ID   MIME_COTJA              Reviewed;         293 AA.
AC   Q9DE65;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Mimecan;
DE   AltName: Full=Osteoglycin;
DE   Flags: Precursor;
GN   Name=OGN;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cornea, and Sclera;
RX   PubMed=11102758; DOI=10.1016/s0945-053x(00)00116-5;
RA   Corpuz L.M., Dunlevy J.R., Hassell J.R., Conrad A.H., Conrad G.W.;
RT   "Molecular cloning and relative tissue expression of keratocan and mimecan
RT   in embryonic quail cornea.";
RL   Matrix Biol. 19:693-698(2000).
CC   -!- FUNCTION: Induces bone formation in conjunction with TGF-beta-1 or TGF-
CC       beta-2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class III subfamily. {ECO:0000305}.
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DR   EMBL; AF128224; AAG48157.1; -; mRNA.
DR   RefSeq; NP_001310151.1; NM_001323222.1.
DR   AlphaFoldDB; Q9DE65; -.
DR   SMR; Q9DE65; -.
DR   PRIDE; Q9DE65; -.
DR   GeneID; 107319663; -.
DR   KEGG; cjo:107319663; -.
DR   CTD; 4969; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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; IPR027211; Mimecan.
DR   InterPro; IPR043547; Mimecan/Epiphycan.
DR   PANTHER; PTHR46269; PTHR46269; 1.
DR   PANTHER; PTHR46269:SF1; PTHR46269:SF1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   PROSITE; PS51450; LRR; 4.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Growth factor;
KW   Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..293
FT                   /note="Mimecan"
FT                   /id="PRO_0000032763"
FT   REPEAT          107..126
FT                   /note="LRR 1"
FT   REPEAT          127..150
FT                   /note="LRR 2"
FT   REPEAT          151..174
FT                   /note="LRR 3"
FT   REPEAT          175..194
FT                   /note="LRR 4"
FT   REPEAT          195..220
FT                   /note="LRR 5"
FT   REPEAT          221..241
FT                   /note="LRR 6"
FT   REPEAT          242..272
FT                   /note="LRR 7"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        250..283
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33049 MW;  4EB15956100495D5 CRC64;
     MKTLQATFFL VAFVPLVKPA PPIQQDSPKF YEYDTDIVTG SLIQQDYEML PKDAIKDGTN
     VSLDTGLRLQ ADDSELSARP TKDTNLPTCL LCVCLSGSVY CEEIDIEAVP PLPKETAYLY
     ARFNKIKRIA VSDFADITTL RRIDFSGNMI EEIEDGAFSK LLLLEELSLA ENRLVKLPVL
     PPKLTTFNAN QNRIKSRGIK NNAFKKLTNL AYLYLGHNAL ESVPLNLPES LRILHLQHNN
     ITTITDDTFC KSNNTRYIRT RMDEIRMEGN PILLAKHVNA FSCLKTLPVG TYY