ID   PGS2_MOUSE              Reviewed;         354 AA.
AC   P28654;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Decorin;
DE   AltName: Full=Bone proteoglycan II;
DE   AltName: Full=PG-S2;
DE   AltName: Full=PG40;
DE   Flags: Precursor;
GN   Name=Dcn;
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=NIH Swiss; TISSUE=Fibroblast;
RA   Naitoh Y., Suzuki S.;
RL   Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7961765; DOI=10.1016/s0021-9258(18)46924-4;
RA   Scholzen T., Solursh M., Suzuki S., Reiter R., Morgan J.L., Buchberg A.M.,
RA   Siracusa L.D., Iozzo R.V.;
RT   "The murine decorin. Complete cDNA cloning, genomic organization,
RT   chromosomal assignment, and expression during organogenesis and tissue
RT   differentiation.";
RL   J. Biol. Chem. 269:28270-28281(1994).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Pancreas;
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: May affect the rate of fibrils formation.
CC   -!- SUBUNIT: Binds to type I and type II collagen, fibronectin and TGF-
CC       beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix. Secreted {ECO:0000250|UniProtKB:P07585}.
CC   -!- PTM: The attached glycosaminoglycan chain can be either chondroitin
CC       sulfate or dermatan sulfate depending upon the tissue of origin.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
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DR   EMBL; X53929; CAA37876.1; -; mRNA.
DR   CCDS; CCDS24141.1; -.
DR   PIR; A55454; A55454.
DR   RefSeq; NP_001177380.1; NM_001190451.2.
DR   RefSeq; NP_031859.1; NM_007833.6.
DR   AlphaFoldDB; P28654; -.
DR   SMR; P28654; -.
DR   STRING; 10090.ENSMUSP00000100924; -.
DR   GlyConnect; 2250; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P28654; 5 sites, 1 glycan.
DR   GlyGen; P28654; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P28654; -.
DR   PhosphoSitePlus; P28654; -.
DR   CPTAC; non-CPTAC-3854; -.
DR   PaxDb; 10090-ENSMUSP00000100924; -.
DR   PeptideAtlas; P28654; -.
DR   ProteomicsDB; 288133; -.
DR   Pumba; P28654; -.
DR   Antibodypedia; 754; 692 antibodies from 40 providers.
DR   DNASU; 13179; -.
DR   Ensembl; ENSMUST00000105287.11; ENSMUSP00000100924.4; ENSMUSG00000019929.17.
DR   Ensembl; ENSMUST00000163448.4; ENSMUSP00000131431.3; ENSMUSG00000019929.17.
DR   GeneID; 13179; -.
DR   KEGG; mmu:13179; -.
DR   UCSC; uc007gwx.2; mouse.
DR   AGR; MGI:94872; -.
DR   CTD; 1634; -.
DR   MGI; MGI:94872; Dcn.
DR   VEuPathDB; HostDB:ENSMUSG00000019929; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158382; -.
DR   HOGENOM; CLU_000288_186_0_1; -.
DR   InParanoid; P28654; -.
DR   OMA; PFHQKGL; -.
DR   OrthoDB; 3953748at2759; -.
DR   PhylomeDB; P28654; -.
DR   TreeFam; TF334562; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   BioGRID-ORCS; 13179; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Dcn; mouse.
DR   PRO; PR:P28654; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P28654; Protein.
DR   Bgee; ENSMUSG00000019929; Expressed in skin of snout and 269 other cell types or tissues.
DR   ExpressionAtlas; P28654; baseline and differential.
DR   GO; GO:0005589; C:collagen type VI trimer; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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; IPR000372; LRRNT.
DR   InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF14; DECORIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   PIRSF; PIRSF002490; SLRP_I; 1.
DR   SMART; SM00364; LRR_BAC; 3.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 8.
DR   Genevisible; P28654; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250|UniProtKB:Q01129"
FT   PROPEP          17..30
FT                   /evidence="ECO:0000250|UniProtKB:Q01129"
FT                   /id="PRO_0000032711"
FT   CHAIN           31..354
FT                   /note="Decorin"
FT                   /id="PRO_0000032712"
FT   REPEAT          68..88
FT                   /note="LRR 1"
FT   REPEAT          89..112
FT                   /note="LRR 2"
FT   REPEAT          113..136
FT                   /note="LRR 3"
FT   REPEAT          137..157
FT                   /note="LRR 4"
FT   REPEAT          158..181
FT                   /note="LRR 5"
FT   REPEAT          182..207
FT                   /note="LRR 6"
FT   REPEAT          208..228
FT                   /note="LRR 7"
FT   REPEAT          229..252
FT                   /note="LRR 8"
FT   REPEAT          253..276
FT                   /note="LRR 9"
FT   REPEAT          277..299
FT                   /note="LRR 10"
FT   REPEAT          300..329
FT                   /note="LRR 11"
FT   REPEAT          330..354
FT                   /note="LRR 12"
FT   CARBOHYD        34
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P07585"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..55
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..341
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39809 MW;  F05B5CC08DCABF6F CRC64;
     MKATLIFFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP YRCQCHLRVV
     QCSDLGLDKV PWDFPPDTTL LDLQNNKITE IKEGAFKNLK DLHTLILVNN KISKISPEAF
     KPLVKLERLY LSKNQLKELP EKMPRTLQEL RVHENEITKL RKSDFNGLNN VLVIELGGNP
     LKNSGIENGA FQGLKSLSYI RISDTNITAI PQGLPTSLTE VHLDGNKITK VDAPSLKGLI
     NLSKLGLSFN SITVMENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYIQ VVYLHNNNIS
     AVGQNDFCRA GHPSRKASYS AVSLYGNPVR YWEIFPNTFR CVYVRSAIQL GNYK
//