; significant impairment of
FT                                transcriptional activation ability).
FT                                /FTId=VAR_017543.
FT   VARIANT     353    353       S -> A (in AN2; familial form).
FT                                /FTId=VAR_008707.
FT   VARIANT     363    363       S -> P (in Peters anomaly).
FT                                /FTId=VAR_017544.
FT   VARIANT     375    375       P -> Q (in AN2; reduced DNA binding
FT                                ability).
FT                                /FTId=VAR_015066.
FT   VARIANT     378    378       Q -> R (in optic nerve aplasia).
FT                                /FTId=VAR_017545.
FT   VARIANT     381    381       M -> V (in bilateral optic nerve
FT                                hypoplasia).
FT                                /FTId=VAR_017546.
FT   VARIANT     391    391       T -> A (in bilateral optic nerve
FT                                aplasia).
FT                                /FTId=VAR_017547.
FT   VARIANT     422    422       Q -> R (in AN2 and ocular anterior
FT                                segment anomalies; loss of DNA binding
FT                                ability).
FT                                /FTId=VAR_008708.
FT   CONFLICT    317    317       R -> L (in Ref. 1).
FT   CONFLICT    369    369       Y -> C (in Ref. 4).
FT   STRAND        6      8
FT   STRAND       14     16
FT   HELIX        23     34
FT   HELIX        39     46
FT   HELIX        50     63
FT   STRAND       77     79
FT   HELIX        81     93
FT   HELIX        99    108
FT   TURN        114    116
FT   HELIX       120    133
FT   HELIX       219    229
FT   HELIX       237    246
FT   HELIX       251    275
SQ   SEQUENCE   422 AA;  46683 MW;  C33CDD2C1B13C397 CRC64;
     MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY
     YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV
     SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ
     EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR
     ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP
     QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT
     SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR
     LQ
//
ID   PAX7_HUMAN              Reviewed;         520 AA.
AC   P23759;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   20-FEB-2007, entry version 74.
DE   Paired box protein Pax-7 (HUP1).
GN   Name=PAX7; Synonyms=HUP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=97480728; PubMed=9339373; DOI=10.1006/geno.1997.4915;
RA   Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B.,
RA   Horst J.;
RT   "The genomic organization and the full coding region of the human PAX7
RT   gene.";
RL   Genomics 45:168-174(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I.,
RA   Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-467 (ISOFORM LONG).
RX   MEDLINE=95075634; PubMed=7527137; DOI=10.1093/nar/22.22.4574;
RA   Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.;
RT   "Molecular cloning and characterization of a human PAX-7 cDNA
RT   expressed in normal and neoplastic myocytes.";
RL   Nucleic Acids Res. 22:4574-4582(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 30-195 (ISOFORM SHORT).
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
CC   -!- FUNCTION: Probable transcription factor. May have a role in
CC       myogenesis.
CC   -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts
CC       with DAXX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P23759-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P23759-2; Sequence=VSP_002370;
CC   -!- DISEASE: A chromosomal aberration involving PAX7 is a cause of
CC       rhabdomyosarcoma 2 (RMS2) [MIM:268220]; also known as alveolar
CC       rhabdomyosarcoma. Translocation t(1;13)(p36;q14) with FOXO1A. The
CC       resulting protein is a transcriptional activator.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X96743; CAA65520.1; -; mRNA.
DR   EMBL; X96744; CAA65521.1; -; Genomic_DNA.
DR   EMBL; X15042; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X15250; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X15251; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96745; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96746; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96747; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96748; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96744; CAA65522.1; -; Genomic_DNA.
DR   EMBL; X15042; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X15250; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X15251; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96745; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96746; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96747; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96748; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; AL021528; CAA16432.1; -; Genomic_DNA.
DR   EMBL; Z35141; CAA84513.1; -; mRNA.
DR   PIR; S78502; S78502.
DR   UniGene; Hs.113253; -.
DR   HSSP; P06601; 1FJL.
DR   SMR; P23759; 38-163, 216-275.
DR   TRANSFAC; T00396; -.
DR   Ensembl; ENSG00000009709; Homo sapiens.
DR   KEGG; hsa:5081; -.
DR   HGNC; HGNC:8621; PAX7.
DR   MIM; 167410; gene.
DR   MIM; 268220; phenotype.
DR   ArrayExpress; P23759; -.
DR   GermOnline; ENSG00000009709; Homo sapiens.
DR   RZPD-ProtExp; Z0758; -.
DR   GO; GO:0003700; F:transcription factor activity; TAS:ProtInc.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00027; PAIREDBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Alternative splicing; Chromosomal rearrangement;
KW   Developmental protein; DNA-binding; Homeobox; Nuclear protein;
KW   Paired box; Proto-oncogene; Transcription; Transcription regulation.
FT   CHAIN         1    520       Paired box protein Pax-7.
FT                                /FTId=PRO_0000050194.
FT   DOMAIN       34    163       Paired.
FT   DNA_BIND    217    276       Homeobox.
FT   COMPBIAS    340    346       Poly-Ala.
FT   VAR_SEQ     151    152       Missing (in isoform Short).
FT                                /FTId=VSP_002370.
SQ   SEQUENCE   520 AA;  56896 MW;  3B0F8CC99D65699C CRC64;
     MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE
     YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG
     EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH
     YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL
     PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS
     YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS
     ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQSEC LVPWASPVPI
     PSPTPRASCL FMESYKVVSG WGMSISQMEK LKSSQMEQFT
//
ID   PAX9_HUMAN              Reviewed;         341 AA.
AC   P55771; Q99582; Q9UQR4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   06-FEB-2007, entry version 63.
DE   Paired box protein Pax-9.
GN   Name=PAX9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20461864; PubMed=10899593; DOI=10.1016/S0167-4781(00)00130-5;
RA   Hetzer-Egger C., Schorpp M., Boehm T.;
RT   "Evolutionary conservation of gene structures of the Pax1/9 gene
RT   family.";
RL   Biochim. Biophys. Acta 1492:517-521(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211.
RX   MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292;
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-339.
RC   TISSUE=Oesophagus;
RX   MEDLINE=97179475; PubMed=9021154; DOI=10.1007/s003359900351;
RA   Peters H., Schuster G., Neubueser A., Richter T., Hoefler H.;
RT   "Isolation of the Pax9 cDNA from adult human esophagus.";
RL   Mamm. Genome 8:62-64(1997).
RN   [5]
RP   VARIANT OLIGODENTIA SER-51.
RX   MEDLINE=22671556; PubMed=12786960;
RX   DOI=10.1034/j.1600-0722.2003.00036.x;
RA   Mostowska A., Kobielak A., Biedziak B., Trzeciak W.H.;
RT   "Novel mutation in the paired box sequence of PAX9 gene in a sporadic
RT   form of oligodontia.";
RL   Eur. J. Oral Sci. 111:272-276(2003).
CC   -!- FUNCTION: Transcription factor required for normal development of
CC       thymus, parathyroid glands, ultimobranchial bodies, teeth,
CC       skeletal elements of skull and larynx as well as distal limbs (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISEASE: Defects in PAX9 are a cause of oligodontia [MIM:604625].
