OPT_HUMAN
ID OPT_HUMAN Reviewed; 332 AA.
AC Q9UBM4; Q5T2G4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Opticin;
DE AltName: Full=Oculoglycan;
DE Flags: Precursor;
GN Name=OPTC; Synonyms=OPT;
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 [MRNA].
RC TISSUE=Retina;
RX PubMed=10636917; DOI=10.1074/jbc.275.3.2123;
RA Reardon A.J., Le Goff M., Briggs M.D., McLeod D., Sheehan J.K.,
RA Thornton D.J., Bishop P.N.;
RT "Identification in vitreous and molecular cloning of opticin, a novel
RT member of the family of leucine-rich repeat proteins of the extracellular
RT matrix.";
RL J. Biol. Chem. 275:2123-2129(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=10837509;
RA Hobby P., Wyatt M.K., Gan W., Bernstein S., Tomarev S., Slingsby C.,
RA Wistow G.J.;
RT "Cloning, modeling, and chromosomal localization for a small leucine-rich
RT repeat proteoglycan (SLRP) family member expressed in human eye.";
RL Mol. Vis. 6:72-78(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10892843;
RA Friedman J.S., Ducharme R., Raymond V., Walter M.A.;
RT "Isolation of a novel iris-specific and leucine-rich repeat protein
RT (oculoglycan) using differential selection.";
RL Invest. Ophthalmol. Vis. Sci. 41:2059-2066(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-182; CYS-229 AND TRP-325, AND
RP TISSUE SPECIFICITY.
RX PubMed=12019215; DOI=10.1093/hmg/11.11.1333;
RA Friedman J.S., Faucher M., Hiscott P., Biron V.L., Malenfant M.,
RA Turcotte P., Raymond V., Walter M.A.;
RT "Protein localization in the human eye and genetic screen of opticin.";
RL Hum. Mol. Genet. 11:1333-1342(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-312.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18164633; DOI=10.1016/j.joca.2007.11.007;
RA Monfort J., Tardif G., Roughley P., Reboul P., Boileau C., Bishop P.N.,
RA Pelletier J.P., Martel-Pelletier J.;
RT "Identification of opticin, a member of the small leucine-rich repeat
RT proteoglycan family, in human articular tissues: a novel target for MMP-13
RT in osteoarthritis.";
RL Osteoarthritis Cartilage 16:749-755(2008).
RN [10]
RP TISSUE SPECIFICITY, AND CLEAVAGE BY MMP1; MMP2; MMP3; MMP7; MMP8; MMP9;
RP ADAMTS4 AND ADAMTS5.
RX PubMed=23845380; DOI=10.1016/j.jbspin.2013.05.007;
RA Tio L., Martel-Pelletier J., Pelletier J.P., Bishop P.N., Roughley P.,
RA Farran A., Benito P., Monfort J.;
RT "Characterization of opticin digestion by proteases involved in
RT osteoarthritis development.";
RL Joint Bone Spine 81:137-141(2014).
RN [11]
RP SULFATION, AND TISSUE SPECIFICITY.
RX PubMed=25136834; DOI=10.1371/journal.pone.0105409;
RA Kanan Y., Siefert J.C., Kinter M., Al-Ubaidi M.R.;
RT "Complement factor H, vitronectin, and opticin are tyrosine-sulfated
RT proteins of the retinal pigment epithelium.";
RL PLoS ONE 9:E105409-E105409(2014).
CC -!- FUNCTION: Inhibits angiogenesis in the vitreous humor of the eye, and
CC therefore represses neovascularization (By similarity). Binds collagen
CC fibrils (By similarity). May be involved in collagen fiber organization
CC via regulation of other members of the small leucine-rich repeat
CC proteoglycan superfamily (By similarity).
CC {ECO:0000250|UniProtKB:P58874, ECO:0000250|UniProtKB:Q920A0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58874}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18164633}.
CC -!- TISSUE SPECIFICITY: Expressed in cartilage and synovial membranes (at
CC protein level) (PubMed:18164633, PubMed:23845380). Expressed in the
CC retina, iris, ligament, skin and fetal liver (at protein level)
CC (PubMed:12019215, PubMed:25136834). Expressed in the retinal pigment
CC epithelium (at protein level) (PubMed:25136834). Expressed in synovial
CC fibroblasts and subchondral bone osteoblasts (PubMed:18164633).
CC {ECO:0000269|PubMed:12019215, ECO:0000269|PubMed:18164633,
CC ECO:0000269|PubMed:23845380, ECO:0000269|PubMed:25136834}.
CC -!- PTM: O-glycosylated. {ECO:0000305|PubMed:16335952}.
CC -!- PTM: Proteolytically cleaved by MMP1, MMP2, MMP3, MMP7, MMP8, MMP9,
CC ADAMTS4, and ADAMTS5 (PubMed:23845380). Proteolytically cleaved by
CC MMP13 (By similarity). The degradation of OPTC by proteases may
CC contribute to osteoarthritis pathophysiology (PubMed:23845380).
CC {ECO:0000250|UniProtKB:P58874, ECO:0000269|PubMed:23845380}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:25136834}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class III subfamily. {ECO:0000305}.
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DR EMBL; AJ133790; CAB53459.1; -; mRNA.
DR EMBL; AF161702; AAD45900.1; -; mRNA.
DR EMBL; AY077681; AAL78286.1; -; mRNA.
DR EMBL; AL391817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91482.1; -; Genomic_DNA.
