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Protein

Decorin

Gene

DCN

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May affect the rate of fibrils formation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-BTA-2022870. Chondroitin sulfate biosynthesis.
R-BTA-2022923. Dermatan sulfate biosynthesis.
R-BTA-2024101. CS/DS degradation.
R-BTA-3000178. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Decorin
Alternative name(s):
Bone proteoglycan II
PG-S2
Gene namesi
Name:DCN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Propeptidei17 – 30141 PublicationPRO_0000032703Add
BLAST
Chaini31 – 360330DecorinPRO_0000032704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341O-linked (Xyl...) (glycosaminoglycan)2 Publications
Disulfide bondi55 ↔ 611 Publication
Disulfide bondi59 ↔ 681 Publication
Glycosylationi212 – 2121N-linked (GlcNAc...)1 Publication
Glycosylationi263 – 2631N-linked (GlcNAc...)1 Publication
Glycosylationi304 – 3041N-linked (GlcNAc...)1 Publication
Disulfide bondi314 ↔ 3471 Publication

Post-translational modificationi

The attached glycosaminoglycan chain can be either chondroitin 4-sulfate, chondroitin 6-sulfate or dermatan sulfate, depending upon the tissue of origin.

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP21793.
PRIDEiP21793.

Interactioni

Subunit structurei

Binds to type I and type II collagen, fibronectin and TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT.3 Publications

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000004562.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 623Combined sources
Beta strandi65 – 673Combined sources
Beta strandi86 – 883Combined sources
Turni99 – 1046Combined sources
Beta strandi110 – 1123Combined sources
Turni123 – 1286Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi155 – 1573Combined sources
Helixi168 – 1714Combined sources
Beta strandi179 – 1813Combined sources
Helixi189 – 1913Combined sources
Helixi196 – 1994Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi225 – 2284Combined sources
Helixi240 – 2423Combined sources
Beta strandi250 – 2523Combined sources
Turni263 – 2653Combined sources
Helixi266 – 2683Combined sources
Beta strandi274 – 2763Combined sources
Turni287 – 2915Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi332 – 3354Combined sources
Helixi337 – 3393Combined sources
Helixi342 – 3454Combined sources
Helixi351 – 3533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XCDX-ray2.31A31-359[»]
1XECX-ray2.30A/B31-359[»]
1XKUX-ray2.15A31-360[»]
DisProtiDP00489.
ProteinModelPortaliP21793.
SMRiP21793. Positions 52-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati74 – 9421LRR 1Add
BLAST
Repeati95 – 11824LRR 2Add
BLAST
Repeati119 – 14224LRR 3Add
BLAST
Repeati143 – 16321LRR 4Add
BLAST
Repeati164 – 18724LRR 5Add
BLAST
Repeati188 – 21326LRR 6Add
BLAST
Repeati214 – 23421LRR 7Add
BLAST
Repeati235 – 25824LRR 8Add
BLAST
Repeati259 – 28224LRR 9Add
BLAST
Repeati283 – 30523LRR 10Add
BLAST
Repeati306 – 33530LRR 11Add
BLAST
Repeati336 – 36025LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 6814Cys-richAdd
BLAST

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOVERGENiHBG016052.
InParanoidiP21793.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG76739V.
TreeFamiTF334562.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028549. Decorin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF5. PTHR24369:SF5. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATIIFLLV AQVSWAGPFQ QKGLFDFMLE DEASGIGPEE HFPEVPEIEP
60 70 80 90 100
MGPVCPFRCQ CHLRVVQCSD LGLEKVPKDL PPDTALLDLQ NNKITEIKDG
110 120 130 140 150
DFKNLKNLHT LILINNKISK ISPGAFAPLV KLERLYLSKN QLKELPEKMP
160 170 180 190 200
KTLQELRVHE NEITKVRKSV FNGLNQMIVV ELGTNPLKSS GIENGAFQGM
210 220 230 240 250
KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA SLKGLNNLAK
260 270 280 290 300
LGLSFNSISA VDNGSLANTP HLRELHLNNN KLVKVPGGLA DHKYIQVVYL
310 320 330 340 350
HNNNISAIGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV
360
RAAVQLGNYK
Length:360
Mass (Da):39,879
Last modified:July 5, 2005 - v2
Checksum:iF7B5B61C2A67CB5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2831V → A in CAA68702 (PubMed:3435485).Curated
Sequence conflicti289 – 2891L → V in CAA68702 (PubMed:3435485).Curated
Sequence conflicti308 – 3103IGS → NRL in BAC56458 (PubMed:12658628).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00712 mRNA. Translation: CAA68702.1.
AY781101 mRNA. Translation: AAV37207.1.
BT021076 mRNA. Translation: AAX09093.1.
BC105175 mRNA. Translation: AAI05176.1.
AB098914 mRNA. Translation: BAC56404.1.
AB098955 mRNA. Translation: BAC56445.1.
AB098968 mRNA. Translation: BAC56458.1.
AB099051 mRNA. Translation: BAC56541.1.
AB099061 mRNA. Translation: BAC56551.1.
PIRiS06280.
RefSeqiNP_776331.2. NM_173906.4.
XP_005206096.1. XM_005206039.1.
UniGeneiBt.23178.

