OPSD_GAMAF
ID OPSD_GAMAF Reviewed; 354 AA.
AC P79756;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Rhodopsin;
GN Name=rho;
OS Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Gambusia.
OX NCBI_TaxID=33528;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holbrooki; TISSUE=Retina;
RX PubMed=9236103; DOI=10.1111/j.1095-8649.1997.tb02528.x;
RA Archer S.N., Hirano J.;
RT "Opsin sequences of the rod visual pigments in two species of Poeciliid
RT fish.";
RL J. Fish Biol. 51:215-219(1997).
RN [2]
RP RETINAL-BINDING, AND FUNCTION.
RX PubMed=18422881; DOI=10.1111/j.1751-1097.2008.00344.x;
RA Toyama M., Hironaka M., Yamahama Y., Horiguchi H., Tsukada O., Uto N.,
RA Ueno Y., Tokunaga F., Seno K., Hariyama T.;
RT "Presence of rhodopsin and porphyropsin in the eyes of 164 fishes,
RT representing marine, diadromous, coastal and freshwater species--a
RT qualitative and comparative study.";
RL Photochem. Photobiol. 84:996-1002(2008).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. While most salt water fish species use retinal as
CC chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of
CC retinal and 3-dehydroretinal (PubMed:18422881). Light-induced
CC isomerization of 11-cis to all-trans retinal triggers a conformational
CC change that activates signaling via G-proteins. Subsequent receptor
CC phosphorylation mediates displacement of the bound G-protein alpha
CC subunit by arrestin and terminates signaling (By similarity).
CC {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P32309, ECO:0000269|PubMed:18422881}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell projection,
CC cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P35359}.
CC Note=Synthesized in the inner segment (IS) of rod photoreceptor cells
CC before vectorial transport to disk membranes in the rod outer segment
CC (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {ECO:0000250|UniProtKB:P02699}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; Y11146; CAA72033.1; -; mRNA.
DR AlphaFoldDB; P79756; -.
DR SMR; P79756; -.
DR STRING; 33528.ENSGAFP00000031268; -.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein level;
KW Cell projection; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..354
FT /note="Rhodopsin"
FT /id="PRO_0000197674"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 309..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 354 AA; 39644 MW; 1CE46D74A03D406B CRC64;
MNGTEGPYFY VPMVNTTGIV RSPYEYPQYY LVSPAAYACL GAYMFFLILV GFPVNFLTLY
VTIEHKKLRT PLNYILLNLA VADLFMVFGG FTTTIYTSMH GYFVLGRLGC NLEGYFATLG
GEIGLWSLVV LAVERWLVVC KPISNFRFTE NHAIMGLVFT WIMANACAAP PLLGWSRYIP
EGMQCSCGVD YYTRAEGFNN ESFVIYMFIC HFCIPLVVVF FCYGRLLCAV KEAAAAQQES
ETTQRAEREV TRMVVILVIG FLVCWTPYAS VAWYIFSNQG SEFGPLFMTI PAFFAKSSSI
YNPMIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTASK TEASSVSSSS VSPA
