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Decorin (Bone proteoglycan II) (PG-S2)

 PGS2_BOVIN              Reviewed;         360 AA.
P21793; Q3MHN1; Q5U7W0; Q861V7; Q862D9; Q862E8; Q862L4; Q862R5;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
27-SEP-2017, entry version 147.
RecName: Full=Decorin;
AltName: Full=Bone proteoglycan II;
AltName: Full=PG-S2;
Flags: Precursor;
Name=DCN;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3435485; DOI=10.1042/bj2480801;
Day A.A., McQuillan C.I., Termine J.D., Young M.R.;
"Molecular cloning and sequence analysis of the cDNA for small
proteoglycan II of bovine bone.";
Biochem. J. 248:801-805(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Khatib H.;
"Sequence of the bovine decorin gene.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 AND 214-360.
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[6]
PROTEIN SEQUENCE OF 31-54.
PubMed=2914936;
Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C.,
Neame P.J.;
"Characterization of the dermatan sulfate proteoglycans, DS-PGI and
DS-PGII, from bovine articular cartilage and skin isolated by octyl-
sepharose chromatography.";
J. Biol. Chem. 264:2876-2884(1989).
[7]
GLYCOSYLATION AT SER-34.
PubMed=6654908;
Pearson C.H., Winterbottom N., Fackre D.S., Scott P.G.,
Carpenter M.R.;
"The NH2-terminal amino acid sequence of bovine skin proteodermatan
sulfate.";
J. Biol. Chem. 258:15101-15104(1983).
[8]
GLYCOSYLATION AT SER-34.
PubMed=3936484; DOI=10.1042/bj2320277;
Chopra R.K., Pearson C.H., Pringle G.A., Fackre D.S., Scott P.G.;
"Dermatan sulphate is located on serine-4 of bovine skin
proteodermatan sulphate. Demonstration that most molecules possess
only one glycosaminoglycan chain and comparison of amino acid
sequences around glycosylation sites in different proteoglycans.";
Biochem. J. 232:277-279(1985).
[9]
INTERACTION WITH DPT.
PubMed=8907183; DOI=10.1093/oxfordjournals.jbchem.a021194;
Okamoto O., Suzuki Y., Kimura S., Shinkai H.;
"Extracellular matrix 22-kDa protein interacts with decorin core
protein and is expressed in cutaneous fibrosis.";
J. Biochem. 119:106-114(1996).
[10]
INTERACTION WITH DPT.
PubMed=9895299; DOI=10.1042/bj3370537;
Okamoto O., Fujiwara S., Abe M., Sato Y.;
"Dermatopontin interacts with transforming growth factor beta and
enhances its biological activity.";
Biochem. J. 337:537-541(1999).
[11]
INTERACTION WITH MFAP2 AND ELN.
PubMed=11723132; DOI=10.1074/jbc.M109540200;
Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.;
"Molecular interactions of biglycan and decorin with elastic fiber
components: biglycan forms a ternary complex with tropoelastin and
microfibril-associated glycoprotein 1.";
J. Biol. Chem. 277:3950-3957(2002).
[12]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 31-360, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-212; ASN-263 AND ASN-304.
PubMed=15501918; DOI=10.1073/pnas.0402976101;
Scott P.G., McEwan P.A., Dodd C.M., Bergmann E.M., Bishop P.N.,
Bella J.;
"Crystal structure of the dimeric protein core of decorin, the
archetypal small leucine-rich repeat proteoglycan.";
Proc. Natl. Acad. Sci. U.S.A. 101:15633-15638(2004).
-!- FUNCTION: May affect the rate of fibrils formation.
-!- SUBUNIT: Binds to type I and type II collagen, fibronectin and
TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts
with DPT. {ECO:0000269|PubMed:11723132,
ECO:0000269|PubMed:8907183, ECO:0000269|PubMed:9895299}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- PTM: The attached glycosaminoglycan chain can be either
chondroitin 4-sulfate, chondroitin 6-sulfate or dermatan sulfate,
depending upon the tissue of origin.
-!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
family. SLRP class I subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00712; CAA68702.1; -; mRNA.
EMBL; AY781101; AAV37207.1; -; mRNA.
EMBL; BT021076; AAX09093.1; -; mRNA.
EMBL; BC105175; AAI05176.1; -; mRNA.
EMBL; AB098914; BAC56404.1; -; mRNA.
EMBL; AB098955; BAC56445.1; -; mRNA.
EMBL; AB098968; BAC56458.1; -; mRNA.
EMBL; AB099051; BAC56541.1; -; mRNA.
EMBL; AB099061; BAC56551.1; -; mRNA.
PIR; S06280; S06280.
RefSeq; NP_776331.2; NM_173906.4.
RefSeq; XP_005206096.1; XM_005206039.1.
UniGene; Bt.23178; -.
PDB; 1XCD; X-ray; 2.31 A; A=31-359.
PDB; 1XEC; X-ray; 2.30 A; A/B=31-359.
PDB; 1XKU; X-ray; 2.15 A; A=31-360.
PDBsum; 1XCD; -.
PDBsum; 1XEC; -.
PDBsum; 1XKU; -.
DisProt; DP00489; -.
ProteinModelPortal; P21793; -.
SMR; P21793; -.
CORUM; P21793; -.
STRING; 9913.ENSBTAP00000004562; -.
PaxDb; P21793; -.
PeptideAtlas; P21793; -.
PRIDE; P21793; -.
