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Database: UniProt
Entry: B4Z6M1_MORBA
LinkDB: B4Z6M1_MORBA
Original site: B4Z6M1_MORBA 
ID   B4Z6M1_MORBA            Unreviewed;       172 AA.
AC   B4Z6M1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Rhodopsin {ECO:0000313|EMBL:ACF34736.1};
DE   Flags: Fragment;
GN   Name=RHO {ECO:0000313|EMBL:ACF34736.1};
OS   Morus bassanus (Northern gannet) (Sula bassana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Sulidae; Morus.
OX   NCBI_TaxID=37578 {ECO:0000313|EMBL:ACF34736.1};
RN   [1] {ECO:0000313|EMBL:ACF34736.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18583609; DOI=10.1126/science.1157704;
RA   Hackett S.J., Kimball R.T., Reddy S., Bowie R.C., Braun E.L., Braun M.J.,
RA   Chojnowski J.L., Cox W.A., Han K.L., Harshman J., Huddleston C.J.,
RA   Marks B.D., Miglia K.J., Moore W.S., Sheldon F.H., Steadman D.W.,
RA   Witt C.C., Yuri T.;
RT   "A phylogenomic study of birds reveals their evolutionary history.";
RL   Science 320:1763-1768(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; EU737245; ACF34736.1; -; Genomic_DNA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProt.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000732; Rhodopsin.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   PANTHER; PTHR24240:SF15; RHODOPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR600732-3};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU000688};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW   Transducer {ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW   Zinc {ECO:0000256|PIRSR:PIRSR600732-1}.
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..172
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT   SITE            5
FT                   /note="Plays an important role in the conformation switch
FT                   to the active conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT   DISULFID        2..79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACF34736.1"
FT   NON_TER         172
FT                   /evidence="ECO:0000313|EMBL:ACF34736.1"
SQ   SEQUENCE   172 AA;  19342 MW;  082B7165A68F2EFA CRC64;
     GCYIEGFFAT LGGEIALWSL VVLAVERYVV VCKPMSNFRF GENHAIMGVA FSWIMALACA
     APPLFGWSRY IPEGMQCSCG IDYYTLKPEI NNESFVIYMF VVHFMIPLMV IFFCYGNLVC
     TVKEAAAQQQ ESATTQKAEK EVTRMVIIMV IAFLICWVPY ASVAFYMXTN QG
//
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