ID   OPT_CANLF               Reviewed;         327 AA.
AC   P83286;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Opticin;
DE   AltName: Full=Oculoglycan;
DE   Flags: Precursor;
GN   Name=OPTC; Synonyms=OPT;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Labrador retriever, and Samoyed; TISSUE=Retina;
RX   PubMed=11814684; DOI=10.1016/s0378-1119(01)00842-3;
RA   Pellegrini B., Acland G.M., Ray J.;
RT   "Cloning and characterization of opticin cDNA: evaluation as a candidate
RT   for canine oculo-skeletal dysplasia.";
RL   Gene 282:121-131(2002).
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:0000250|UniProtKB:P58874}.
CC   -!- TISSUE SPECIFICITY: Ocular tissues, cartilage, ligament, skin, muscle
CC       and testes. {ECO:0000269|PubMed:11814684}.
CC   -!- PTM: O-glycosylated. {ECO:0000305}.
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   -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:Q9UBM4}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class III subfamily. {ECO:0000305}.
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DR   EMBL; AY048585; AAL05430.1; -; mRNA.
DR   RefSeq; NP_001003056.1; NM_001003056.1.
DR   AlphaFoldDB; P83286; -.
DR   SMR; P83286; -.
DR   STRING; 9615.ENSCAFP00000013921; -.
DR   PaxDb; P83286; -.
DR   GeneID; 403591; -.
DR   KEGG; cfa:403591; -.
DR   CTD; 26254; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; P83286; -.
DR   OrthoDB; 914775at2759; -.
DR   Proteomes; UP000002254; Unplaced.
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   InterPro; IPR000372; LRRNT.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   2: Evidence at transcript 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..327
FT                   /note="Opticin"
FT                   /id="PRO_0000032764"
FT   DOMAIN          111..148
FT                   /note="LRRNT"
FT   REPEAT          149..170
FT                   /note="LRR 1"
FT   REPEAT          173..194
FT                   /note="LRR 2"
FT   REPEAT          197..218
FT                   /note="LRR 3"
FT   REPEAT          219..237
FT                   /note="LRR 4"
FT   REPEAT          243..263
FT                   /note="LRR 5"
FT   REPEAT          264..285
FT                   /note="LRR 6"
FT   REPEAT          295..315
FT                   /note="LRR 7"
FT   SITE            20..21
FT                   /note="Cleavage; by MMP7"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBM4"
FT   SITE            110..111
FT                   /note="Cleavage; by MMP13"
FT                   /evidence="ECO:0000250|UniProtKB:P58874"
FT   MOD_RES         61
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         67
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        284..317
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  36075 MW;  AA01D1F1EB453488 CRC64;
     MKLPAFLSLL ALVLLEAGTA SLPKERKRRD EMHGEGDSYV VLGNYVLGPD NYDEVIDLSD
     YEGLMDYGDQ LPEAKVTNLA PPTGISSAQS TMTPRTLSLK PTMIRPTELG VLGSPNSHGL
     PTCLICVCLG SSVYCDDADL ENIPPLPKTT TYLYARFNRI RRIRAGDFKG LTKLKRIDLS
     SNSISSIDDD ALRLLPALQD LILPENQLAA LPALPPAIEV LDARHNQLQS SGIQPEALRA
     LEKLQFLYLA DNLLDSIPGP LPPSLRSLHL QNNLIETMQT DAFCDPEEHK HSRRWLEDIR
     LDGNPINLGL FPSAYFCLPR LPTGHCC