OPSB_HUMAN
ID OPSB_HUMAN Reviewed; 348 AA.
AC P03999; Q13877;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 200.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Retinal cone cell;
RX PubMed=2937147; DOI=10.1126/science.2937147;
RA Nathans J., Thomas D., Hogness D.S.;
RT "Molecular genetics of human color vision: the genes encoding blue, green,
RT and red pigments.";
RL Science 232:193-202(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9089077; DOI=10.1007/pl00006157;
RA Shimmin L.C., Mai P., Li W.H.;
RT "Sequences and evolution of human and squirrel monkey blue opsin genes.";
RL J. Mol. Evol. 44:378-382(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRITANOPIA SER-264.
RA Li T., Studencki A., Falk J., Smith V., Pokorny J., Went L., O'Shea R.,
RA Applebury M.L.;
RT "A point mutation in the blue cone opsin gene causes tritanopia in two
RT autosomal dominant tritan pedigrees.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 272-310.
RX PubMed=2565599; DOI=10.1126/science.2565599;
RA Sarkar G., Sommer S.S.;
RT "Access to a messenger RNA sequence or its protein product is not limited
RT by tissue or species specificity.";
RL Science 244:331-334(1989).
RN [5]
RP REVIEW.
RX PubMed=3303660; DOI=10.1016/0042-6989(86)90115-x;
RA Applebury M.L., Hargrave P.A.;
RT "Molecular biology of the visual pigments.";
RL Vision Res. 26:1881-1895(1986).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30168605; DOI=10.1002/lsm.23015;
RA Castellano-Pellicena I., Uzunbajakava N.E., Mignon C., Raafs B.,
RA Botchkarev V.A., Thornton M.J.;
RT "Does blue light restore human epidermal barrier function via activation of
RT Opsin during cutaneous wound healing?";
RL Lasers. Surg. Med. 51:370-382(2019).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY ULTRAVIOLET A
RP LIGHT.
RX PubMed=31380578; DOI=10.1111/bjd.18410;
RA Lan Y., Wang Y., Lu H.;
RT "Opsin 3 is a key regulator of ultraviolet A-induced photoageing in human
RT dermal fibroblast cells.";
RL Br. J. Dermatol. 182:1228-1244(2020).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31730232; DOI=10.1111/php.13178;
RA Wang Y., Lan Y., Lu H.;
RT "Opsin3 Downregulation Induces Apoptosis of Human Epidermal Melanocytes via
RT Mitochondrial Pathway.";
RL Photochem. Photobiol. 96:83-93(2020).
RN [9]
RP VARIANTS CBT ARG-79 AND PRO-214.
RX PubMed=1531728;
RA Weitz C.J., Miyake Y., Shinzato K., Montag E., Zrenner E., Went L.N.,
RA Nathans J.;
RT "Human tritanopia associated with two amino acid substitutions in the blue-
RT sensitive opsin.";
RL Am. J. Hum. Genet. 50:498-507(1992).
RN [10]
RP VARIANT CBT SER-264.
RX PubMed=1386496;
RA Weitz C.J., Went L.N., Nathans J.;
RT "Human tritanopia associated with a third amino acid substitution in the
RT blue-sensitive visual pigment.";
RL Am. J. Hum. Genet. 51:444-446(1992).
RN [11]
RP VARIANT CBT ILE-190.
RX PubMed=23022137; DOI=10.1016/j.visres.2012.09.007;
RA Baraas R.C., Hagen L.A., Dees E.W., Neitz M.;
RT "Substitution of isoleucine for threonine at position 190 of S-opsin causes
RT S-cone-function abnormalities.";
RL Vision Res. 73:1-9(2012).
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 (Probable). Required for the maintenance of cone outer
CC segment organization in the ventral retina, but not essential for the
CC 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:P51491,
CC ECO:0000305|PubMed:2937147}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=420 nm;
CC -!- INTERACTION:
CC P03999; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-13385956, EBI-11956541;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2937147,
CC ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass
CC 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:0000269|PubMed:30168605}.
CC -!- TISSUE SPECIFICITY: The three color pigments are found in the cone
CC photoreceptor cells (PubMed:2937147). Expressed throughout the
CC epidermis and dermis, primarily in the stratum granulosum in the facial
CC and abdominal skin (at protein level) (PubMed:30168605). Expressed in
CC dermal fibroblasts (at protein level) (PubMed:31380578). Expressed in
CC melanocytes (at protein level) (PubMed:31730232).
CC {ECO:0000269|PubMed:2937147, ECO:0000269|PubMed:30168605,
CC ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}.