CC       It is a form of familial or selective tooth agenesis. Oligodontia
CC       is defined as the agenesis of 6 or more permanent teeth without
CC       associated systemic disorders. Agenesis of one or more teeth
CC       constitutes one of the most common developmental anomalies in man.
CC       Reported incidences vary from 1.6% to 9.6%, excluding third molar
CC       (Wisdom tooth) agenesis, which occurs in 20% of the population.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX9ID41644ch14q12.html".
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ238381; CAB41533.1; -; Genomic_DNA.
DR   EMBL; AJ238382; CAB41533.1; JOINED; Genomic_DNA.
DR   EMBL; AJ238383; CAB41533.1; JOINED; Genomic_DNA.
DR   EMBL; BC001159; AAH01159.1; -; mRNA.
DR   EMBL; L09745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X92850; CAA63436.1; -; mRNA.
DR   UniGene; Hs.132576; -.
DR   HSSP; Q02548; 1K78.
DR   SMR; P55771; 8-130.
DR   TRANSFAC; T02986; -.
DR   Ensembl; ENSG00000198807; Homo sapiens.
DR   KEGG; hsa:5083; -.
DR   H-InvDB; HIX0011606; -.
DR   HGNC; HGNC:8623; PAX9.
DR   MIM; 167416; gene.
DR   MIM; 604625; phenotype.
DR   ArrayExpress; P55771; -.
DR   GermOnline; ENSG00000198807; Homo sapiens.
DR   RZPD-ProtExp; IOH4822; -.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR   InterPro; IPR009057; Homeodomain_like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
KW   Developmental protein; Disease mutation; DNA-binding; Nuclear protein;
KW   Paired box; Transcription; Transcription regulation.
FT   CHAIN         1    341       Paired box protein Pax-9.
FT                                /FTId=PRO_0000050203.
FT   DOMAIN        4    130       Paired.
FT   VARIANT      51     51       G -> S (in oligodontia).
FT                                /FTId=VAR_015698.
FT   CONFLICT    211    211       V -> G (in Ref. 3).
SQ   SEQUENCE   341 AA;  36310 MW;  F5E6B0BC991E7C1D CRC64;
     MEPAFGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY
     NETGSILPGA IGGSKPRVTT PTVVKHIRTY KQRDPGIFAW EIRDRLLADG VCDKYNVPSV
     SSISRILRNK IGNLAQQGHY DSYKQHQPTP QPALPYNHIY SYPSPITAAA AKVPTPPGVP
     AIPGSVAMPR TWPSSHSVTD ILGIRSITDQ VSDSSPYHSP KVEEWSSLGR NNFPAAAPHA
     VNGLEKGALE QEAKYGQAPN GLPAVGSFVS ASSMAPYPTP AQVSPYMTYS AAPSGYVAGH
     GWQHAGGTSL SPHNCDIPAS LAFKGMQAAR EGSHSVTASA L
//
ID   PAXI_HUMAN              Reviewed;         591 AA.
AC   P49023; O14970; O14971; O60360;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   20-FEB-2007, entry version 71.
DE   Paxillin.
GN   Name=PXN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX   MEDLINE=95197488; PubMed=7534286; DOI=10.1074/jbc.270.10.5039;
RA   Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S.,
RA   Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R.,
RA   Chen L.B., Griffin J.D.;
RT   "Molecular cloning of human paxillin, a focal adhesion protein
RT   phosphorylated by P210BCR/ABL.";
RL   J. Biol. Chem. 270:5039-5047(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA   Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA   Lathrop M., Cox R.D., Bell G.I.;
RT   "Transcription map of the 5cM region surrounding the hepatocyte
RT   nuclear factor-1a/MODY3 gene on chromosome 12.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA).
RC   TISSUE=Placenta;
RX   MEDLINE=97207310; PubMed=9054445; DOI=10.1074/jbc.272.11.7437;
RA   Mazaki Y., Hashimoto S., Sabe H.;
RT   "Monocyte cells and cancer cells express novel paxillin isoforms with
RT   different binding properties to focal adhesion proteins.";
RL   J. Biol. Chem. 272:7437-7444(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
RP   INTERACTION WITH ITGA4.
RX   PubMed=10604475; DOI=10.1038/45264;
RA   Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M.,
RA   Ginsberg M.H.;
RT   "Binding of paxillin to alpha4 integrins modifies integrin-dependent
RT   biological responses.";
RL   Nature 402:676-681(1999).
RN   [6]
RP   INTERACTION WITH GIT1.
RX   PubMed=10938112; DOI=10.1128/MCB.20.17.6354-6363.2000;
RA   Zhao Z.-S., Manser E., Loo T.-H., Lim L.;
RT   "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes
RT   focal complex disassembly.";
RL   Mol. Cell. Biol. 20:6354-6363(2000).
RN   [7]
RP   INTERACTION WITH DDEF2.
RX   MEDLINE=20214823; PubMed=10749932;
RA   Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.;
RT   "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an
RT   ADP-ribosylation factor GTPase-activating protein activity, is
RT   involved in paxillin recruitment to focal adhesions and cell
RT   migration.";
RL   Mol. Biol. Cell 11:1315-1327(2000).
RN   [8]
RP   PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
RX   MEDLINE=21634701; PubMed=11774284; DOI=10.1002/ijc.1609;
RA   Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H.,
RA   Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E.,
RA   Akedo H.;
RT   "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in
RT   MM1 cancer cell migration.";
RL   Int. J. Cancer 97:330-335(2002).
RN   [9]
RP   INTERACTION WITH RNF5.
RX   PubMed=12861019; DOI=10.1128/MCB.23.15.5331-5345.2003;
RA   Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S.,
RA   Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H.,
RA   Ronai Z.;
RT   "RNF5, a RING finger protein that regulates cell motility by targeting
RT   paxillin ubiquitination and altered localization.";
RL   Mol. Cell. Biol. 23:5331-5345(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16212419; DOI=10.1021/pr050134h;
RA   Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
RT   "Phosphoproteome analysis of HeLa cells using stable isotope labeling
RT   with amino acids in cell culture (SILAC).";
RL   J. Proteome Res. 4:1661-1671(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200;
RA   Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,
RA   Lauffenburger D.A., White F.M.;
RT   "Time-resolved mass spectrometry of tyrosine phosphorylation sites in
RT   the epidermal growth factor receptor signaling network reveals dynamic
RT   modules.";
RL   Mol. Cell. Proteomics 4:1240-1250(2005).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16094384; DOI=10.1038/nmeth776;
RA   Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,
RA   Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
RT   "Quantitative phosphoproteome analysis using a dendrimer conjugation
RT   chemistry and tandem mass spectrometry.";
RL   Nat. Methods 2:591-598(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, AND
RP   MASS SPECTROMETRY.
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
CC   -!- FUNCTION: Cytoskeletal protein involved in actin-membrane
CC       attachment at sites of cell adhesion to the extracellular matrix
CC       (focal adhesion).
