OPSV_CHICK
ID OPSV_CHICK Reviewed; 347 AA.
AC P28684;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Violet-sensitive opsin;
DE AltName: Full=Violet cone opsin;
DE AltName: Full=Violet cone photoreceptor pigment;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=1385866; DOI=10.1073/pnas.89.13.5932;
RA Okano T., Kojima D., Fukada Y., Shichida Y., Yoshizawa T.;
RT "Primary structures of chicken cone visual pigments: vertebrate rhodopsins
RT have evolved out of cone visual pigments.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5932-5936(1992).
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)=415 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; M92039; AAA49141.1; -; mRNA.
DR PIR; C46137; C46137.
DR RefSeq; NP_990769.1; NM_205438.1.
DR AlphaFoldDB; P28684; -.
DR SMR; P28684; -.
DR PRIDE; P28684; -.
DR GeneID; 396419; -.
DR KEGG; gga:396419; -.
DR CTD; 611; -.
DR VEuPathDB; HostDB:geneid_396525; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P28684; -.
DR PRO; PR:P28684; -.
DR Proteomes; UP000000539; Unplaced.
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:0016038; P:absorption of visible light; IDA:AgBase.
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..347
FT /note="Violet-sensitive opsin"
FT /id="PRO_0000197768"
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; 38720 MW; 11B99472DFACE453 CRC64;
MSSDDDFYLF TNGSVPGPWD GPQYHIAPPW AFYLQTAFMG IVFAVGTPLN AVVLWVTVRY
KRLRQPLNYI LVNISASGFV SCVLSVFVVF VASARGYFVF GKRVCELEAF VGTHGGLVTG
WSLAFLAFER YIVICKPFGN FRFSSRHALL VVVATWLIGV GVGLPPFFGW SRYMPEGLQC
SCGPDWYTVG TKYRSEYYTW FLFIFCFIVP LSLIIFSYSQ LLSALRAVAA QQQESATTQK
AEREVSRMVV VMVGSFCLCY VPYAALAMYM VNNRDHGLDL RLVTIPAFFS KSACVYNPII
YCFMNKQFRA CIMETVCGKP LTDDSDASTS AQRTEVSSVS SSQVGPT