CC -!- INDUCTION: Induced by ultraviolet A light in dermal fibroblasts.
CC {ECO:0000269|PubMed:31380578}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region.
CC -!- DISEASE: Tritan color blindness (CBT) [MIM:190900]: A disorder of
CC vision characterized by a selective deficiency of blue spectral
CC sensitivity. {ECO:0000269|PubMed:1386496, ECO:0000269|PubMed:1531728,
CC ECO:0000269|PubMed:23022137}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Mutations of the color pigment genes; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/cppmut.htm";
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DR EMBL; M13299; AAB05207.1; -; Genomic_DNA.
DR EMBL; M13295; AAB05207.1; JOINED; Genomic_DNA.
DR EMBL; M13296; AAB05207.1; JOINED; Genomic_DNA.
DR EMBL; M13297; AAB05207.1; JOINED; Genomic_DNA.
DR EMBL; M13298; AAB05207.1; JOINED; Genomic_DNA.
DR EMBL; U53874; AAC51334.1; -; Genomic_DNA.
DR EMBL; L32835; AAL31362.1; -; Genomic_DNA.
DR EMBL; M26172; AAA35608.1; -; mRNA.
DR PIR; A03156; OOHUB.
DR RefSeq; NP_001699.1; NM_001708.2.
DR AlphaFoldDB; P03999; -.
DR SMR; P03999; -.
DR BioGRID; 107082; 7.
DR IntAct; P03999; 1.
DR STRING; 9606.ENSP00000249389; -.
DR GlyGen; P03999; 1 site.
DR iPTMnet; P03999; -.
DR PhosphoSitePlus; P03999; -.
DR BioMuta; OPN1SW; -.
DR DMDM; 129203; -.
DR MassIVE; P03999; -.
DR PaxDb; P03999; -.
DR PeptideAtlas; P03999; -.
DR PRIDE; P03999; -.
DR ProteomicsDB; 51629; -.
DR Antibodypedia; 31899; 81 antibodies from 19 providers.
DR DNASU; 611; -.
DR Ensembl; ENST00000249389.3; ENSP00000249389.3; ENSG00000128617.3.
DR GeneID; 611; -.
DR CTD; 611; -.
DR DisGeNET; 611; -.
DR GeneCards; OPN1SW; -.
DR HGNC; HGNC:1012; OPN1SW.
DR HPA; ENSG00000128617; Tissue enriched (retina).
DR MalaCards; OPN1SW; -.
DR MIM; 190900; phenotype.
DR MIM; 613522; gene.
DR neXtProt; NX_P03999; -.
DR Orphanet; 88629; Tritanopia.
DR PharmGKB; PA31938; -.
DR VEuPathDB; HostDB:ENSG00000128617; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P03999; -.
DR OMA; CLCYVPY; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P03999; -.
DR TreeFam; TF324998; -.
DR PathwayCommons; P03999; -.
DR Reactome; R-HSA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-HSA-2453864; Retinoid cycle disease events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-419771; Opsins.
DR SignaLink; P03999; -.
DR BioGRID-ORCS; 611; 8 hits in 1067 CRISPR screens.
DR GeneWiki; OPN1SW; -.
DR GenomeRNAi; 611; -.
DR Pharos; P03999; Tbio.
DR PRO; PR:P03999; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P03999; protein.
DR Bgee; ENSG00000128617; Expressed in sural nerve and 88 other tissues.
DR Genevisible; P03999; HS.
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; IDA:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0071492; P:cellular response to UV-A; IDA: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:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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 Cell membrane; Cell projection; Chromophore; Cytoplasm; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..348
FT /note="Short-wave-sensitive opsin 1"
FT /id="PRO_0000197762"
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 CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 107..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 79
FT /note="G -> R (in CBT; dbSNP:rs104894031)"
FT /evidence="ECO:0000269|PubMed:1531728"
FT /id="VAR_004838"
FT VARIANT 190
FT /note="T -> I (in CBT; dbSNP:rs1190183515)"
FT /evidence="ECO:0000269|PubMed:23022137"
FT /id="VAR_081835"
FT VARIANT 214
FT /note="S -> P (in CBT; dbSNP:rs104894032)"
FT /evidence="ECO:0000269|PubMed:1531728"
FT /id="VAR_004839"
FT VARIANT 264
FT /note="P -> S (in CBT; dbSNP:rs104894033)"
FT /evidence="ECO:0000269|PubMed:1386496, ECO:0000269|Ref.3"
FT /id="VAR_004840"
FT CONFLICT 308..310
FT /note="KQF -> VKL (in Ref. 4)"
FT /evidence="ECO:0000305"
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