Ensembl; ENSBTAT00000004562; ENSBTAP00000004562; ENSBTAG00000003505.
GeneID; 280760; -.
KEGG; bta:280760; -.
CTD; 1634; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118969; -.
HOVERGEN; HBG016052; -.
InParanoid; P21793; -.
KO; K04660; -.
OMA; PLGPVCP; -.
OrthoDB; EOG091G044B; -.
TreeFam; TF334562; -.
Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
Reactome; R-BTA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-BTA-2022870; Chondroitin sulfate biosynthesis.
Reactome; R-BTA-2022923; Dermatan sulfate biosynthesis.
Reactome; R-BTA-2024101; CS/DS degradation.
Reactome; R-BTA-3000178; ECM proteoglycans.
EvolutionaryTrace; P21793; -.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000003505; -.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031012; C:extracellular matrix; IDA:CAFA.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005518; F:collagen binding; IEA:InterPro.
GO; GO:0098633; F:collagen fibril binding; IDA:CAFA.
GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:CAFA.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR028549; Decorin.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000372; LRRNT.
InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
PANTHER; PTHR24369:SF136; PTHR24369:SF136; 1.
Pfam; PF13855; LRR_8; 3.
Pfam; PF01462; LRRNT; 1.
PIRSF; PIRSF002490; SLRP_I; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 8.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Extracellular matrix; Glycoprotein;
Leucine-rich repeat; Proteoglycan; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 16 {ECO:0000250|UniProtKB:Q01129}.
PROPEP 17 30 {ECO:0000269|PubMed:2914936}.
/FTId=PRO_0000032703.
CHAIN 31 360 Decorin.
/FTId=PRO_0000032704.
REPEAT 74 94 LRR 1.
REPEAT 95 118 LRR 2.
REPEAT 119 142 LRR 3.
REPEAT 143 163 LRR 4.
REPEAT 164 187 LRR 5.
REPEAT 188 213 LRR 6.
REPEAT 214 234 LRR 7.
REPEAT 235 258 LRR 8.
REPEAT 259 282 LRR 9.
REPEAT 283 305 LRR 10.
REPEAT 306 335 LRR 11.
REPEAT 336 360 LRR 12.
COMPBIAS 55 68 Cys-rich.
CARBOHYD 34 34 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000269|PubMed:3936484,
ECO:0000269|PubMed:6654908}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15501918}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15501918}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15501918}.
DISULFID 55 61 {ECO:0000269|PubMed:15501918}.
DISULFID 59 68 {ECO:0000269|PubMed:15501918}.
DISULFID 314 347 {ECO:0000269|PubMed:15501918}.
CONFLICT 283 283 V -> A (in Ref. 1; CAA68702).
{ECO:0000305}.
CONFLICT 289 289 L -> V (in Ref. 1; CAA68702).
{ECO:0000305}.
CONFLICT 308 310 IGS -> NRL (in Ref. 5; BAC56458).
{ECO:0000305}.
STRAND 60 62 {ECO:0000244|PDB:1XKU}.
STRAND 65 67 {ECO:0000244|PDB:1XKU}.
STRAND 86 88 {ECO:0000244|PDB:1XKU}.
TURN 99 104 {ECO:0000244|PDB:1XKU}.
STRAND 110 112 {ECO:0000244|PDB:1XKU}.
TURN 123 128 {ECO:0000244|PDB:1XKU}.
STRAND 134 136 {ECO:0000244|PDB:1XKU}.
STRAND 155 157 {ECO:0000244|PDB:1XKU}.
HELIX 168 171 {ECO:0000244|PDB:1XKU}.
STRAND 179 181 {ECO:0000244|PDB:1XKU}.
HELIX 189 191 {ECO:0000244|PDB:1XKU}.
HELIX 196 199 {ECO:0000244|PDB:1XKU}.
STRAND 205 207 {ECO:0000244|PDB:1XKU}.
STRAND 225 228 {ECO:0000244|PDB:1XKU}.
HELIX 240 242 {ECO:0000244|PDB:1XKU}.
STRAND 250 252 {ECO:0000244|PDB:1XKU}.
TURN 263 265 {ECO:0000244|PDB:1XKU}.
HELIX 266 268 {ECO:0000244|PDB:1XKU}.
STRAND 274 276 {ECO:0000244|PDB:1XKU}.
TURN 287 291 {ECO:0000244|PDB:1XKU}.
STRAND 297 299 {ECO:0000244|PDB:1XKU}.
STRAND 312 314 {ECO:0000244|PDB:1XKU}.
STRAND 326 329 {ECO:0000244|PDB:1XKU}.
STRAND 332 335 {ECO:0000244|PDB:1XKU}.
HELIX 337 339 {ECO:0000244|PDB:1XKU}.
HELIX 342 345 {ECO:0000244|PDB:1XKU}.
HELIX 351 353 {ECO:0000244|PDB:1XKU}.
SEQUENCE 360 AA; 39879 MW; F7B5B61C2A67CB5E CRC64;
MKATIIFLLV AQVSWAGPFQ QKGLFDFMLE DEASGIGPEE HFPEVPEIEP MGPVCPFRCQ
CHLRVVQCSD LGLEKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK
ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKSV FNGLNQMIVV
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA
SLKGLNNLAK LGLSFNSISA VDNGSLANTP HLRELHLNNN KLVKVPGGLA DHKYIQVVYL
HNNNISAIGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RAAVQLGNYK


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