ID OPSD_LIMBE Reviewed; 289 AA.
AC O42427;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 22-FEB-2023, entry version 86.
DE RecName: Full=Rhodopsin;
DE Flags: Fragment;
GN Name=rho;
OS Limnocottus bergianus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Cottidae; Limnocottus.
OX NCBI_TaxID=61633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9417898; DOI=10.1006/mpev.1997.0428;
RA Hunt D.M., Fitzgibbon J., Slobodyanyuk S.J., Bowmaker J.K., Dulai K.S.;
RT "Molecular evolution of the cottoid fish endemic to Lake Baikal deduced
RT from nuclear DNA evidence.";
RL Mol. Phylogenet. Evol. 8:415-422(1997).
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 (By similarity). 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}.
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}.
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DR EMBL; U97270; AAB61724.1; -; Genomic_DNA.
DR AlphaFoldDB; O42427; -.
DR SMR; O42427; -.
DR GlyCosmos; O42427; 1 site, No reported glycans.
DR GO; GO:0016020; C: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 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 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.
DR PROSITE; PS00238; OPSIN; 1.
PE 3: Inferred from homology;
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..>289
FT /note="Rhodopsin"
FT /id="PRO_0000197679"
FT TOPO_DOM <1..7
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 33..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 68..81
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..104
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 105..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 145..173
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..195
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 196..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 246..257
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..279
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 280..>289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 105..107
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 84
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 267
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 289
SQ SEQUENCE 289 AA; 32446 MW; 1E93812014C8B0A2 CRC64;
YLVNPAGYAA LGAYMFLLIL IGSPVNFLTL YVTLEHKKLR TPLNYILLNL AVADLFMVLG
GFTTTMYTSM HGYSVLGRLG CILEGFFATL GGEIALWSLV VLAIERWIVV CKPISNFRFT
EDHAIMGLAF SWVMALACAV PPLVGWSRYI PEGMQCSCGV DYYTRAEGFN NESFVIYMFI
VHFLIPLSVI FFCYGRLLCA VKEAAAAQQE SETTQRPEKE VTRMVVIMVI AFLVCCLPNA
SVAWWIFCNQ GSDFGPIFMT LPSFFAKSAA IYNPMIYICM NKQFRHCMI
//
