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OPSB_PANTR
ID   OPSB_PANTR              Reviewed;         348 AA.
AC   P60015;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Short-wave-sensitive opsin 1;
DE   AltName: Full=Blue cone photoreceptor pigment;
DE   AltName: Full=Blue-sensitive opsin;
DE            Short=BOP;
GN   Name=OPN1SW; Synonyms=BCP;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9549095; DOI=10.1093/oxfordjournals.molbev.a025941;
RA   Shimmin L.C., Miller J., Tran H.N., Li W.H.;
RT   "Contrasting levels of DNA polymorphism at the autosomal and X-linked
RT   visual color pigment loci in humans and squirrel monkeys.";
RL   Mol. Biol. Evol. 15:449-455(1998).
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 (By similarity). Required for the maintenance of cone
CC       outer segment organization in the ventral retina, but not essential for
CC       the maintenance of functioning cone photoreceptors (By similarity).
CC       Involved in ensuring correct abundance and localization of retinal
CC       membrane proteins (By similarity). May increase spectral sensitivity in
CC       dim light (By similarity). {ECO:0000250|UniProtKB:P03999,
CC       ECO:0000250|UniProtKB:P51491}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P03999};
CC       Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear
CC       region {ECO:0000250|UniProtKB:P03999}.
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; AF039435; AAB95490.1; -; Genomic_DNA.
DR   EMBL; AF039433; AAB95490.1; JOINED; Genomic_DNA.
DR   EMBL; AF039434; AAB95490.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001009127.1; NM_001009127.1.
DR   AlphaFoldDB; P60015; -.
DR   SMR; P60015; -.
DR   STRING; 9598.ENSPTRP00000033678; -.
DR   PaxDb; P60015; -.
DR   Ensembl; ENSPTRT00000036429; ENSPTRP00000033678; ENSPTRG00000019669.
DR   GeneID; 472508; -.
DR   KEGG; ptr:472508; -.
DR   CTD; 611; -.
DR   VGNC; VGNC:8710; OPN1SW.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234549; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; P60015; -.
DR   OMA; CLCYVPY; -.
DR   OrthoDB; 940057at2759; -.
DR   TreeFam; TF324998; -.
DR   Proteomes; UP000002277; Chromosome 7.
DR   Bgee; ENSPTRG00000019669; Expressed in fibroblast and 19 other tissues.
DR   GO; GO:0120199; C:cone photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0097381; C:photoreceptor disc membrane; IEA:UniProt.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0071492; P:cellular response to UV-A; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Cell membrane; Cell projection; Chromophore; Cytoplasm; 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..348
FT                   /note="Short-wave-sensitive opsin 1"
FT                   /id="PRO_0000197764"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..173
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..273
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..281
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..306
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         293
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   348 AA;  39135 MW;  83FAB2E7111CB581 CRC64;
     MRKMSEEEFY LFKNISSVGP WDGPQYHIAP VWAFYLQAAF MGTVFLIGFP LNAMVLVATL
     RYKKLRQPLN YILVNVSFGG FLLCIFSVFP VFVASCNGYF VFGRHVCALE GFLGTVAGLV
     TGWSLAFLAF ERYIVICKPF GNFRFSSKHA LTVVLATWTI GIGVSIPPFF GWSRFIPEGL
     QCSCGPDWYT VGTKYRSESY TWFLFIFCFI VPLSLICFSY TQLLRALKAV AAQQQESATT
     QKAEREVSRM VVVMVGSFCV CYVPYAAFAM YMVNNRNHGL DLRLVTIPSF FSKSACIYNP
     IIYCFMNKQF QACIMKMVCG KAMTDESDTC SSQKTEVSTV SSTQVGPN
 
 
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