PGS2_BOVIN
ID PGS2_BOVIN Reviewed; 360 AA.
AC P21793; Q3MHN1; Q5U7W0; Q861V7; Q862D9; Q862E8; Q862L4; Q862R5;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Decorin;
DE AltName: Full=Bone proteoglycan II;
DE AltName: Full=PG-S2;
DE Flags: Precursor;
GN Name=DCN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3435485; DOI=10.1042/bj2480801;
RA Day A.A., McQuillan C.I., Termine J.D., Young M.R.;
RT "Molecular cloning and sequence analysis of the cDNA for small proteoglycan
RT II of bovine bone.";
RL Biochem. J. 248:801-805(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Khatib H.;
RT "Sequence of the bovine decorin gene.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 AND 214-360.
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [6]
RP PROTEIN SEQUENCE OF 31-54.
RX PubMed=2914936; DOI=10.1016/s0021-9258(19)81694-0;
RA Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C., Neame P.J.;
RT "Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-
RT PGII, from bovine articular cartilage and skin isolated by octyl-sepharose
RT chromatography.";
RL J. Biol. Chem. 264:2876-2884(1989).
RN [7]
RP GLYCOSYLATION AT SER-34.
RX PubMed=6654908; DOI=10.1016/s0021-9258(17)43777-x;
RA Pearson C.H., Winterbottom N., Fackre D.S., Scott P.G., Carpenter M.R.;
RT "The NH2-terminal amino acid sequence of bovine skin proteodermatan
RT sulfate.";
RL J. Biol. Chem. 258:15101-15104(1983).
RN [8]
RP GLYCOSYLATION AT SER-34.
RX PubMed=3936484; DOI=10.1042/bj2320277;
RA Chopra R.K., Pearson C.H., Pringle G.A., Fackre D.S., Scott P.G.;
RT "Dermatan sulphate is located on serine-4 of bovine skin proteodermatan
RT sulphate. Demonstration that most molecules possess only one
RT glycosaminoglycan chain and comparison of amino acid sequences around
RT glycosylation sites in different proteoglycans.";
RL Biochem. J. 232:277-279(1985).
RN [9]
RP INTERACTION WITH DPT.
RX PubMed=8907183; DOI=10.1093/oxfordjournals.jbchem.a021194;
RA Okamoto O., Suzuki Y., Kimura S., Shinkai H.;
RT "Extracellular matrix 22-kDa protein interacts with decorin core protein
RT and is expressed in cutaneous fibrosis.";
RL J. Biochem. 119:106-114(1996).
RN [10]
RP INTERACTION WITH DPT.
RX PubMed=9895299; DOI=10.1042/bj3370537;
RA Okamoto O., Fujiwara S., Abe M., Sato Y.;
RT "Dermatopontin interacts with transforming growth factor beta and enhances
RT its biological activity.";
RL Biochem. J. 337:537-541(1999).
RN [11]
RP INTERACTION WITH MFAP2 AND ELN.
RX PubMed=11723132; DOI=10.1074/jbc.m109540200;
RA Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.;
RT "Molecular interactions of biglycan and decorin with elastic fiber
RT components: biglycan forms a ternary complex with tropoelastin and
RT microfibril-associated glycoprotein 1.";
RL J. Biol. Chem. 277:3950-3957(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 31-360, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-212; ASN-263 AND ASN-304.
RX PubMed=15501918; DOI=10.1073/pnas.0402976101;
RA Scott P.G., McEwan P.A., Dodd C.M., Bergmann E.M., Bishop P.N., Bella J.;
RT "Crystal structure of the dimeric protein core of decorin, the archetypal
RT small leucine-rich repeat proteoglycan.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15633-15638(2004).
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 {ECO:0000269|PubMed:11723132, ECO:0000269|PubMed:8907183,
CC ECO:0000269|PubMed:9895299}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: The attached glycosaminoglycan chain can be either chondroitin 4-
CC sulfate, chondroitin 6-sulfate or dermatan sulfate, depending upon the
CC tissue of origin.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000305}.
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DR EMBL; Y00712; CAA68702.1; -; mRNA.
DR EMBL; AY781101; AAV37207.1; -; mRNA.
DR EMBL; BT021076; AAX09093.1; -; mRNA.
DR EMBL; BC105175; AAI05176.1; -; mRNA.
DR EMBL; AB098914; BAC56404.1; -; mRNA.
DR EMBL; AB098955; BAC56445.1; -; mRNA.
DR EMBL; AB098968; BAC56458.1; -; mRNA.
DR EMBL; AB099051; BAC56541.1; -; mRNA.
DR EMBL; AB099061; BAC56551.1; -; mRNA.
DR PIR; S06280; S06280.
DR RefSeq; NP_776331.2; NM_173906.4.
DR RefSeq; XP_005206096.1; XM_005206039.1.
DR PDB; 1XCD; X-ray; 2.31 A; A=31-359.
DR PDB; 1XEC; X-ray; 2.30 A; A/B=31-359.
DR PDB; 1XKU; X-ray; 2.15 A; A=31-360.
DR PDBsum; 1XCD; -.
DR PDBsum; 1XEC; -.
DR PDBsum; 1XKU; -.
DR AlphaFoldDB; P21793; -.
DR SMR; P21793; -.
DR CORUM; P21793; -.
DR IntAct; P21793; 1.
DR STRING; 9913.ENSBTAP00000004562; -.
DR iPTMnet; P21793; -.
DR PaxDb; P21793; -.
DR PeptideAtlas; P21793; -.
DR PRIDE; P21793; -.
DR Ensembl; ENSBTAT00000004562; ENSBTAP00000004562; ENSBTAG00000003505.
DR GeneID; 280760; -.
DR KEGG; bta:280760; -.
DR CTD; 1634; -.
DR VEuPathDB; HostDB:ENSBTAG00000003505; -.
DR VGNC; VGNC:27918; DCN.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158382; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; P21793; -.
DR OMA; MSQVIVM; -.
DR OrthoDB; 826997at2759; -.
DR TreeFam; TF334562; -.
DR Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-BTA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-BTA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-BTA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-BTA-2024101; CS/DS degradation.
DR Reactome; R-BTA-3000178; ECM proteoglycans.
DR EvolutionaryTrace; P21793; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000003505; Expressed in uterine cervix and 103 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:CAFA.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0098633; F:collagen fibril binding; IDA:CAFA.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:CAFA.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR DisProt; DP00489; -.
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; 7.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:Q01129"
FT PROPEP 17..30
FT /evidence="ECO:0000269|PubMed:2914936"
FT /id="PRO_0000032703"
FT CHAIN 31..360
FT /note="Decorin"
FT /id="PRO_0000032704"
FT REPEAT 74..94
FT /note="LRR 1"
FT REPEAT 95..118
FT /note="LRR 2"
FT REPEAT 119..142
FT /note="LRR 3"
FT REPEAT 143..163
FT /note="LRR 4"
FT REPEAT 164..187
FT /note="LRR 5"
FT REPEAT 188..213
FT /note="LRR 6"
FT REPEAT 214..234
FT /note="LRR 7"
FT REPEAT 235..258
FT /note="LRR 8"
FT REPEAT 259..282
FT /note="LRR 9"
FT REPEAT 283..305
FT /note="LRR 10"
FT REPEAT 306..335
FT /note="LRR 11"
FT REPEAT 336..360
FT /note="LRR 12"
FT CARBOHYD 34
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:3936484,
FT ECO:0000269|PubMed:6654908"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15501918"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15501918"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15501918"
FT DISULFID 55..61
FT /evidence="ECO:0000269|PubMed:15501918"
FT DISULFID 59..68
FT /evidence="ECO:0000269|PubMed:15501918"
FT DISULFID 314..347
FT /evidence="ECO:0000269|PubMed:15501918"
FT CONFLICT 283
FT /note="V -> A (in Ref. 1; CAA68702)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> V (in Ref. 1; CAA68702)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..310
FT /note="IGS -> NRL (in Ref. 5; BAC56458)"
FT /evidence="ECO:0000305"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1XKU"
FT TURN 99..104
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1XKU"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1XKU"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1XKU"
FT TURN 287..291
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1XKU"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1XKU"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1XKU"
SQ 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
