ID I6U2D9_9TELE Unreviewed; 274 AA.
AC I6U2D9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
GN Name=Rh {ECO:0000313|EMBL:AFN07334.1};
OS Schismatorhynchos nukta (nukta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeoninae incertae sedis; Schismatorhynchos.
OX NCBI_TaxID=643448 {ECO:0000313|EMBL:AFN07334.1};
RN [1] {ECO:0000313|EMBL:AFN07334.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CTOL03180 {ECO:0000313|EMBL:AFN07334.1};
RX PubMed=22728909; DOI=10.1016/j.ympev.2012.06.007;
RA Yang L., Arunachalam M., Sado T., Levin B.A., Golubtsov A.S., Freyhof J.,
RA Friel J.P., Chen W.-J., Hirt M.V., Manickam R., Agnew M.K., Simons A.M.,
RA Saitoh K., Miya M., Mayden R.L., He, S;
RT "Molecular phylogeny of the cyprinid tribe Labeonini (Teleostei:
RT Cypriniformes).";
RL Mol. Phylogenet. Evol. 65:362-379(2012).
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; JX074613; AFN07334.1; -; Genomic_DNA.
DR AlphaFoldDB; I6U2D9; -.
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..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 31..274
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT SITE 90
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 273
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT DISULFID 87..164
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFN07334.1"
FT NON_TER 274
FT /evidence="ECO:0000313|EMBL:AFN07334.1"
SQ SEQUENCE 274 AA; 31236 MW; FF33EDE54803159B CRC64;
YEYPQYYLVA PWAYACLSAY MFFLILTGFP VNFLTLYVTI EHKKLRTPLN YILLNLAIAD
LFMVFGGFTT TMYTSMHGYF VFGRLGCNLE GFFATLGGEM GLWSLVVLAV ERWMVVCKPV
SNFRFGENHA IMGVVFTWIM ASACAVPPLV GWSRYIPEGM QCSCGVDYYT RAPGVNNESF
VIYMFIVHFI IPLIVIFFCY GRLVCTVKEA AAQQQESETT QRAEREVTRM VIIMVIAFLV
CWTPYASVAW YIFTHQGSEF GPVFMTLPAF FAKT
//
