ID   OPT_BOVIN               Reviewed;         321 AA.
AC   P58874; P83285; Q6X8P9;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Opticin;
DE   AltName: Full=Oculoglycan;
DE   Flags: Precursor;
GN   Name=OPTC; Synonyms=OPT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, AND HOMODIMERIZATION.
RC   TISSUE=Eye;
RX   PubMed=12951322; DOI=10.1074/jbc.m303117200;
RA   Le Goff M.M., Hindson V.J., Jowitt T.A., Scott P.G., Bishop P.N.;
RT   "Characterization of opticin and evidence of stable dimerization in
RT   solution.";
RL   J. Biol. Chem. 278:45280-45287(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-25; 188-192; 227-233; 238-243; 288-294 AND 295-309,
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
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   [3]
RP   CLEAVAGE BY MMP13.
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).
CC   -!- FUNCTION: Inhibits angiogenesis in the vitreous humor of the eye, and
CC       therefore represses neovascularization (By similarity). Binds collagen
CC       fibrils (PubMed:12951322, PubMed:10636917). May be involved in collagen
CC       fiber organization via regulation of other members of the small
CC       leucine-rich repeat proteoglycan superfamily (By similarity).
CC       {ECO:0000250|UniProtKB:Q920A0, ECO:0000269|PubMed:10636917,
CC       ECO:0000269|PubMed:12951322}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12951322}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:10636917}.
CC   -!- PTM: O-glycosylated (sialylated oligosaccharides).
CC       {ECO:0000269|PubMed:12951322}.
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       (PubMed:18164633). {ECO:0000250|UniProtKB:Q9UBM4,
CC       ECO:0000269|PubMed:18164633}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class III subfamily. {ECO:0000305}.
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DR   EMBL; AY249537; AAP76303.1; -; mRNA.
DR   RefSeq; NP_991339.1; NM_205770.1.
DR   RefSeq; XP_005216715.1; XM_005216658.3.
DR   AlphaFoldDB; P58874; -.
DR   SMR; P58874; -.
DR   STRING; 9913.ENSBTAP00000018286; -.
DR   PaxDb; P58874; -.
DR   Ensembl; ENSBTAT00000018286; ENSBTAP00000018286; ENSBTAG00000013764.
DR   GeneID; 404034; -.
DR   KEGG; bta:404034; -.
DR   CTD; 26254; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013764; -.
DR   VGNC; VGNC:32441; OPTC.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000154248; -.
DR   HOGENOM; CLU_067583_2_0_1; -.
DR   InParanoid; P58874; -.
DR   OMA; EHKYTRR; -.
DR   OrthoDB; 914775at2759; -.
DR   TreeFam; TF351924; -.
DR   Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000013764; Expressed in anterior segment of eyeball and 78 other tissues.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW   Signal; Sulfation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..321
FT                   /note="Opticin"
FT                   /id="PRO_0000180087"
FT   DOMAIN          105..142
FT                   /note="LRRNT"
FT   REPEAT          143..164
FT                   /note="LRR 1"
FT   REPEAT          167..188
FT                   /note="LRR 2"
FT   REPEAT          191..212
FT                   /note="LRR 3"
FT   REPEAT          237..258
FT                   /note="LRR 4"
FT   REPEAT          259..279
FT                   /note="LRR 5"
FT   REPEAT          289..309
FT                   /note="LRR 6"
FT   SITE            20..21
FT                   /note="Cleavage; by MMP7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBM4"
FT   SITE            104..105
FT                   /note="Cleavage; by MMP13"
FT                   /evidence="ECO:0000269|PubMed:18164633"
FT   SITE            109..110
FT                   /note="Cleavage; by MMP13"
FT                   /evidence="ECO:0000269|PubMed:18164633"
FT   MOD_RES         61
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        278..311
FT                   /evidence="ECO:0000250"
FT   CONFLICT        23
FT                   /note="S -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="L -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="L -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  35731 MW;  FB87F0CEEE7E0EC3 CRC64;
     MKLLALLSLL ILMLQEARTA SLSEEREGDP YAILHLGDYV LSLDNYDEVI DPSNYDELID
     YGDQLPQVKG TSLASLTRTR FTQSTEAART LPSNPTTARP PTLGLLAAPA NHGLPTCLIC
     VCLGSSVYCD DADLENIPPL PQTTAYLYAR FNRISHIRAG DFKGLTKLKR IDLSGNSISS
     IDDKALRLLP ALRDLILPEN KLVALPTLPT SIEVLDVRMN RLQSSGIQPE AFRALEKLQF
     LYLADNLLDA IPPSLPLSLR SLHLQNNMIE TMQRDAFCDA EEHRHTRRPL EDIRLDGNPI
     NLSLFPSAYF CLPRLPTGRF V