CC   -!- SUBUNIT: Binds in vitro to vinculin as well as to the SH3 domain
CC       of c-SRC and, when tyrosine phosphorylated, to the SH2 domain of
CC       V-CRK. Isoform beta binds to focal adhesion kinase but weakly to
CC       vinculin. Isoform gamma binds to vinculin but only weakly to focal
CC       adhesion kinase. Interacts with GIT1 and NUDT16L1/SDOS. Component
CC       of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and
CC       PAK1 (By similarity). Binds DDEF2. Interacts with unphosphorylated
CC       ITGA4. Interacts with RNF5.
CC   -!- INTERACTION:
CC       Q09463:rnf-5 (xeno); NbExp=2; IntAct=EBI-702209, EBI-963421;
CC       Q99942:RNF5; NbExp=3; IntAct=EBI-702209, EBI-348482;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Beta;
CC         IsoId=P49023-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=P49023-2; Sequence=VSP_003114;
CC       Name=Gamma;
CC         IsoId=P49023-3; Sequence=VSP_003115;
CC   -!- PTM: Phosphorylated on tyrosine residues during integrin-mediated
CC       cell adhesion, embryonic development, fibroblast transformation
CC       and following stimulation of cells by mitogens.
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U14588; AAC50104.1; -; mRNA.
DR   EMBL; U87946; AAD00648.1; -; Genomic_DNA.
DR   EMBL; U87941; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87942; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87943; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87944; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87945; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; D86862; BAA18997.1; -; mRNA.
DR   EMBL; D86863; BAA18998.1; -; mRNA.
DR   EMBL; AC004263; AAC05175.1; -; Genomic_DNA.
DR   PIR; A55933; A55933.
DR   UniGene; Hs.446336; -.
DR   PDB; 1KKY; Model; A=142-157.
DR   PDB; 1KL0; Model; B=142-157.
DR   IntAct; P49023; -.
DR   Ensembl; ENSG00000089159; Homo sapiens.
DR   KEGG; hsa:5829; -.
DR   HGNC; HGNC:9718; PXN.
DR   HPA; CAB003841; -.
DR   MIM; 602505; gene.
DR   ArrayExpress; P49023; -.
DR   GermOnline; ENSG00000089159; Homo sapiens.
DR   RZPD-ProtExp; D0240; -.
DR   RZPD-ProtExp; IOH10180; -.
DR   RZPD-ProtExp; IOH29384; -.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR   GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR   GO; GO:0007172; P:signal complex formation; TAS:ProtInc.
DR   InterPro; IPR001781; LIM_Zn_bd.
DR   InterPro; IPR001904; Paxillin.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF03535; Paxillin; 1.
DR   PRINTS; PR00832; PAXILLIN.
DR   ProDom; PD000094; LIM; 4.
DR   SMART; SM00132; LIM; 4.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
KW   3D-structure; Alternative splicing; Cell adhesion; Cytoskeleton;
KW   LIM domain; Metal-binding; Phosphorylation; Repeat; Zinc.
FT   CHAIN         1    591       Paxillin.
FT                                /FTId=PRO_0000075853.
FT   DOMAIN      356    415       LIM zinc-binding 1.
FT   DOMAIN      416    473       LIM zinc-binding 2.
FT   DOMAIN      474    533       LIM zinc-binding 3.
FT   DOMAIN      534    591       LIM zinc-binding 4.
FT   COMPBIAS     46     53       Pro-rich.
FT   MOD_RES      31     31       Phosphotyrosine.
FT   MOD_RES      88     88       Phosphotyrosine.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphotyrosine.
FT   MOD_RES     181    181       Phosphotyrosine.
FT   MOD_RES     303    303       Phosphoserine.
FT   VAR_SEQ     278    311       Missing (in isoform Alpha).
FT                                /FTId=VSP_003114.
FT   VAR_SEQ     278    311       IQDLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSW
FT                                PLEEVVLLVSISSSVQEGEKYPHPCAARHRTPSLRSPDQPP
FT                                PCPQ (in isoform Gamma).
FT                                /FTId=VSP_003115.
FT   CONFLICT     73     73       G -> S (in Ref. 4).
FT   HELIX       143    155
SQ   SEQUENCE   591 AA;  64533 MW;  0FFDC07047E96636 CRC64;
     MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
     TILDPLDQWQ PSGSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF
     PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL
     YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG
     EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQD LEQRADGERC WAAGWPRDGG
     RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA
     CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC
     NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA
     RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK
     PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C
//
ID   OPSD_XENLA              Reviewed;         354 AA.
AC   P29403;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   28-NOV-2006, entry version 52.
DE   Rhodopsin.
GN   Name=rho;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93287804; PubMed=8510503; DOI=10.1016/0169-328X(93)90016-I;
RA   Saha M.S., Grainger R.M.;
RT   "Early opsin expression in Xenopus embryos precedes photoreceptor
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 17:307-318(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=96216396; PubMed=8621718; DOI=10.1074/jbc.271.6.3179;
RA   Batni S., Scalzetti L.C., Moody S.A., Knox B.E.;
RT   "Characterization of the Xenopus rhodopsin gene.";
RL   J. Biol. Chem. 271:3179-3186(1996).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC       vision in dim light.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S62229; AAB27128.2; -; mRNA.
DR   EMBL; L04692; AAB59950.1; -; mRNA.
DR   EMBL; L07770; AAC42232.1; -; mRNA.
DR   EMBL; U23808; AAC59901.1; -; Genomic_DNA.
DR   PIR; I51200; I51200.
DR   HSSP; P02699; 1F88.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000732; Rhodopsin.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Phosphorylation; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Vision.
FT   CHAIN         1    354       Rhodopsin.
FT                                /FTId=PRO_0000197727.
FT   TOPO_DOM      1     36       Extracellular.
FT   TRANSMEM     37     61       1 (Potential).
FT   TOPO_DOM     62     73       Cytoplasmic.
FT   TRANSMEM     74     98       2 (Potential).
FT   TOPO_DOM     99    113       Extracellular.
FT   TRANSMEM    114    133       3 (Potential).
FT   TOPO_DOM    134    152       Cytoplasmic.
FT   TRANSMEM    153    176       4 (Potential).
FT   TOPO_DOM    177    202       Extracellular.
FT   TRANSMEM    203    230       5 (Potential).
FT   TOPO_DOM    231    252       Cytoplasmic.
FT   TRANSMEM    253    276       6 (Potential).
FT   TOPO_DOM    277    284       Extracellular.
FT   TRANSMEM    285    309       7 (Potential).
FT   TOPO_DOM    310    354       Cytoplasmic.
FT   BINDING     296    296       Retinal chromophore (covalent).
FT   LIPID       322    322       S-palmitoyl cysteine (By similarity).
FT   LIPID       323    323       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    110    187       By similarity.
FT   CONFLICT    107    107       P -> Q (in Ref. 2).
FT   CONFLICT    137    137       I -> M (in Ref. 2).
FT   CONFLICT    241    241       L -> A (in Ref. 2).
