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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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16By similarityAdd BLAST16
PropeptideiPRO_000003270317 – 301 PublicationAdd BLAST14
ChainiPRO_000003270431 – 360DecorinAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34O-linked (Xyl...) (glycosaminoglycan)2 Publications1
Disulfide bondi55 ↔ 611 Publication
Disulfide bondi59 ↔ 681 Publication
Glycosylationi212N-linked (GlcNAc...)1 Publication1
Glycosylationi263N-linked (GlcNAc...)1 Publication1
Glycosylationi304N-linked (GlcNAc...)1 Publication1
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.
PeptideAtlasiP21793.
PRIDEiP21793.

Expressioni

Gene expression databases

BgeeiENSBTAG00000003505.

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

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 62Combined sources3
Beta strandi65 – 67Combined sources3
Beta strandi86 – 88Combined sources3
Turni99 – 104Combined sources6
Beta strandi110 – 112Combined sources3
Turni123 – 128Combined sources6
Beta strandi134 – 136Combined sources3
Beta strandi155 – 157Combined sources3
Helixi168 – 171Combined sources4
Beta strandi179 – 181Combined sources3
Helixi189 – 191Combined sources3
Helixi196 – 199Combined sources4
Beta strandi205 – 207Combined sources3
Beta strandi225 – 228Combined sources4
Helixi240 – 242Combined sources3
Beta strandi250 – 252Combined sources3
Turni263 – 265Combined sources3
Helixi266 – 268Combined sources3
Beta strandi274 – 276Combined sources3
Turni287 – 291Combined sources5
Beta strandi297 – 299Combined sources3
Beta strandi312 – 314Combined sources3
Beta strandi326 – 329Combined sources4
Beta strandi332 – 335Combined sources4
Helixi337 – 339Combined sources3
Helixi342 – 345Combined sources4
Helixi351 – 353Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP21793.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati74 – 94LRR 1Add BLAST21
Repeati95 – 118LRR 2Add BLAST24
Repeati119 – 142LRR 3Add BLAST24
Repeati143 – 163LRR 4Add BLAST21
Repeati164 – 187LRR 5Add BLAST24
Repeati188 – 213LRR 6Add BLAST26
Repeati214 – 234LRR 7Add BLAST21
Repeati235 – 258LRR 8Add BLAST24
Repeati259 – 282LRR 9Add BLAST24
Repeati283 – 305LRR 10Add BLAST23
Repeati306 – 335LRR 11Add BLAST30
Repeati336 – 360LRR 12Add BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi55 – 68Cys-richAdd BLAST14

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.
OrthoDBiEOG091G044B.
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)DescriptionActionsGraphical viewLength
Sequence conflicti283V → A in CAA68702 (PubMed:3435485).Curated1
Sequence conflicti289L → V in CAA68702 (PubMed:3435485).Curated1
Sequence conflicti308 – 310IGS → NRL in BAC56458 (PubMed:12658628).Curated3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XCDX-ray2.31A31-359[»]
1XECX-ray2.30A/B31-359[»]
1XKUX-ray2.15A31-360[»]
DisProtiDP00489.
ProteinModelPortaliP21793.
SMRiP21793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000004562.

Proteomic databases

PaxDbiP21793.
PeptideAtlasiP21793.
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.
OrthoDBiEOG091G044B.
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.

Gene expression databases

BgeeiENSBTAG00000003505.

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...

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: November 2, 2016
This is version 143 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.