ID A0A0E3SV33_MUSST Unreviewed; 339 AA. AC A0A0E3SV33; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 27-MAR-2024, entry version 25. DE RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951}; DE Flags: Fragment; GN Name=Rh1 {ECO:0000313|EMBL:AKB91227.1}; OS Muscicapa striata (Spotted flycatcher) (Setophaga striata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Parulidae; OC Setophaga. OX NCBI_TaxID=1212470 {ECO:0000313|EMBL:AKB91227.1}; RN [1] {ECO:0000313|EMBL:AKB91227.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25827331; DOI=10.1111/mec.13180; RA Bloch N.I., Price T.D., Chang B.S.; RT "Evolutionary dynamics of Rh2 opsins in birds demonstrate an episode of RT accelerated evolution in the New World warblers (Setophaga)."; RL Mol. Ecol. 24:2449-2462(2015). 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 --------------------------------------------------------------------------- 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; KM977603; AKB91227.1; -; mRNA. DR AlphaFoldDB; A0A0E3SV33; -. 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:0016037; P:light absorption; IEA:UniProt. DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd15080; 7tmA_MWS_opsin; 1. 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; IPR027430; Retinal_BS. DR InterPro; IPR000732; Rhodopsin. DR InterPro; IPR019477; Rhodopsin_N. DR PANTHER; PTHR24240; OPSIN; 1. DR PANTHER; PTHR24240:SF15; RHODOPSIN; 1. DR Pfam; PF00001; 7tm_1; 1. DR Pfam; PF10413; Rhodopsin_N; 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. DR PROSITE; PS00238; OPSIN; 1. PE 2: Evidence at transcript level; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRSR:PIRSR600732- KW 50}; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600732- KW 4}; Lipoprotein {ECO:0000256|PIRSR:PIRSR600732-5}; 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|PIRSR:PIRSR600732-50}; 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 40..63 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 75..96 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 102..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 153..173 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 203..223 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 254..277 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT TRANSMEM 283..308 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004951" FT DOMAIN 54..306 FT /note="G-protein coupled receptors family 1 profile" FT /evidence="ECO:0000259|PROSITE:PS50262" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT BINDING 279 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-1" FT SITE 113 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 296 FT /note="N6-(retinylidene)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-50" FT LIPID 322 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-5" FT LIPID 323 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-5" FT CARBOHYD 2 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4" FT CARBOHYD 15 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR600732-4" FT DISULFID 110..187 FT /evidence="ECO:0000256|PIRSR:PIRSR600732-3" FT NON_TER 339 FT /evidence="ECO:0000313|EMBL:AKB91227.1" SQ SEQUENCE 339 AA; 38193 MW; 1DB64DD7C9A5AB76 CRC64; MNGTEGQDFY VPMSNKTGVV RSPFEYPQYY LAEPWKFSAL AAYMFMLILL GFPINFLTLY VTIQHKKLRT PLNYILLNLA VADLFMVFGG FTTTMYTSMN GYFVFGVTGC YIEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFS WIMALACAAP PLFGWSRYIP EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFMIPLAIIF FCYGNLVCTV KEAAAQQQES ATTQKAEKEV TRMVIIMVIS FLICWVPYAS VAFYIFTNQG SDFGPIFMTI PAFFAKSSAI YNPVIYIVMN KQFRNCMITT LCCGKNPLGD EDTSAGKTE //