DR EMBL; BC074942; AAH74942.1; -; mRNA.
DR EMBL; BC074943; AAH74943.1; -; mRNA.
DR CCDS; CCDS1439.1; -.
DR RefSeq; NP_055174.1; NM_014359.3.
DR RefSeq; XP_011507708.1; XM_011509406.2.
DR AlphaFoldDB; Q9UBM4; -.
DR SMR; Q9UBM4; -.
DR BioGRID; 117640; 42.
DR IntAct; Q9UBM4; 2.
DR STRING; 9606.ENSP00000356191; -.
DR GlyGen; Q9UBM4; 1 site.
DR iPTMnet; Q9UBM4; -.
DR PhosphoSitePlus; Q9UBM4; -.
DR BioMuta; OPTC; -.
DR DMDM; 8928250; -.
DR MassIVE; Q9UBM4; -.
DR PaxDb; Q9UBM4; -.
DR PeptideAtlas; Q9UBM4; -.
DR PRIDE; Q9UBM4; -.
DR ProteomicsDB; 84008; -.
DR Antibodypedia; 34546; 114 antibodies from 28 providers.
DR DNASU; 26254; -.
DR Ensembl; ENST00000367222.7; ENSP00000356191.2; ENSG00000188770.10.
DR GeneID; 26254; -.
DR KEGG; hsa:26254; -.
DR MANE-Select; ENST00000367222.7; ENSP00000356191.2; NM_014359.4; NP_055174.1.
DR UCSC; uc001gzu.2; human.
DR CTD; 26254; -.
DR DisGeNET; 26254; -.
DR GeneCards; OPTC; -.
DR HGNC; HGNC:8158; OPTC.
DR HPA; ENSG00000188770; Not detected.
DR MIM; 605127; gene.
DR neXtProt; NX_Q9UBM4; -.
DR OpenTargets; ENSG00000188770; -.
DR PharmGKB; PA31947; -.
DR VEuPathDB; HostDB:ENSG00000188770; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154248; -.
DR HOGENOM; CLU_067583_2_0_1; -.
DR InParanoid; Q9UBM4; -.
DR OMA; EHKYTRR; -.
DR OrthoDB; 914775at2759; -.
DR PhylomeDB; Q9UBM4; -.
DR TreeFam; TF351924; -.
DR PathwayCommons; Q9UBM4; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; Q9UBM4; -.
DR BioGRID-ORCS; 26254; 11 hits in 1062 CRISPR screens.
DR GeneWiki; Opticin; -.
DR GenomeRNAi; 26254; -.
DR Pharos; Q9UBM4; Tbio.
DR PRO; PR:Q9UBM4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UBM4; protein.
DR Bgee; ENSG00000188770; Expressed in tibialis anterior and 81 other tissues.
DR ExpressionAtlas; Q9UBM4; baseline and differential.
DR Genevisible; Q9UBM4; HS.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..332
FT /note="Opticin"
FT /id="PRO_0000032765"
FT DOMAIN 116..153
FT /note="LRRNT"
FT REPEAT 154..175
FT /note="LRR 1"
FT REPEAT 178..199
FT /note="LRR 2"
FT REPEAT 202..223
FT /note="LRR 3"
FT REPEAT 248..269
FT /note="LRR 4"
FT REPEAT 270..290
FT /note="LRR 5"
FT REPEAT 300..320
FT /note="LRR 6"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 20..21
FT /note="Cleavage; by MMP7"
FT /evidence="ECO:0000269|PubMed:23845380"
FT SITE 32..33
FT /note="Cleavage; by MMP7"
FT /evidence="ECO:0000269|PubMed:23845380"
FT SITE 87..88
FT /note="Cleavage; by MMP2"
FT /evidence="ECO:0000269|PubMed:23845380"
FT SITE 114..115
FT /note="Cleavage; by MMP13"
FT /evidence="ECO:0000250|UniProtKB:P58874"
FT MOD_RES 65
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 71
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 139
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 289..322
FT /evidence="ECO:0000250"
FT VARIANT 182
FT /note="I -> T (in dbSNP:rs139024490)"
FT /evidence="ECO:0000269|PubMed:12019215"
FT /id="VAR_055228"
FT VARIANT 229
FT /note="R -> C (in dbSNP:rs150633473)"
FT /evidence="ECO:0000269|PubMed:12019215"
FT /id="VAR_055229"
FT VARIANT 325
FT /note="R -> W (in dbSNP:rs56219555)"
FT /evidence="ECO:0000269|PubMed:12019215"
FT /id="VAR_055230"
SQ SEQUENCE 332 AA; 37261 MW; 8060B4C46DF41C20 CRC64;
MRLLAFLSLL ALVLQETGTA SLPRKERKRR EEQMPREGDS FEVLPLRNDV LNPDNYGEVI
DLSNYEELTD YGDQLPEVKV TSLAPATSIS PAKSTTAPGT PSSNPTMTRP TTAGLLLSSQ
PNHGLPTCLV CVCLGSSVYC DDIDLEDIPP LPRRTAYLYA RFNRISRIRA EDFKGLTKLK
RIDLSNNLIS SIDNDAFRLL HALQDLILPE NQLEALPVLP SGIEFLDVRL NRLQSSGIQP
AAFRAMEKLQ FLYLSDNLLD SIPGPLPLSL RSVHLQNNLI ETMQRDVFCD PEEHKHTRRQ
LEDIRLDGNP INLSLFPSAY FCLPRLPIGR FT
