OPSB_CHICK
ID OPSB_CHICK Reviewed; 361 AA.
AC P28682;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Blue-sensitive opsin;
DE AltName: Full=Blue 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], AND PROTEIN SEQUENCE OF 304-318.
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)=455 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; M92037; AAA48633.1; -; mRNA.
DR PIR; B46137; B46137.
DR RefSeq; NP_990848.1; NM_205517.1.
DR AlphaFoldDB; P28682; -.
DR SMR; P28682; -.
DR GeneID; 396525; -.
DR KEGG; gga:396525; -.
DR CTD; 102090745; -.
DR VEuPathDB; HostDB:geneid_396525; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P28682; -.
DR PRO; PR:P28682; -.
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; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..361
FT /note="Blue-sensitive opsin"
FT /id="PRO_0000197759"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT TRANSMEM 44..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..80
FT /note="Cytoplasmic"
FT TRANSMEM 81..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..120
FT /note="Extracellular"
FT TRANSMEM 121..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..159
FT /note="Cytoplasmic"
FT TRANSMEM 160..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..209
FT /note="Extracellular"
FT TRANSMEM 210..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..259
FT /note="Cytoplasmic"
FT TRANSMEM 260..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..291
FT /note="Extracellular"
FT TRANSMEM 292..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..361
FT /note="Cytoplasmic"
FT REGION 338..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 117..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 361 AA; 39657 MW; B9F262EA617D2888 CRC64;
MHPPRPTTDL PEDFYIPMAL DAPNITALSP FLVPQTHLGS PGLFRAMAAF MFLLIALGVP
INTLTIFCTA RFRKLRSHLN YILVNLALAN LLVILVGSTT ACYSFSQMYF ALGPTACKIE
GFAATLGGMV SLWSLAVVAF ERFLVICKPL GNFTFRGSHA VLGCVATWVL GFVASAPPLF
GWSRYIPEGL QCSCGPDWYT TDNKWHNESY VLFLFTFCFG VPLAIIVFSY GRLLITLRAV
ARQQEQSATT QKADREVTKM VVVMVLGFLV CWAPYTAFAL WVVTHRGRSF EVGLASIPSV
FSKSSTVYNP VIYVLMNKQF RSCMLKLLFC GRSPFGDDED VSGSSQATQV SSVSSSHVAP
A
