ID A0A067YNE7_9TELE Unreviewed; 254 AA. AC A0A067YNE7; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 22-FEB-2023, entry version 24. DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951}; DE Flags: Fragment; GN Name=RH {ECO:0000313|EMBL:AHE80835.1}; OS Henicorhynchus sp. MNHN 2013-0116. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Labeoninae; 'Osteochilini'; Henicorhynchus. OX NCBI_TaxID=1441809 {ECO:0000313|EMBL:AHE80835.1}; RN [1] {ECO:0000313|EMBL:AHE80835.1} RP NUCLEOTIDE SEQUENCE. RA Veran M., Pasco-Viel E.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AHE80835.1} RP NUCLEOTIDE SEQUENCE. RA Yang L., Mayden R.L., Laudet V., Viriot L.; RT "Stability versus diversity of pharyngeal dentition during the evolutionary RT radiation of two related clades of the subfamily Cyprininae (Teleostei: RT Cypriniformes)."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KC631260; AHE80835.1; -; Genomic_DNA. DR AlphaFoldDB; A0A067YNE7; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004930; F:G protein-coupled receptor activity; 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|ARBA:ARBA00022991, 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|ARBA:ARBA00022543, KW ECO:0000256|RuleBase:RU004951}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951}; KW Retinal protein {ECO:0000256|ARBA:ARBA00022925, KW ECO:0000256|RuleBase:RU004951}; KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606, KW ECO:0000256|RuleBase:RU004951}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, 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..25 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 37..57 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 77..95 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 115..135 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 216..238 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT DOMAIN 16..254 FT /note="G-protein coupled receptors family 1 profile" FT /evidence="ECO:0000259|PROSITE:PS50262" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT BINDING 241 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT SITE 75 FT /note="Plays an important role in the conformation switch FT to the active conformation" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-2" FT DISULFID 72..149 FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHE80835.1" FT NON_TER 254 FT /evidence="ECO:0000313|EMBL:AHE80835.1" SQ SEQUENCE 254 AA; 28793 MW; 683A54639220F329 CRC64; CLAAYMFFLI LTGFPVNFLT LYVTIEHKKL RTPLNYILLN LAISDLFMVF GGFTTTMYTS LHGYFVFGRI GCNLEGFFAT LGGEMGLWSL VVLAFERWMV VCKPVSNFRF GENHAIMGVA FTWVMACSCA VPPLVGWSRY IPEGMQCSCG VNYYTRVPGV NNESFVIYMF IVHFLIPLVV IFFCYGRLVC TVKEAAAQQQ ESETTQRAER EVTRMVIIMV IGFLICWVPY ASVAWYIFTH QGSEFGPVFM TLPA //