SQ   SEQUENCE   354 AA;  39787 MW;  CD18F49EC63D8FFE CRC64;
     MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF
     VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG
     GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP
     EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES
     LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI
     YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA
//
ID   OPS2_DROME              Reviewed;         381 AA.
AC   P08099; Q9VE29;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-APR-2007, entry version 73.
DE   Opsin Rh2 (Ocellar opsin).
GN   Name=Rh2; ORFNames=CG16740;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86133563; PubMed=2936466; DOI=10.1016/0092-8674(86)90836-6;
RA   Cowman A.F., Zuker C.S., Rubin G.M.;
RT   "An opsin gene expressed in only one photoreceptor cell type of the
RT   Drosophila eye.";
RL   Cell 44:705-710(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   LOCALIZATION OF OPSIN RH2, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=88261498; PubMed=2455230; DOI=10.1038/333737a0;
RA   Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.;
RT   "Targeted misexpression of a Drosophila opsin gene leads to altered
RT   visual function.";
RL   Nature 333:737-741(1988).
RN   [5]
RP   LOCALIZATION OF OPSIN RH2.
RX   MEDLINE=88261503; PubMed=2968518; DOI=10.1038/333779a0;
RA   Pollock J.A., Benzer S.;
RT   "Transcript localization of four opsin genes in the three visual
RT   organs of Drosophila; RH2 is ocellus specific.";
RL   Nature 333:779-782(1988).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=420 nm;
CC   -!- INTERACTION:
CC       Q9VL06:CG5604; NbExp=1; IntAct=EBI-162315, EBI-173559;
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominant opsin expressed in the dorsal
CC       ocelli.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M12896; AAA28734.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55601.1; -; Genomic_DNA.
DR   PIR; A24058; OOFF2.
DR   UniGene; Dm.2404; -.
DR   HSSP; P02699; 1EDV.
DR   DIP; DIP:22447N; -.
DR   IntAct; P08099; -.
DR   Ensembl; CG16740; Drosophila melanogaster.
DR   KEGG; dme:Dmel_CG16740; -.
DR   FlyBase; FBgn0003248; Rh2.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-012289-MONOMER; -.
DR   GermOnline; CG16740; Drosophila melanogaster.
DR   GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA:FlyBase.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007602; P:phototransduction; IGI:FlyBase.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001735; Opsin_RH1/RH2.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; Complete proteome; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transducer;
KW   Transmembrane; Vision.
FT   CHAIN         1    381       Opsin Rh2.
FT                                /FTId=PRO_0000197625.
FT   TOPO_DOM      1     56       Extracellular.
FT   TRANSMEM     57     81       1 (Potential).
FT   TOPO_DOM     82     93       Cytoplasmic.
FT   TRANSMEM     94    119       2 (Potential).
FT   TOPO_DOM    120    133       Extracellular.
FT   TRANSMEM    134    153       3 (Potential).
FT   TOPO_DOM    154    172       Cytoplasmic.
FT   TRANSMEM    173    196       4 (Potential).
FT   TOPO_DOM    197    220       Extracellular.
FT   TRANSMEM    221    248       5 (Potential).
FT   TOPO_DOM    249    283       Cytoplasmic.
FT   TRANSMEM    284    307       6 (Potential).
FT   TOPO_DOM    308    314       Extracellular.
FT   TRANSMEM    315    339       7 (Potential).
FT   TOPO_DOM    340    381       Cytoplasmic.
FT   BINDING     326    326       Retinal chromophore (covalent).
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Probable).
FT   DISULFID    130    207       Potential.
SQ   SEQUENCE   381 AA;  42722 MW;  628322D228396F9D CRC64;
     MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL
     GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI
     WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS
     YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL
     VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD
     EPKPDAPASD TETTSEADSK A
//
ID   OPS2_DROPS              Reviewed;         381 AA.
AC   P28679; Q298F1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 3.
DT   06-MAR-2007, entry version 52.
DE   Opsin Rh2 (Ocellar opsin).
GN   Name=Rh2; ORFNames=GA14120;
OS   Drosophila pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7237;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Apple Hill;
RX   MEDLINE=93012921; PubMed=1398053;
RA   Carulli J.P., Hartl D.L.;
RT   "Variable rates of evolution among Drosophila opsin genes.";
RL   Genetics 132:193-204(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=420 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- PTM: Some or all of the Ser/Thr residues present in the C-terminal
CC       part may be phosphorylated.
CC   -!- MISCELLANEOUS: Opsin Rh2 is the predominant opsin expressed in the
CC       dorsal ocelli.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous
CC       gene model prediction.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X65878; CAA46709.1; -; Genomic_DNA.
DR   EMBL; CM000070; EAL28004.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S40692; S40692.
DR   HSSP; P02699; 1EDV.
DR   FlyBase; FBgn0012708; Dpse\Rh2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001735; Opsin_RH1/RH2.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; Complete proteome; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transducer;
KW   Transmembrane; Vision.
FT   CHAIN         1    381       Opsin Rh2.
FT                                /FTId=PRO_0000197626.
FT   TOPO_DOM      1     56       Extracellular.
FT   TRANSMEM     57     81       1 (Potential).
FT   TOPO_DOM     82     93       Cytoplasmic.
FT   TRANSMEM     94    119       2 (Potential).
FT   TOPO_DOM    120    133       Extracellular.
FT   TRANSMEM    134    153       3 (Potential).
FT   TOPO_DOM    154    172       Cytoplasmic.
FT   TRANSMEM    173    196       4 (Potential).
FT   TOPO_DOM    197    220       Extracellular.
FT   TRANSMEM    221    248       5 (Potential).
FT   TOPO_DOM    249    283       Cytoplasmic.
FT   TRANSMEM    284    307       6 (Potential).
FT   TOPO_DOM    308    314       Extracellular.
FT   TRANSMEM    315    339       7 (Potential).
FT   TOPO_DOM    340    381       Cytoplasmic.
FT   BINDING     326    326       Retinal chromophore (covalent).
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Probable).
FT   DISULFID    130    207       Potential.
FT   CONFLICT     45     45       Y -> H (in Ref. 1).
FT   CONFLICT    342    343       KY -> ND (in Ref. 1).
FT   CONFLICT    358    358       S -> T (in Ref. 1).
FT   CONFLICT    381    381       A -> D (in Ref. 1).
SQ   SEQUENCE   381 AA;  42733 MW;  2033C05C4503FEAF CRC64;
     MERSLLPEPP LAMALLGPRF EAQTGGNRSV LDNVLPDMAP LVNPYWSRFA PMDPTMSKIL
     GLFTLVILII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAACGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKIAFI
     WMMAVFWTIM PLIGWSSYVP EGNLTACSID YMTRQWNPRS YLITYSLFVY YTPLFMICYS
     YWFIIATVAA HEKAMRDQAK KMNVKSLRSS EDCDKSAENK LAKVALTTIS LWFMAWTPYL
     IICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRLVLKEK CPMCVCGSTD
     EPKPDAPPSD TETTSEAESK A
//
ID   OPSC2_HEMSA             Reviewed;         377 AA.
