ID   OPSD2_MIZYE             Reviewed;         399 AA.
AC   O15974;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Rhodopsin, G0-coupled;
DE   AltName: Full=G0-rhodopsin;
GN   Name=SCOP2;
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=9287291; DOI=10.1074/jbc.272.37.22979;
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A., Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual cells.";
RL   J. Biol. Chem. 272:22979-22982(1997).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Retina. Expressed in the hyperpolarizing cell layer
CC       of the photoreceptor cells with its photoreceptive region adjacent to
CC       the lens.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250}.
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; AB006455; BAA22218.1; -; mRNA.
DR   AlphaFoldDB; O15974; -.
DR   SMR; O15974; -.
DR   PRIDE; O15974; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IPR002962; Peropsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01244; PEROPSIN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..399
FT                   /note="Rhodopsin, G0-coupled"
FT                   /id="PRO_0000197736"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT   TRANSMEM        18..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..55
FT                   /note="Cytoplasmic"
FT   TRANSMEM        56..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..95
FT                   /note="Extracellular"
FT   TRANSMEM        96..115
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..134
FT                   /note="Cytoplasmic"
FT   TRANSMEM        135..158
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..182
FT                   /note="Extracellular"
FT   TRANSMEM        183..210
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..240
FT                   /note="Cytoplasmic"
FT   TRANSMEM        241..263
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..271
FT                   /note="Extracellular"
FT   TRANSMEM        272..295
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..399
FT                   /note="Cytoplasmic"
FT   MOD_RES         282
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   399 AA;  45097 MW;  5AA6857ABC912100 CRC64;
     MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN
     LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII
     ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD
     VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF
     ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR
     DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV
     KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI