ID F5B5Q5_9GOBI Unreviewed; 276 AA.
AC F5B5Q5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Rhodopsin {ECO:0000256|ARBA:ARBA00013487, ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
GN Name=Rhod {ECO:0000313|EMBL:AEC05071.1};
OS Smilosicyopus sasali.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Sicydiinae; Smilosicyopus.
OX NCBI_TaxID=1001960 {ECO:0000313|EMBL:AEC05071.1};
RN [1] {ECO:0000313|EMBL:AEC05071.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=9A {ECO:0000313|EMBL:AEC05071.1};
RA Keith P., Lord C., Lorion J., Watanabe S., Tsukamoto K., Couloux A.,
RA Dettai A.;
RT "Phylogeny and biogeography of Sicydiinae (Teleostei: Gobiidae) inferred
RT from mitochondrial and nuclear genes.";
RL Mar. Biol. 158:311-326(2010).
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000256|ARBA:ARBA00004504}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC 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; HQ639159; AEC05071.1; -; Genomic_DNA.
DR AlphaFoldDB; F5B5Q5; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
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 6..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004951"
FT DOMAIN 25..276
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT SITE 84
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 267
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT DISULFID 81..158
FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEC05071.1"
FT NON_TER 276
FT /evidence="ECO:0000313|EMBL:AEC05071.1"
SQ SEQUENCE 276 AA; 31061 MW; 8641914FCAD47757 CRC64;
YLVNPAAYAA LGAYMFFLIL AGFPINFLTL YVTIEHKKLR TPLNYILLNL AVADLFMVFG
GFTTTMYTSM HGYFVLGRLG CNLEGFFATL GGEIALWSLV VLAIERWIVV CKPISNFRFG
ENHAIMGVAF TWIMACSCAV PPLVGWSRYI PEGMQCSCGV DYYTRAEGFN NESFVIYMFI
VHFSIPFTVI FFCYGRLLCA VKEAAAAQQE SETTQRAERE VTRMVVIMVI AFLVSWLPYA
SVAWYIFTHQ GSEFGPLFMT LPAFFAKSSA IYNPLI
//
