ID D9IY00_OPSBI Unreviewed; 268 AA.
AC D9IY00;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
OS Opsariichthys bidens (Chinese hook snout carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Opsariichthyinae; Opsariichthys.
OX NCBI_TaxID=141458 {ECO:0000313|EMBL:ADJ56015.1};
RN [1] {ECO:0000313|EMBL:ADJ56015.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CTOL00123 {ECO:0000313|EMBL:ADJ56015.1};
RX PubMed=20553898; DOI=10.1016/j.ympev.2010.05.021;
RA Tang K.L., Agnew M.K., Hirt M.V., Sado T., Schneider L.M., Freyhof J.,
RA Sulaiman Z., Swartz E., Vidthayanon C., Miya M., Saitoh K., Simons A.M.,
RA Wood R.M., Mayden R.L.;
RT "Systematics of the subfamily Danioninae (Teleostei: Cypriniformes:
RT Cyprinidae).";
RL Mol. Phylogenet. Evol. 57:189-214(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000256|PIRSR:PIRSR600732-50}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000256|RuleBase:RU004951}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU004951}.
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DR EMBL; HM223957; ADJ56015.1; -; Genomic_DNA.
DR AlphaFoldDB; D9IY00; -.
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:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
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; IPR001760; Opsin.
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; PR00238; OPSIN.
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 Chromophore {ECO:0000256|PIRSR:PIRSR600732-50,
KW ECO:0000256|RuleBase:RU004951};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600732-3};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU004951};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Photoreceptor protein {ECO:0000256|RuleBase:RU004951};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951};
KW Retinal protein {ECO:0000256|PIRSR:PIRSR600732-50,
KW ECO:0000256|RuleBase:RU004951};
KW Sensory transduction {ECO:0000256|RuleBase:RU004951};
KW Transducer {ECO:0000256|RuleBase:RU004951};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004951};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW Zinc {ECO:0000256|PIRSR:PIRSR600732-1}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 223..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 23..268
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT SITE 82
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT MOD_RES 265
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT DISULFID 79..156
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADJ56015.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:ADJ56015.1"
SQ SEQUENCE 268 AA; 30255 MW; 84E99FCFCC121711 CRC64;
VAPWAYACLA AYMFFLILTG FPINFLTLYV TLEHKKLRTP LNYSLLNLAV ADLFMVFGGF
TTTMYTSLNG YFVFGRLGCN LEGFFATLGG EMALWSIVTL AIERWLVVCK PISNFRFGEN
HAIMGVVFTW VMACSCAVPP LVGWSRYIPE GMQCSCGIDY YTRAEGYNNE SFVIYMFLVH
ALIPFIIIFF CYGRLVCAVK DAAAQQQESE TTQRAEREVT RMVILMGFAY LVCWTPYAST
AWYIFTHKGT SFGPVFMTIP AFFAKTSA
//
