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   02-SEP-2026, entry version 97.
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: Cell projection, rhabdomere membrane
CC       {ECO:0000250|UniProtKB:P31356}; Multi-pass membrane protein
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   GlyCosmos; O16005; 1 site, No reported glycans.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0016918; F:retinal binding; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   CDD; cd15337; 7tmA_Opsin_Gq_invertebrates; 1.
DR   FunFam; 1.20.1070.10:FF:000044; Opsin, ultraviolet-sensitive; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR050125; GPCR_opsins.
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   PANTHER; PTHR24240; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF02162; XYPPX; 3.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00239; RHODOPSNTAIL.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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   Cell membrane; Cell projection; Chromophore; Disulfide bond;
KW   G protein-coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   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        367..401
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..425
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..452
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
//