Genome annotation databases

EnsembliENSBTAT00000004562; ENSBTAP00000004562; ENSBTAG00000003505.
GeneIDi280760.
KEGGibta:280760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00712 mRNA. Translation: CAA68702.1.
AY781101 mRNA. Translation: AAV37207.1.
BT021076 mRNA. Translation: AAX09093.1.
BC105175 mRNA. Translation: AAI05176.1.
AB098914 mRNA. Translation: BAC56404.1.
AB098955 mRNA. Translation: BAC56445.1.
AB098968 mRNA. Translation: BAC56458.1.
AB099051 mRNA. Translation: BAC56541.1.
AB099061 mRNA. Translation: BAC56551.1.
PIRiS06280.
RefSeqiNP_776331.2. NM_173906.4.
XP_005206096.1. XM_005206039.1.
UniGeneiBt.23178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XCDX-ray2.31A31-359[»]
1XECX-ray2.30A/B31-359[»]
1XKUX-ray2.15A31-360[»]
DisProtiDP00489.
ProteinModelPortaliP21793.
SMRiP21793. Positions 52-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000004562.

Proteomic databases

PaxDbiP21793.
PRIDEiP21793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000004562; ENSBTAP00000004562; ENSBTAG00000003505.
GeneIDi280760.
KEGGibta:280760.

Organism-specific databases

CTDi1634.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOVERGENiHBG016052.
InParanoidiP21793.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG76739V.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiR-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-BTA-2022870. Chondroitin sulfate biosynthesis.
R-BTA-2022923. Dermatan sulfate biosynthesis.
R-BTA-2024101. CS/DS degradation.
R-BTA-3000178. ECM proteoglycans.

Miscellaneous databases

EvolutionaryTraceiP21793.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028549. Decorin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF5. PTHR24369:SF5. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of the cDNA for small proteoglycan II of bovine bone."
    Day A.A., McQuillan C.I., Termine J.D., Young M.R.
    Biochem. J. 248:801-805(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of the bovine decorin gene."
    Khatib H.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.
  5. "Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
    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.
    Mol. Reprod. Dev. 65:9-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 AND 214-360.
  6. "Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography."
    Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C., Neame P.J.
    J. Biol. Chem. 264:2876-2884(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-54.
  7. "The NH2-terminal amino acid sequence of bovine skin proteodermatan sulfate."
    Pearson C.H., Winterbottom N., Fackre D.S., Scott P.G., Carpenter M.R.
    J. Biol. Chem. 258:15101-15104(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-34.
  8. "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."
    Chopra R.K., Pearson C.H., Pringle G.A., Fackre D.S., Scott P.G.
    Biochem. J. 232:277-279(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-34.
  9. "Extracellular matrix 22-kDa protein interacts with decorin core protein and is expressed in cutaneous fibrosis."
    Okamoto O., Suzuki Y., Kimura S., Shinkai H.
    J. Biochem. 119:106-114(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DPT.
  10. "Dermatopontin interacts with transforming growth factor beta and enhances its biological activity."
    Okamoto O., Fujiwara S., Abe M., Sato Y.
    Biochem. J. 337:537-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DPT.
  11. "Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1."
    Reinboth B., Hanssen E., Cleary E.G., Gibson M.A.
    J. Biol. Chem. 277:3950-3957(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MFAP2 AND ELN.
  12. "Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan."
    Scott P.G., McEwan P.A., Dodd C.M., Bergmann E.M., Bishop P.N., Bella J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15633-15638(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 31-360, DISULFIDE BONDS, GLYCOSYLATION AT ASN-212; ASN-263 AND ASN-304.

Entry informationi

Entry nameiPGS2_BOVIN
AccessioniPrimary (citable) accession number: P21793
Secondary accession number(s): Q3MHN1
, Q5U7W0, Q861V7, Q862D9, Q862E8, Q862L4, Q862R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 5, 2005
Last modified: June 8, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.