AC   Q25158;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   31-OCT-2006, entry version 40.
DE   Compound eye opsin BCRH2.
OS   Hemigrapsus sanguineus (Crab).
OC   Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca;
OC   Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus.
OX   NCBI_TaxID=40176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=9318091;
RA   Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.;
RT   "Two opsins from the compound eye of the crab Hemigrapsus
RT   sanguineus.";
RL   J. Exp. Biol. 199:441-450(1996).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal. This opsin produces visual pigments with
CC       maximal absorption in the blue-green region of the spectrum.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells
CC       (R1-R7) forming the main rhabdom in each ommatidium.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D50584; BAA09133.1; -; mRNA.
DR   HSSP; P02699; 1L9H.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000856; Opsin_RH3/RH4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphorylation; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Vision.
FT   CHAIN         1    377       Compound eye opsin BCRH2.
FT                                /FTId=PRO_0000197750.
FT   TOPO_DOM      1     53       Extracellular.
FT   TRANSMEM     54     78       1 (Potential).
FT   TOPO_DOM     79     90       Cytoplasmic.
FT   TRANSMEM     91    115       2 (Potential).
FT   TOPO_DOM    116    131       Extracellular.
FT   TRANSMEM    132    151       3 (Potential).
FT   TOPO_DOM    152    170       Cytoplasmic.
FT   TRANSMEM    171    194       4 (Potential).
FT   TOPO_DOM    195    218       Extracellular.
FT   TRANSMEM    219    246       5 (Potential).
FT   TOPO_DOM    247    281       Cytoplasmic.
FT   TRANSMEM    282    305       6 (Potential).
FT   TOPO_DOM    306    313       Extracellular.
FT   TRANSMEM    314    338       7 (Potential).
FT   TOPO_DOM    339    377       Cytoplasmic.
FT   BINDING     325    325       Retinal chromophore (covalent) (By
FT                                similarity).
FT   CARBOHYD      3      3       N-linked (GlcNAc...) (Potential).
FT   DISULFID    128    205       By similarity.
SQ   SEQUENCE   377 AA;  42114 MW;  FD6CC2E0E199A256 CRC64;
     MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI
     YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV
     WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV
     IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV
     FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI
     SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET
     KSNDDSQSNS TVAQDKA
//
ID   OPSO_LIMPO              Reviewed;         376 AA.
AC   P35361;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   31-OCT-2006, entry version 41.
DE   Ocellar opsin.
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura;
OC   Limulidae; Limulus.
OX   NCBI_TaxID=6850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Median ocelli;
RX   MEDLINE=93317641; PubMed=8327495;
RA   Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.;
RT   "Opsins from the lateral eyes and ocelli of the horseshoe crab,
RT   Limulus polyphemus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=530 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Ocellar cells; median ocelli.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L03792; AAA28274.1; -; mRNA.
DR   EMBL; L03782; AAA02499.1; -; mRNA.
DR   PIR; A48197; A48197.
DR   HSSP; P02699; 1EDV.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001391; Opsin_lateye.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00578; OPSINLTRLEYE.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphorylation; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Vision.
FT   CHAIN         1    376       Ocellar opsin.
FT                                /FTId=PRO_0000197752.
FT   TOPO_DOM      1     46       Extracellular.
FT   TRANSMEM     47     71       1 (Potential).
FT   TOPO_DOM     72     83       Cytoplasmic.
FT   TRANSMEM     84    108       2 (Potential).
FT   TOPO_DOM    109    123       Extracellular.
FT   TRANSMEM    124    143       3 (Potential).
FT   TOPO_DOM    144    162       Cytoplasmic.
FT   TRANSMEM    163    186       4 (Potential).
FT   TOPO_DOM    187    210       Extracellular.
FT   TRANSMEM    211    238       5 (Potential).
FT   TOPO_DOM    239    274       Cytoplasmic.
FT   TRANSMEM    275    298       6 (Potential).
FT   TOPO_DOM    299    306       Extracellular.
FT   TRANSMEM    307    331       7 (Potential).
FT   TOPO_DOM    332    376       Cytoplasmic.
FT   BINDING     318    318       Retinal chromophore (covalent) (By
FT                                similarity).
FT   CARBOHYD     17     17       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
FT   DISULFID    120    197       By similarity.
SQ   SEQUENCE   376 AA;  42112 MW;  FA9647C40531CBF8 CRC64;
     MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII
     CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC
     EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL
     PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE
     HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS
     SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE
     ASATMTMEEK PKSPEA
//
ID   OPSD2_PATYE             Reviewed;         399 AA.
AC   O15974;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   31-OCT-2006, entry version 38.
DE   Rhodopsin, G0-coupled (G0-rhodopsin).
GN   Name=SCOP2;
OS   Patinopecten yessoensis (Ezo giant scallop) (Yesso scallop).
OC   Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida;
OC   Pectinoidea; Pectinidae; Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   MEDLINE=97435252; PubMed=9287291; DOI=10.1074/jbc.272.37.22979;
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A.,
RA   Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual
RT   cells.";
RL   J. Biol. Chem. 272:22979-22982(1997).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Retina. Expressed in the hyperpolarizing cell
CC       layer of the photoreceptor cells with its photoreceptive region
CC       adjacent to the lens.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB006455; BAA22218.1; -; mRNA.
DR   HSSP; P02699; 1F88.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR002962; Peropsin.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01244; PEROPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphorylation; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Vision.
FT   CHAIN         1    399       Rhodopsin, G0-coupled.
FT                                /FTId=PRO_0000197736.
FT   TOPO_DOM      1     17       Extracellular.
FT   TRANSMEM     18     43       1 (Potential).
FT   TOPO_DOM     44     55       Cytoplasmic.
FT   TRANSMEM     56     81       2 (Potential).
FT   TOPO_DOM     82     95       Extracellular.
FT   TRANSMEM     96    115       3 (Potential).
FT   TOPO_DOM    116    134       Cytoplasmic.
FT   TRANSMEM    135    158       4 (Potential).
FT   TOPO_DOM    159    182       Extracellular.
FT   TRANSMEM    183    210       5 (Potential).
FT   TOPO_DOM    211    240       Cytoplasmic.
FT   TRANSMEM    241    263       6 (Potential).
FT   TOPO_DOM    264    271       Extracellular.
FT   TRANSMEM    272    295       7 (Potential).
FT   TOPO_DOM    296    399       Cytoplasmic.
FT   BINDING     282    282       Retinal chromophore (covalent).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   DISULFID     92    169       By similarity.
SQ   SEQUENCE   399 AA;  45097 MW;  5AA6857ABC912100 CRC64;
     MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN
     LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII
     ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD
     VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF
     ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR
     DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV
     KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI
//
ID   OPS2_SCHGR              Reviewed;         380 AA.
AC   Q26495;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   31-OCT-2006, entry version 40.
DE   Opsin-2.
