ID   OPSV_XENLA              Reviewed;         347 AA.
AC   P51473; Q5U505;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Violet-sensitive opsin;
DE   AltName: Full=Violet cone opsin;
DE   AltName: Full=Violet cone photoreceptor pigment;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=9733587; DOI=10.1006/exer.1998.0507;
RA   Starace D.M., Knox B.E.;
RT   "Cloning and expression of a Xenopus short wavelength cone pigment.";
RL   Exp. Eye Res. 67:209-220(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=425 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: The 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.
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; U23463; AAA64418.1; -; mRNA.
DR   EMBL; BC084882; AAH84882.1; -; mRNA.
DR   RefSeq; NP_001079121.1; NM_001085652.1.
DR   AlphaFoldDB; P51473; -.
DR   SMR; P51473; -.
DR   DNASU; 373655; -.
DR   GeneID; 373655; -.
DR   KEGG; xla:373655; -.
DR   CTD; 373655; -.
DR   Xenbase; XB-GENE-993056; opn1sw.L.
DR   OMA; CLCYVPY; -.
DR   OrthoDB; 940057at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 373655; Expressed in camera-type eye and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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..347
FT                   /note="Violet-sensitive opsin"
FT                   /id="PRO_0000197770"
FT   TOPO_DOM        1..31
FT                   /note="Extracellular"
FT   TRANSMEM        32..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..68
FT                   /note="Cytoplasmic"
FT   TRANSMEM        69..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..108
FT                   /note="Extracellular"
FT   TRANSMEM        109..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..147
FT                   /note="Cytoplasmic"
FT   TRANSMEM        148..171
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        172..197
FT                   /note="Extracellular"
FT   TRANSMEM        198..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..247
FT                   /note="Cytoplasmic"
FT   TRANSMEM        248..271
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..279
FT                   /note="Extracellular"
FT   TRANSMEM        280..304
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..347
FT                   /note="Cytoplasmic"
FT   REGION          323..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         291
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        105..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   347 AA;  39000 MW;  018E6B3E7D1238CB CRC64;
     MLEEEDFYLF KNVSNVSPFD GPQYHIAPKW AFTLQAIFMG MVFLIGTPLN FIVLLVTIKY
     KKLRQPLNYI LVNITVGGFL MCIFSIFPVF VSSSQGYFFF GRIACSIDAF VGTLTGLVTG
     WSLAFLAFER YIVICKPMGN FNFSSSHALA VVICTWIIGI VVSVPPFLGW SRYMPEGLQC
     SCGPDWYTVG TKYRSEYYTW FIFIFCFVIP LSLICFSYGR LLGALRAVAA QQQESASTQK
     AEREVSRMVI FMVGSFCLCY VPYAAMAMYM VTNRNHGLDL RLVTIPAFFS KSSCVYNPII
     YSFMNKQFRG CIMETVCGRP MSDDSSVSST SQRTEVSTVS SSQVSPA