OPT_MOUSE
ID OPT_MOUSE Reviewed; 328 AA.
AC Q920A0; Q8K3K2; Q91ZZ9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Opticin;
DE AltName: Full=Oculoglycan;
DE Flags: Precursor;
GN Name=Optc; Synonyms=Opt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ;
RX PubMed=11527931;
RA Takanosu M., Boyd T.C., Le Goff M., Henry S.P., Zhang Y., Bishop P.N.,
RA Mayne R.;
RT "Structure, chromosomal location, and tissue-specific expression of the
RT mouse opticin gene.";
RL Invest. Ophthalmol. Vis. Sci. 42:2202-2210(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22159013; DOI=10.1167/iovs.11-8514;
RA Le Goff M.M., Lu H., Ugarte M., Henry S., Takanosu M., Mayne R.,
RA Bishop P.N.;
RT "The vitreous glycoprotein opticin inhibits preretinal
RT neovascularization.";
RL Invest. Ophthalmol. Vis. Sci. 53:228-234(2012).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29323130; DOI=10.1038/s41598-017-18047-w;
RA Farran A., Valverde-Franco G., Tio L., Lussier B., Fahmi H.,
RA Pelletier J.P., Bishop P.N., Monfort J., Martel-Pelletier J.;
RT "In vivo effect of opticin deficiency in cartilage in a surgically induced
RT mouse model of osteoarthritis.";
RL Sci. Rep. 8:457-457(2018).
CC -!- FUNCTION: Inhibits angiogenesis in the vitreous humor of the eye, and
CC therefore represses neovascularization (PubMed:22159013). Binds
CC collagen fibrils (By similarity). May be involved in collagen fiber
CC organization via regulation of other members of the small leucine-rich
CC repeat proteoglycan superfamily (PubMed:29323130).
CC {ECO:0000250|UniProtKB:P58874, ECO:0000269|PubMed:22159013,
CC ECO:0000269|PubMed:29323130}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58874}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P58874}.
CC -!- TISSUE SPECIFICITY: Expressed in cartilage (at protein level)
CC (PubMed:29323130). Expressed in the vitreous collagen, inner limiting
CC membrane, lens capsule, trabecular meshwork, anterior surface of the
CC iris, the area adjacent to the nonpigmented ciliary epithelium, and
CC weakly expressed in the retina of the eye (at protein level)
CC (PubMed:22159013). Expressed in the nonpigmented ciliary epithelium of
CC the eye (PubMed:11527931). {ECO:0000269|PubMed:11527931,
CC ECO:0000269|PubMed:22159013, ECO:0000269|PubMed:29323130}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the presumptive ciliary body during
CC development. {ECO:0000269|PubMed:11527931}.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:Q9UBM4}.
CC -!- PTM: Proteolytically cleaved by MMP1, MMP2, MMP3, MMP7, MMP8, MMP9,
CC ADAMTS4, and ADAMTS5 (By similarity). Proteolytically cleaved by MMP13
CC (By similarity). {ECO:0000250|UniProtKB:P58874,
CC ECO:0000250|UniProtKB:Q9UBM4}.
CC -!- DISRUPTION PHENOTYPE: Increased organization of cartilage collagen
CC fibers featuring more smaller diameter fibers that are closely packed
CC (PubMed:29323130). Dysregulation of small leucine-rich repeat
CC proteoglycan superfamily members in cartilage, including an increase in
CC Lum and Epyc, and a decrease in Fmod and Prelp (PubMed:29323130). In a
CC surgical osteoarthritis model, a reduction in cartilage degradation and
CC inflammatory markers, decreased loss of cartilage integrity, and
CC reduced synovial membrane thickness (PubMed:29323130). Decrease in
CC vitreous body vaso-obliteration upon hypoxia, and an increase in
CC preretinal neovascularization upon restoration of normoxia
CC (PubMed:22159013). {ECO:0000269|PubMed:22159013,
CC ECO:0000269|PubMed:29323130}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class III subfamily. {ECO:0000305}.
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DR EMBL; AF333980; AAL12835.1; -; mRNA.
DR EMBL; AF333981; AAL12836.1; -; Genomic_DNA.
DR EMBL; AY077682; AAL78287.1; -; mRNA.
DR RefSeq; NP_473417.2; NM_054076.3.
DR AlphaFoldDB; Q920A0; -.
DR SMR; Q920A0; -.
DR STRING; 10090.ENSMUSP00000120568; -.
DR GlyGen; Q920A0; 4 sites.
DR PhosphoSitePlus; Q920A0; -.
DR MaxQB; Q920A0; -.
DR PaxDb; Q920A0; -.
DR PRIDE; Q920A0; -.
DR ProteomicsDB; 294395; -.
DR DNASU; 269120; -.
DR GeneID; 269120; -.
DR KEGG; mmu:269120; -.
DR CTD; 26254; -.
DR MGI; MGI:2151113; Optc.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q920A0; -.
DR OrthoDB; 914775at2759; -.
DR PhylomeDB; Q920A0; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 269120; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Itpr1; mouse.
DR PRO; PR:Q920A0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q920A0; protein.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:MGI.
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; 5.
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..328
FT /note="Opticin"
FT /id="PRO_0000032766"
FT DOMAIN 112..149
FT /note="LRRNT"
FT REPEAT 150..171
FT /note="LRR 1"
FT REPEAT 174..195
FT /note="LRR 2"
FT REPEAT 198..219
FT /note="LRR 3"
FT REPEAT 244..265
FT /note="LRR 4"
FT REPEAT 266..286
FT /note="LRR 5"
FT REPEAT 296..316
FT /note="LRR 6"
FT SITE 20..21
FT /note="Cleavage; by MMP7"
FT /evidence="ECO:0000250|UniProtKB:Q9UBM4"
FT SITE 30..31
FT /note="Cleavage; by MMP7"
FT /evidence="ECO:0000250|UniProtKB:Q9UBM4"
FT SITE 111..112
FT /note="Cleavage; by MMP13"
FT /evidence="ECO:0000250|UniProtKB:P58874"
FT MOD_RES 69
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 285..318
FT /evidence="ECO:0000250"
FT CONFLICT 168
FT /note="D -> Y (in Ref. 1; AAL12836/AAL12835)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..287
FT /note="CDT -> SLS (in Ref. 1; AAL12836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 36422 MW; 3DF84F66FFC66DF3 CRC64;
MKFLAFLSLL SLVLQKAETA SLLGEREREE QSPEEGDTYA SLYVGNHTLS IEDYNEVIDL
SNYEELADYG DQIPEAKISN LTLPTRTSPT STVAQKTLSP NLTMAVPTTT GLLNSQSSHG
LPTCLVCVCL GSSVYCDDAD LENIPPLPQM TTYLYARFNH ISHIQAGDFK GLTKLRRIDL
SGNSISSIHN DALRLLPALQ DLILPENQLA ALPVLPSGIE FLDVRLNRLQ SSGIQPEAFV
ALKKLQFLYL ANNMLDSIPG PLPLSLRSLH LQNNMIETME SDTFCDTGEH RHERRQLEDI
RLDGNPINLS LFPEAYFCLP RLPVGHFT