GN   Name=Lo2;
OS   Schistocerca gregaria (Desert locust).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97301174; PubMed=9156194; DOI=10.1016/S0042-6989(96)00198-8;
RA   Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.;
RT   "Primary structure of locust opsins: a speculative model which may
RT   account for ultraviolet wavelength light detection.";
RL   Vision Res. 37:495-503(1997).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80072; CAA56378.1; -; mRNA.
DR   HSSP; P02699; 1F88.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000856; Opsin_RH3/RH4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
KW   Chromophore; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphorylation; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Vision.
FT   CHAIN         1    380       Opsin-2.
FT                                /FTId=PRO_0000197636.
FT   TOPO_DOM      1     51       Extracellular.
FT   TRANSMEM     52     76       1 (Potential).
FT   TOPO_DOM     77     88       Cytoplasmic.
FT   TRANSMEM     89    115       2 (Potential).
FT   TOPO_DOM    116    128       Extracellular.
FT   TRANSMEM    129    148       3 (Potential).
FT   TOPO_DOM    149    166       Cytoplasmic.
FT   TRANSMEM    167    191       4 (Potential).
FT   TOPO_DOM    192    215       Extracellular.
FT   TRANSMEM    216    243       5 (Potential).
FT   TOPO_DOM    244    279       Cytoplasmic.
FT   TRANSMEM    280    303       6 (Potential).
FT   TOPO_DOM    304    311       Extracellular.
FT   TRANSMEM    312    336       7 (Potential).
FT   TOPO_DOM    337    380       Cytoplasmic.
FT   BINDING     323    323       Retinal chromophore (covalent) (By
FT                                similarity).
FT   CARBOHYD      3      3       N-linked (GlcNAc...) (Potential).
FT   DISULFID    125    202       Potential.
SQ   SEQUENCE   380 AA;  42531 MW;  113504F71027C07A CRC64;
     MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF
     MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG
     WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP
     FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI
     GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM
     IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS
     KSDTSSTATD RTVGNVSASA
//
ID   AQP1_HUMAN              Reviewed;         269 AA.
AC   P29972; Q8TBI5; Q8TDC1;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   20-MAR-2007, entry version 85.
DE   Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Water channel protein for red
DE   blood cells and kidney proximal tubule) (Urine water channel).
GN   Name=AQP1; Synonyms=CHIP28;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=92107900; PubMed=1722319;
RA   Preston G.M., Agre P.;
RT   "Isolation of the cDNA for erythrocyte integral membrane protein of 28
RT   kilodaltons: member of an ancient channel family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93340184; PubMed=8340403;
RA   Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.;
RT   "The human aquaporin-CHIP gene. Structure, organization, and
RT   chromosomal localization.";
RL   J. Biol. Chem. 268:15772-15778(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retinal pigment epithelium;
RX   MEDLINE=96326579; PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4;
RA   Ruiz A.C., Bok D.;
RT   "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in
RT   human retinal pigment epithelium.";
RL   Biochim. Biophys. Acta 1282:174-178(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   MEDLINE=94290349; PubMed=7517253;
RA   Li X., Yu H., Koide S.S.;
RT   "The water channel gene in human uterus.";
RL   Biochem. Mol. Biol. Int. 32:371-377(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165.
RA   Rieder M.J., Johanson E.J., da Ponte S.H., Hastings N.C., Ahearn M.O.,
RA   Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.;
RT   "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW-
RT   FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu).";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE OF 5-269.
RC   TISSUE=Articular cartilage;
RA   Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.;
RT   "Human chondrocytes in situ express aquaporin water channels: changes
RT   in AQP1 abundance in pathologies of articular cartilage.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 2-36.
RX   PubMed=2007592;
RA   Smith B.L., Agre P.;
RT   "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit
RT   oligomer similar to channel proteins.";
RL   J. Biol. Chem. 266:6407-6415(1991).
RN   [10]
RP   FUNCTION.
RX   MEDLINE=92229472; PubMed=1373524;
RA   Preston G.M., Carroll T.P., Guggino W.B., Agre P.;
RT   "Appearance of water channels in Xenopus oocytes expressing red cell
RT   CHIP28 protein.";
RL   Science 256:385-387(1992).
RN   [11]
RP   TARGET OF MERCURY INHIBITION.
RX   MEDLINE=93106996; PubMed=7677994;
RA   Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT   "The mercury-sensitive residue at cysteine 189 in the CHIP28 water
RT   channel.";
RL   J. Biol. Chem. 268:17-20(1993).
RN   [12]
RP   TOPOLOGY.
RX   MEDLINE=94124503; PubMed=7507481;
RA   Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT   "Membrane topology of aquaporin CHIP. Analysis of functional epitope-
RT   scanning mutants by vectorial proteolysis.";
RL   J. Biol. Chem. 269:1668-1673(1994).
RN   [13]
RP   STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
RX   MEDLINE=94313979; PubMed=7518771;
RA   Walz T., Smith B.L., Agre P., Engel A.;
RT   "The three-dimensional structure of human erythrocyte aquaporin
RT   CHIP.";
RL   EMBO J. 13:2985-2993(1994).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
RX   MEDLINE=97320502; PubMed=9177353; DOI=10.1038/42512;
RA   Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y.,
RA   Smith B.L., Agre P., Engel A.;
RT   "The three-dimensional structure of aquaporin-1.";
RL   Nature 387:624-627(1997).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
RX   MEDLINE=20487015; PubMed=11034202; DOI=10.1038/35036519;
RA   Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B.,
RA   Engel A., Fujiyoshi Y.;
RT   "Structural determinants of water permeation through aquaporin-1.";
RL   Nature 407:599-605(2000).
RN   [16]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
RX   MEDLINE=21423577; PubMed=11532455; DOI=10.1016/S0014-5793(01)02743-0;
RA   de Groot B.L., Engel A., Grubmueller H.;
RT   "A refined structure of human aquaporin-1.";
RL   FEBS Lett. 504:206-211(2001).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
RX   PubMed=11171962; DOI=10.1073/pnas.041489198;
RA   Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.;
RT   "Visualization of a water-selective pore by electron crystallography
RT   in vitreous ice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001).
RN   [18]
RP   VARIANT BLOOD GROUP COLTON VAL-45.
RX   MEDLINE=94365170; PubMed=7521882;
RA   Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.;
RT   "Human red cell aquaporin CHIP. I. Molecular characterization of ABH
RT   and Colton blood group antigens.";
RL   J. Clin. Invest. 94:1043-1049(1994).
RN   [19]
RP   VARIANT LEU-38.
RX   MEDLINE=94360246; PubMed=7521540;
RA   Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.;
RT   "Mutations in aquaporin-1 in phenotypically normal humans without
RT   functional CHIP water channels.";
RL   Science 265:1585-1587(1994).
CC   -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC       membranes of red cells and kidney proximal tubules with high
CC       permeability to water, thereby permitting water to move in the
CC       direction of an osmotic gradient.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a number of tissues including
CC       erythrocytes, renal tubules, retinal pigment epithelium, heart,
CC       lung, skeletal muscle, kidney and pancreas. Weakly expressed in
CC       brain, placenta and liver.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing
CC       three membrane-spanning domains and a pore-forming loop with the
CC       signature motif Asn-Pro-Ala (NPA).
