ID   OPSV_ORYLA              Reviewed;         334 AA.
AC   P87368;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative violet-sensitive opsin;
DE   AltName: Full=KFH-V;
DE   AltName: Full=Violet cone photoreceptor pigment;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Hisatomi O., Satoh T., Tokunaga F.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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: The three color pigments are found in the cone
CC       photoreceptor cells.
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; AB001605; BAA19422.1; -; mRNA.
DR   RefSeq; NP_001098126.1; NM_001104656.1.
DR   AlphaFoldDB; P87368; -.
DR   SMR; P87368; -.
DR   STRING; 8090.ENSORLP00000024036; -.
DR   GeneID; 100049181; -.
DR   KEGG; ola:100049181; -.
DR   CTD; 30582; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   OrthoDB; 940057at2759; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
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; IPR001521; Opsin_blue.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00574; OPSINBLUE.
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   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW   Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..334
FT                   /note="Putative violet-sensitive opsin"
FT                   /id="PRO_0000197771"
FT   TOPO_DOM        1..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..88
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         288
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   334 AA;  37394 MW;  557422B64F75580F CRC64;
     MGKYFYLYEN ISKVGPYDGP QYYLAPTWAF YLQAAFMGFV FFVGTPLNFV VLLATAKYKK
     LRVPLNYILV NITFAGFIFV TFSVSQVFLA SVRGYYFFGQ TLCALEAAVG AVAGLVTSWS
     LAVLSFERYL VICKPFGAFK FGSNHALAAV IFTWFMGVVR CPPFFGWSRY IPEGLGCSCG
     PDWYTNCEEF SCASYSKFLL VTCFICPITI IIFSYSQLLG ALRAVAAQQA ESASTQKAEK
     EVSRMIIVMV ASFVTCYGPY ALTAQYYAYS QDENKDYRLV TIPAFFSKSS CVYNPLIYAF
     MNKQFNGCIM EMVFGKKMEE ASEVSSKTEV STDS