OPSD_SEPOF
ID OPSD_SEPOF Reviewed; 464 AA.
AC O16005;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Rhodopsin;
GN Name=RHO;
OS Sepia officinalis (Common cuttlefish).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX NCBI_TaxID=6610;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9662500; DOI=10.1242/jeb.201.15.2299;
RA Bellingham J., Morris A.G., Hunt D.M.;
RT "The rhodopsin gene of the cuttlefish Sepia officinalis: sequence and
RT spectral tuning.";
RL J. Exp. Biol. 201:2299-2306(1998).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Light-induced isomerization of 11-cis to all-trans retinal
CC triggers a conformational change that activates signaling via G-
CC proteins. Signaling mediates the activation of phospholipase C (By
CC similarity). Subsequent receptor phosphorylation mediates displacement
CC of the bound G-protein alpha subunit by arrestin and terminates
CC signaling (By similarity). {ECO:0000250|UniProtKB:P08100,
CC ECO:0000250|UniProtKB:P31356}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P31356}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P31356}. Note=Detected on
CC the rhabdomere membrane in the photoreceptor outer segment.
CC {ECO:0000250|UniProtKB:P31356}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal (By similarity). After hydrolysis of the Schiff base and
CC release of the covalently bound all-trans-retinal, active rhodopsin is
CC regenerated by binding of a fresh molecule of 11-cis-retinal (By
CC similarity). {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P31356}.
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; AF000947; AAC26329.1; -; mRNA.
DR AlphaFoldDB; O16005; -.
DR SMR; O16005; -.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0016918; F:retinal binding; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
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; IPR006031; XYPPX.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF02162; XYPPX; 5.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..464
FT /note="Rhodopsin"
FT /id="PRO_0000197747"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 59..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 98..109
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 173..199
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 225..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 284..293
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P31356"
FT TOPO_DOM 316..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 344..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..134
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT COMPBIAS 393..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 336
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 337
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 464 AA; 51506 MW; E90CB72E07E54E33 CRC64;
MGRDIPDNET WWYNPTMEVH PHWKQFNQVP DAVYYSLGIF IGICGIIGCT GNGIVIYLFT
KTKSLQTPAN MFIINLAFSD FTFSLVNGFP LMTISCFIKK WVFGMAACKV YGFIGGIFGL
MSIMTMSMIS IDRYNVIGRP MAASKKMSHR RAFLMIIFVW MWSTLWSIGP IFGWGAYVLE
GVLCNCSFDY ITRDSATRSN IVCMYIFAFC FPILIIFFCY FNIVMAVSNH EKEMAAMAKR
LNAKELRKAQ AGASAEMKLA KISIVIVTQF LLSWSPYAVV ALLAQFGPIE WVTPYAAQLP
VMFAKASAIH NPLIYSVSHP KFREAIAENF PWIITCCQFD EKEVEDDKDA ETEIPATEQS
GGESADAAQM KEMMAMMQKM QQQQAAYPPQ GAYPPQGGYP PQGYPPPPAQ GGYPPQGYPP
PPQGYPPAQG YPPQGYPPPQ GAPPQGAPPQ AAPPQGVDNQ AYQA