CC   -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group
CC       system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46),
CC       approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-
CC       46). Co(A-B-) which is very rare, is due to a complete absence of
CC       AQP1.
CC   -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC       concentrations of mercury.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC   -!- WEB RESOURCE: NAME=BGMUT;
CC       NOTE=Blood group antigen gene mutation database";
CC       URL="http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=colton".
CC   -!- WEB RESOURCE: NAME=Protein Spotlight;
CC       NOTE=Liquid states - Issue 36 of July 2003;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt036.shtml".
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DR   EMBL; M77829; AAA58425.1; -; mRNA.
DR   EMBL; U41517; AAC50648.1; -; mRNA.
DR   EMBL; U41518; AAC50649.1; -; mRNA.
DR   EMBL; S73482; AAB31193.1; -; mRNA.
DR   EMBL; AC004691; AAC16481.1; -; Genomic_DNA.
DR   EMBL; AC005155; AAC23788.1; -; Genomic_DNA.
DR   EMBL; AY953319; AAX24129.1; -; Genomic_DNA.
DR   EMBL; BC022486; AAH22486.1; -; mRNA.
DR   EMBL; AF480415; AAL87136.1; -; Genomic_DNA.
DR   PIR; A41616; A41616.
DR   UniGene; Hs.312228; -.
DR   UniGene; Hs.76152; -.
DR   PDB; 1FQY; EM; A=1-269.
DR   PDB; 1H6I; EM; A=1-269.
DR   PDB; 1IH5; EM; A=1-269.
DR   Ensembl; ENSG00000106125; Homo sapiens.
DR   KEGG; hsa:358; -.
DR   H-InvDB; HIX0006573; -.
DR   HGNC; HGNC:633; AQP1.
DR   HPA; CAB001707; -.
DR   MIM; 107776; gene.
DR   MIM; 110450; phenotype.
DR   ArrayExpress; P29972; -.
DR   GermOnline; ENSG00000106125; Homo sapiens.
DR   RZPD-ProtExp; RZPDo839D02147; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0005372; F:water transporter activity; TAS:ProtInc.
DR   GO; GO:0007588; P:excretion; TAS:ProtInc.
DR   GO; GO:0006833; P:water transport; TAS:ProtInc.
DR   InterPro; IPR012269; AQP.
DR   InterPro; IPR000425; MIP.
DR   Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PIRSF; PIRSF002276; AQP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   ProDom; PD000295; MIP; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
KW   3D-structure; Blood group antigen; Direct protein sequencing;
KW   Glycoprotein; Membrane; Polymorphism; Repeat; Transmembrane;
KW   Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    269       Aquaporin-1.
FT                                /FTId=PRO_0000063920.
FT   TOPO_DOM      2      7       Cytoplasmic.
FT   TRANSMEM      8     36       Helix 1.
FT   TOPO_DOM     37     48       Extracellular.
FT   TRANSMEM     49     66       Helix 2.
FT   TOPO_DOM     67     70       Cytoplasmic.
FT   TOPO_DOM     71     76       In membrane.
FT   TRANSMEM     77     84       Helix B.
FT   TOPO_DOM     85     94       Cytoplasmic.
FT   TRANSMEM     95    115       Helix 3.
FT   TOPO_DOM    116    136       Extracellular.
FT   TRANSMEM    137    155       Helix 4.
FT   TOPO_DOM    156    166       Cytoplasmic.
FT   TRANSMEM    167    183       Helix 5.
FT   TOPO_DOM    184    186       Extracellular.
FT   TOPO_DOM    187    192       In membrane.
FT   TRANSMEM    193    200       Helix E.
FT   TOPO_DOM    201    207       Extracellular.
FT   TRANSMEM    208    228       Helix 6.
FT   TOPO_DOM    229    269       Cytoplasmic.
FT   MOTIF        76     78       NPA 1.
FT   MOTIF       192    194       NPA 2.
FT   COMPBIAS    159    162       Poly-Arg.
FT   SITE         56     56       Substrate discrimination.
FT   SITE        180    180       Substrate discrimination.
FT   SITE        189    189       Hg(2+)-sensitive residue.
FT   SITE        195    195       Substrate discrimination.
FT   CARBOHYD     42     42       N-linked (GlcNAc...).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   VARIANT      38     38       P -> L (in Co(A-B-) antigen; non
FT                                functional AQP1; red cells show low
FT                                osmotic water permeability).
FT                                /FTId=VAR_013279.
FT   VARIANT      45     45       A -> V (in Co(A-B+) antigen).
FT                                /FTId=VAR_004400.
FT   VARIANT     165    165       G -> D.
FT                                /FTId=VAR_022318.
FT   CONFLICT     45     45       A -> T (in Ref. 7; AAH22486).
FT   HELIX         8     35
FT   STRAND       37     42
FT   HELIX        48     65
FT   STRAND       68     71
FT   HELIX        76     83
FT   HELIX        94    114
FT   TURN        119    122
FT   STRAND      132    135
FT   HELIX       136    154
FT   HELIX       166    182
FT   TURN        183    185
FT   HELIX       192    199
FT   HELIX       207    227
SQ   SEQUENCE   269 AA;  28526 MW;  BA204D82FB26352E CRC64;
     MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI
     ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT
     GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
     LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD
     RVKVWTSGQV EEYDLDADDI NSRVEMKPK
//
ID   IFNA2_HUMAN             Reviewed;         188 AA.
AC   P01563; P01564; Q14606; Q96KI6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   20-FEB-2007, entry version 79.
DE   Interferon alpha-2 precursor (Interferon alpha-A) (LeIF A).
GN   Name=IFNA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=81052322; PubMed=6159538; DOI=10.1038/287411a0;
RA   Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G.,
RA   Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R.,
RA   Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M.,
RA   Familletti P.C., Pestka S.;
RT   "Human leukocyte interferon produced by E. coli is biologically
RT   active.";
RL   Nature 287:411-416(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=81148795; PubMed=6163083; DOI=10.1038/290020a0;
RA   Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M.,
RA   McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.;
RT   "The structure of eight distinct cloned human leukocyte interferon
RT   cDNAs.";
RL   Nature 290:20-26(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=82060261; PubMed=6170983;
RA   Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.;
RT   "DNA sequence of a major human leukocyte interferon gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bone marrow tumor;
RX   MEDLINE=86069501; PubMed=3906813;
RA   Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.;
RT   "Cloning of human leukocyte interferon cDNA and a strategy for its
RT   production in E. coli.";
RL   Rev. Latinoam. Microbiol. 27:141-150(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   MEDLINE=98357449; PubMed=9694076;
RA   Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P.,
RA   Mannoni P., Chabannon C.;
RT   "A defective retroviral vector encoding human interferon alpha 2 can
RT   transduce human leukemic cell lines.";
RL   Cancer Gene Ther. 5:247-256(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188.
