ID MIME_MOUSE Reviewed; 298 AA. AC Q62000; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Mimecan; DE AltName: Full=Osteoglycin; DE Flags: Precursor; GN Name=Ogn; Synonyms=Og; 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 [MRNA]. RC STRAIN=BALB/cJ; TISSUE=Limb bud; RX PubMed=7607548; DOI=10.1016/0378-1119(95)00070-m; RA Ujita M., Shinomura T., Kimata K.; RT "Molecular cloning of the mouse osteoglycin-encoding gene."; RL Gene 158:237-240(1995). RN [2] 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, and Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Induces bone formation in conjunction with TGF-beta-1 or TGF- CC beta-2. {ECO:0000250|UniProtKB:P19879}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250|UniProtKB:Q8MJF1}. CC -!- PTM: Contains keratan sulfate. {ECO:0000250|UniProtKB:P19879}. 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; D31951; BAA06721.1; -; mRNA. DR EMBL; BC021939; AAH21939.1; -; mRNA. DR CCDS; CCDS26505.1; -. DR PIR; JC4130; JC4130. DR RefSeq; NP_032786.1; NM_008760.4. DR AlphaFoldDB; Q62000; -. DR SMR; Q62000; -. DR BioGRID; 201907; 1. DR IntAct; Q62000; 15. DR STRING; 10090.ENSMUSP00000021822; -. DR GlyCosmos; Q62000; 1 site, No reported glycans. DR GlyGen; Q62000; 2 sites. DR iPTMnet; Q62000; -. DR PhosphoSitePlus; Q62000; -. DR CPTAC; non-CPTAC-4048; -. DR MaxQB; Q62000; -. DR PaxDb; 10090-ENSMUSP00000021822; -. DR PeptideAtlas; Q62000; -. DR ProteomicsDB; 295606; -. DR Pumba; Q62000; -. DR Antibodypedia; 2122; 342 antibodies from 34 providers. DR DNASU; 18295; -. DR Ensembl; ENSMUST00000021822.7; ENSMUSP00000021822.6; ENSMUSG00000021390.7. DR GeneID; 18295; -. DR KEGG; mmu:18295; -. DR UCSC; uc007qjr.1; mouse. DR AGR; MGI:109278; -. DR CTD; 4969; -. DR MGI; MGI:109278; Ogn. DR VEuPathDB; HostDB:ENSMUSG00000021390; -. DR eggNOG; KOG0619; Eukaryota. DR GeneTree; ENSGT00940000157238; -. DR HOGENOM; CLU_067583_1_0_1; -. DR InParanoid; Q62000; -. DR OMA; RIIHLQF; -. DR OrthoDB; 1080036at2759; -. DR PhylomeDB; Q62000; -. DR TreeFam; TF351924; -. DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis. DR Reactome; R-MMU-2022857; Keratan sulfate degradation. DR BioGRID-ORCS; 18295; 1 hit in 77 CRISPR screens. DR ChiTaRS; Ogn; mouse. DR PRO; PR:Q62000; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q62000; Protein. DR Bgee; ENSMUSG00000021390; Expressed in aorta tunica media and 238 other cell types or tissues. DR ExpressionAtlas; Q62000; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0061975; P:articular cartilage development; IBA:GO_Central. DR GO; GO:0060348; P:bone development; IBA:GO_Central. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI. 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:SF1; MIMECAN; 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; Q62000; MM. PE 1: Evidence at protein level; KW Disulfide bond; Extracellular matrix; Glycoprotein; Growth factor; KW Leucine-rich repeat; Proteoglycan; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..298 FT /note="Mimecan" FT /id="PRO_0000032761" FT REPEAT 112..131 FT /note="LRR 1" FT REPEAT 132..155 FT /note="LRR 2" FT REPEAT 156..179 FT /note="LRR 3" FT REPEAT 180..199 FT /note="LRR 4" FT REPEAT 200..225 FT /note="LRR 5" FT REPEAT 226..246 FT /note="LRR 6" FT REPEAT 247..277 FT /note="LRR 7" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 258 FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine" FT /evidence="ECO:0000255" FT DISULFID 255..288 FT /evidence="ECO:0000250|UniProtKB:P19879" SQ SEQUENCE 298 AA; 34012 MW; 0C5DB4A5AB6B05FE CRC64; METVHSTFLL LLFVPLTQQA PQSQLDSHVN YEYATGNSEE TKFSQDYEDK YLDGKSIKEK ETMIIPDEKS LQLQKDEVIP SLPTKKENDE MPTCLLCVCL SGSVYCEEVD IDAVPPLPKE SAYLYARFNK IKKLTAKDFA DMPNLRRLDF TGNLIEDIED GTFSKLSLLE ELTLAENQLL RLPVLPPKLT LLNAKHNKIK SKGIKANTFK KLNKLSFLYL DHNDLESVPP NLPESLRVIH LQFNSISSLT DDTFCKANDT RYIRERIEEI RLEGNPIALG KHPNSFICLK RLPIGSYF //