ID B8QPE9_9TELE Unreviewed; 273 AA.
AC B8QPE9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Rhodopsin {ECO:0000256|ARBA:ARBA00013487, ECO:0000256|RuleBase:RU004951};
DE Flags: Fragment;
GN Name=Rhod {ECO:0000313|EMBL:ACI00498.1};
OS Callionymus schaapii (short-snout sand-dragonet).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Syngnathiaria; Syngnathiformes; Callionymoidei; Callionymidae; Callionymus;
OC Callionymus.
OX NCBI_TaxID=546510 {ECO:0000313|EMBL:ACI00498.1};
RN [1] {ECO:0000313|EMBL:ACI00498.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Extraction B254 {ECO:0000313|EMBL:ACI00498.1};
RX PubMed=19059489; DOI=10.1016/j.ympev.2008.11.013;
RA Li B., Dettai A., Cruaud C., Couloux A., Desoutter-Meniger M.,
RA Lecointre G.;
RT "RNF213, a new nuclear marker for acanthomorph phylogeny.";
RL Mol. Phylogenet. Evol. 50:345-363(2009).
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; EU637946; ACI00498.1; -; Genomic_DNA.
DR AlphaFoldDB; B8QPE9; -.
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..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 123..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..273
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 BINDING 248
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:ACI00498.1"
FT NON_TER 273
FT /evidence="ECO:0000313|EMBL:ACI00498.1"
SQ SEQUENCE 273 AA; 30643 MW; EF923D5A305E3D30 CRC64;
VNPAAYAALG AYMFLLILLG FPINFLTLYV TIENKKLRTP LNYILLNLAV ANLFMVFGGF
TTTMYTSMHG YFVLGRLGCN LEGFFATLGG EIGLWSLVVL AIERWVVVCK PISNFRFGEN
HAIMGLVFTW VMACACAVPP LVGWSRYIPE GMQCSCGVDY YTRAEGFNNE SFVVYMFICH
FIIPMTIVFF CYGRLLCAVK EAAAAQQESE TTQRAEREVT RMVVIMVIAF LVCWVPYASV
AWYIFTHQGS EFGPVFMTLP AFFAKSSSIY NPL
//
