ID   OPSB_HUMAN              Reviewed;         345 AA.
AC   P03999; Q13877;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2023, sequence version 2.
DT   27-MAR-2024, entry version 209.
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-261.
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 269-307.
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-76 AND PRO-211.
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-261.
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-187.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAB05207.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAC51334.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL31362.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AH003620; AAB05207.1; ALT_INIT; 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; ALT_INIT; Genomic_DNA.
DR   EMBL; L32835; AAL31362.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M26172; AAA35608.1; -; mRNA.
DR   CCDS; CCDS5806.2; -.
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   GlyCosmos; P03999; 1 site, No reported glycans.
DR   GlyGen; P03999; 1 site.
DR   iPTMnet; P03999; -.
DR   PhosphoSitePlus; P03999; -.
DR   BioMuta; OPN1SW; -.
DR   DMDM; 129203; -.
DR   MassIVE; P03999; -.
DR   PaxDb; 9606-ENSP00000249389; -.
DR   PeptideAtlas; P03999; -.
DR   ProteomicsDB; 51629; -.
DR   Antibodypedia; 31899; 88 antibodies from 19 providers.
DR   DNASU; 611; -.
DR   Ensembl; ENST00000249389.3; ENSP00000249389.3; ENSG00000128617.3.
DR   MANE-Select; ENST00000249389.3; ENSP00000249389.3; NM_001385125.1; NP_001372054.1.
DR   AGR; HGNC:1012; -.
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   OpenTargets; ENSG00000128617; -.
DR   Orphanet; 88629; Tritanopia.
DR   PharmGKB; PA31938; -.
DR   VEuPathDB; HostDB:ENSG00000128617; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234549; -.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; P03999; -.
DR   OrthoDB; 5350930at2759; -.
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 1145 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 cell types or tissues.
DR   GO; GO:0120199; C:cone photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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   CDD; cd15076; 7tmA_SWS1_opsin; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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   PANTHER; PTHR24240; OPSIN; 1.
DR   PANTHER; PTHR24240:SF16; SHORT-WAVE-SENSITIVE OPSIN 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00574; OPSINBLUE.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
DR   Genevisible; P03999; HS.
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..345
FT                   /note="Short-wave-sensitive opsin 1"
FT                   /id="PRO_0000197762"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..270
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         290
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        104..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         76
FT                   /note="G -> R (in CBT; dbSNP:rs104894031)"
FT                   /evidence="ECO:0000269|PubMed:1531728"
FT                   /id="VAR_004838"
FT   VARIANT         187
FT                   /note="T -> I (in CBT; dbSNP:rs1190183515)"
FT                   /evidence="ECO:0000269|PubMed:23022137"
FT                   /id="VAR_081835"
FT   VARIANT         211
FT                   /note="S -> P (in CBT; dbSNP:rs104894032)"
FT                   /evidence="ECO:0000269|PubMed:1531728"
FT                   /id="VAR_004839"
FT   VARIANT         261
FT                   /note="P -> S (in CBT; dbSNP:rs104894033)"
FT                   /evidence="ECO:0000269|PubMed:1386496, ECO:0000269|Ref.3"
FT                   /id="VAR_004840"
FT   CONFLICT        305..307
FT                   /note="KQF -> VKL (in Ref. 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  38719 MW;  E4C7EFFBB92107F3 CRC64;
     MSEEEFYLFK NISSVGPWDG PQYHIAPVWA FYLQAAFMGT VFLIGFPLNA MVLVATLRYK
     KLRQPLNYIL VNVSFGGFLL CIFSVFPVFV ASCNGYFVFG RHVCALEGFL GTVAGLVTGW
     SLAFLAFERY IVICKPFGNF RFSSKHALTV VLATWTIGIG VSIPPFFGWS RFIPEGLQCS
     CGPDWYTVGT KYRSESYTWF LFIFCFIVPL SLICFSYTQL LRALKAVAAQ QQESATTQKA
     EREVSRMVVV MVGSFCVCYV PYAAFAMYMV NNRNHGLDLR LVTIPSFFSK SACIYNPIIY
     CFMNKQFQAC IMKMVCGKAM TDESDTCSSQ KTEVSTVSST QVGPN
//