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 24-JAN-2024, entry version 182. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9UBM4; 1 site, No reported glycans. DR GlyGen; Q9UBM4; 1 site. DR iPTMnet; Q9UBM4; -. DR PhosphoSitePlus; Q9UBM4; -. DR BioMuta; OPTC; -. DR DMDM; 8928250; -. DR MassIVE; Q9UBM4; -. DR PaxDb; 9606-ENSP00000356191; -. DR PeptideAtlas; Q9UBM4; -. DR ProteomicsDB; 84008; -. DR Antibodypedia; 34546; 135 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 AGR; HGNC:8158; -. 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; EEHKYTR; -. DR OrthoDB; 1080036at2759; -. 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; 12 hits in 1140 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 82 other cell types or tissues. DR ExpressionAtlas; Q9UBM4; baseline and differential. 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:0061975; P:articular cartilage development; IBA:GO_Central. DR GO; GO:0060348; P:bone development; IBA:GO_Central. DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR043547; Mimecan/Epiphycan/Opticin. DR PANTHER; PTHR46269; EPIPHYCAN-RELATED; 1. DR PANTHER; PTHR46269:SF4; OPTICIN; 1. DR Pfam; PF13855; LRR_8; 1. DR SMART; SM00369; LRR_TYP; 4. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 4. DR Genevisible; Q9UBM4; HS. 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 //