RX   MEDLINE=81015442; PubMed=6158094;
RA   Streuli M., Nagata S., Weissmann C.;
RT   "At least three human type alpha interferons: structure of alpha 2.";
RL   Science 209:1343-1347(1980).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 24-188.
RX   MEDLINE=83299241; PubMed=6310510; DOI=10.1093/nar/11.16.5661;
RA   Weber H., Weissmann C.;
RT   "Formation of genes coding for hybrid proteins by recombination
RT   between related, cloned genes in E. coli.";
RL   Nucleic Acids Res. 11:5661-5669(1983).
RN   [8]
RP   PROTEIN SEQUENCE OF 24-112 AND 136-188.
RX   MEDLINE=81052321; PubMed=6159537; DOI=10.1038/287408a0;
RA   Allen G., Fantes K.H.;
RT   "A family of structural genes for human lymphoblastoid (leukocyte-
RT   type) interferon.";
RL   Nature 287:408-411(1980).
RN   [9]
RP   PROTEIN SEQUENCE OF 24-58.
RX   MEDLINE=98087498; PubMed=9425112;
RA   Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.;
RT   "Identification of nine interferon-alpha subtypes produced by Sendai
RT   virus-induced human peripheral blood leucocytes.";
RL   Biochem. J. 329:295-302(1998).
RN   [10]
RP   DISULFIDE BONDS.
RX   MEDLINE=81123083; PubMed=6162107; DOI=10.1038/289606a0;
RA   Wetzel R.;
RT   "Assignment of the disulphide bonds of leukocyte interferon.";
RL   Nature 289:606-607(1981).
RN   [11]
RP   GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C.
RX   MEDLINE=91264809; PubMed=2049076;
RA   Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.;
RT   "Natural human interferon-alpha 2 is O-glycosylated.";
RL   Biochem. J. 276:511-518(1991).
RN   [12]
RP   POLYMORPHISM.
RX   MEDLINE=95353982; PubMed=7627809;
RA   Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S.,
RA   Liao M.-J., Testa D.;
RT   "Interferon-alpha 2 variants in the human genome.";
RL   J. Interferon Cytokine Res. 15:341-349(1995).
RN   [13]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE=94052087; PubMed=8234245; DOI=10.1002/prot.340170109;
RA   Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A.,
RA   Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.;
RT   "A homology model of human interferon alpha-2.";
RL   Proteins 17:62-74(1993).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   MEDLINE=97148339; PubMed=8994971; DOI=10.1016/S0969-2126(96)00152-9;
RA   Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P.,
RA   Nagabhushan T.L., Walter M.R.;
RT   "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray
RT   crystallography.";
RL   Structure 4:1453-1463(1996).
RN   [15]
RP   STRUCTURE BY NMR.
RX   MEDLINE=98118493; PubMed=9417943; DOI=10.1006/jmbi.1997.1396;
RA   Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.;
RT   "The three-dimensional high resolution structure of human interferon
RT   alpha-2a determined by heteronuclear NMR spectroscopy in solution.";
RL   J. Mol. Biol. 274:661-675(1997).
CC   -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral
CC       activities. Interferon stimulates the production of two enzymes: a
CC       protein kinase and an oligoadenylate synthetase.
CC   -!- SUBCELLULAR LOCATION: Secreted protein.
CC   -!- POLYMORPHISM: Three forms exist; alpha-2a (shown here), alpha-2b
CC       and alpha-2c.
CC   -!- PHARMACEUTICAL: Available under the names Roferon-A (Roche) or
CC       Intron-A (Schering-Plough). Used as an anticancer drug for its
CC       antiproliferative activity.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family.
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DR   EMBL; J00207; AAB59402.1; -; Genomic_DNA.
DR   EMBL; V00544; CAA23805.1; -; mRNA.
DR   EMBL; V00548; CAA23809.1; -; mRNA.
DR   EMBL; V00549; CAA23810.1; -; mRNA.
DR   EMBL; Y11834; CAA72532.1; -; Genomic_DNA.
DR   EMBL; M54886; AAA59181.1; -; mRNA.
DR   EMBL; M29883; AAA52715.1; -; Genomic_DNA.
DR   EMBL; A04970; CAA00410.1; -; Unassigned_DNA.
DR   PIR; A93234; IVHUA2.
DR   PIR; I78570; I78570.
DR   UniGene; Hs.211575; -.
DR   PDB; 1ITF; NMR; @=24-188.
DR   PDB; 1RH2; X-ray; A/B/C/D/E/F=24-188.
DR   PDB; 2HIE; Model; @=24-188.
DR   DIP; DIP:3784N; -.
DR   DIP; DIP:481N; -.
DR   GlycoSuiteDB; P01563; -.
DR   Ensembl; ENSG00000188379; Homo sapiens.
DR   KEGG; hsa:3440; -.
DR   HGNC; HGNC:5423; IFNA2.
DR   MIM; 147562; gene.
DR   LinkHub; P01563; -.
DR   ArrayExpress; P01563; -.
DR   GermOnline; ENSG00000188379; Homo sapiens.
DR   RZPD-ProtExp; A0813; -.
DR   RZPD-ProtExp; IOH35221; -.
DR   RZPD-ProtExp; RZPDo834E0933; -.
DR   GO; GO:0005132; F:interferon-alpha/beta receptor binding; TAS:ProtInc.
DR   GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   InterPro; IPR009079; 4_helix_cytokine.
DR   InterPro; IPR000471; Interferon_abd.
DR   Gene3D; G3DSA:1.20.120.210; Interferon_abd; 1.
DR   PANTHER; PTHR11691; Interferon_abd; 1.
DR   Pfam; PF00143; Interferon; 1.
DR   PRINTS; PR00266; INTERFERONAB.
DR   ProDom; PD000550; Interferon_abd; 1.
DR   SMART; SM00076; IFabd; 1.
DR   PROSITE; PS00252; INTERFERON_A_B_D; 1.
KW   3D-structure; Antiviral defense; Cytokine; Direct protein sequencing;
KW   Glycoprotein; Pharmaceutical; Polymorphism; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    188       Interferon alpha-2.
FT                                /FTId=PRO_0000016360.
FT   CARBOHYD    129    129       O-linked (GalNAc...).
FT                                /FTId=CAR_000049.
FT   DISULFID     24    121
FT   DISULFID     52    161
FT   VARIANT      46     46       K -> R (in alpha-2B and alpha-2C).
FT                                /FTId=VAR_004012.
FT   VARIANT      57     57       H -> R (in alpha-2C).
FT                                /FTId=VAR_013001.
FT   HELIX        33     44
FT   TURN         49     54
FT   HELIX        63     66
FT   HELIX        76     91
FT   HELIX        93     98
FT   HELIX       101    123
FT   TURN        126    127
FT   TURN        133    133
FT   HELIX       134    155
FT   TURN        156    157
FT   HELIX       160    178
FT   TURN        179    182
SQ   SEQUENCE   188 AA;  21550 MW;  101DD21D394CBF97 CRC64;
     MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG
     FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA
     CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL
     QESLRSKE
//
