OPSD1_MIZYE
ID OPSD1_MIZYE Reviewed; 499 AA.
AC O15973;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Rhodopsin, GQ-coupled;
DE AltName: Full=GQ-rhodopsin;
GN Name=SCOP1;
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 such as rhodopsin and porphyropsin are light-
CC absorbing molecules that mediate vision. Rhodopsin consists of an
CC apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor
CC is coupled to the activation of phospholipase C. Porphyropsin consists
CC of opsin covalently linked to 11-cis 3,4-didehydroretinal.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Retina. Expressed in the depolarizing cell layer of
CC the photoreceptor cells distant from 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}.
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; AB006454; BAA22217.1; -; mRNA.
DR AlphaFoldDB; O15973; -.
DR SMR; O15973; -.
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; IPR001760; Opsin.
DR InterPro; IPR000856; Opsin_RH3/RH4.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00577; OPSINRH3RH4.
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 1: Evidence at protein 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..499
FT /note="Rhodopsin, GQ-coupled"
FT /id="PRO_0000197735"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT TRANSMEM 51..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..87
FT /note="Cytoplasmic"
FT TRANSMEM 88..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..128
FT /note="Extracellular"
FT TRANSMEM 129..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..168
FT /note="Cytoplasmic"
FT TRANSMEM 169..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..216
FT /note="Extracellular"
FT TRANSMEM 217..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..278
FT /note="Cytoplasmic"
FT TRANSMEM 279..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..310
FT /note="Extracellular"
FT TRANSMEM 311..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..499
FT /note="Cytoplasmic"
FT MOD_RES 322
FT /note="N6-(retinylidene)lysine"
FT LIPID 353
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 354
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 499 AA; 55946 MW; 853D1B7E35E09EEA CRC64;
MADNKSTLPG LPDINGTLNR SMTPNTGWEG PYDMSVHLHW TQFPPVTEEW HYIIGVYITI
VGLLGIMGNT TVVYIFSNTK SLRSPSNLFV VNLAVSDLIF SAVNGFPLLT VSSFHQKWIF
GSLFCQLYGF VGGVFGLMSI NTLTAISIDR YVVITKPLQA SQTMTRRKVH LMIVIVWVLS
ILLSIPPFFG WGAYIPEGFQ TSCTFDYLTK TARTRTYIVV LYLFGFLIPL IIIGVCYVLI
IRGVRRHDQK MLTITRSMKT EDARANNKRA RSELRISKIA MTVTCLFIIS WSPYAIIALI
AQFGPAHWIT PLVSELPMML AKSSSMHNPV VYALSHPKFR KALYQRVPWL FCCCKPKEKA
DFRTSVCSKR SVTRTESVNS DVSSVISNLS DSTTTLGLTS EGATRANRET SFRRSVSIIK
GDEDPCTHPD TFLLAYKEVE VGNLFDMTDD QNRRDSNLHS LYIPTRVQHR PTTQSLGTTP
GGVYIVDNGQ RVNGLTFNS
