PGS2_MOUSE
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 03-AUG-2022, entry version 175.
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.
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}.
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; 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 GlyGen; P28654; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P28654; -.
DR PhosphoSitePlus; P28654; -.
DR CPTAC; non-CPTAC-3854; -.
DR PaxDb; P28654; -.
DR PeptideAtlas; P28654; -.
DR PRIDE; P28654; -.
DR ProteomicsDB; 288133; -.
DR Antibodypedia; 754; 630 antibodies from 40 providers.
DR DNASU; 13179; -.
DR Ensembl; ENSMUST00000105287; ENSMUSP00000100924; ENSMUSG00000019929.
DR Ensembl; ENSMUST00000163448; ENSMUSP00000131431; ENSMUSG00000019929.
DR GeneID; 13179; -.
DR KEGG; mmu:13179; -.
DR UCSC; uc007gwx.2; mouse.
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; MSQVIVM; -.
DR OrthoDB; 826997at2759; -.
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 72 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 267 other tissues.
DR ExpressionAtlas; P28654; baseline and differential.
DR Genevisible; P28654; MM.
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:0031012; C:extracellular matrix; ISO:MGI.
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:0030021; F:extracellular matrix structural constituent conferring compression resistance; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO: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:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA: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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR028549; Decorin.
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:SF14; PTHR45712:SF14; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR PIRSF; PIRSF002490; SLRP_I; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 8.
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"
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
