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Protein

Decorin

Gene

Dcn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May affect the rate of fibrils formation (By similarity). May be implicated in the dilatation of the rat cervix.By similarity

GO - Molecular functioni

  • collagen binding Source: RGD
  • extracellular matrix binding Source: Ensembl
  • glycosaminoglycan binding Source: Ensembl
  • poly(A) RNA binding Source: Ensembl
  • protein kinase inhibitor activity Source: GO_Central
  • protein N-terminus binding Source: RGD

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Decorin
Alternative name(s):
Bone proteoglycan II
Dermatan sulfate proteoglycan-II
Short name:
DSPG
PG-S2
PG40
Gene namesi
Name:Dcn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi61895. Dcn.

Subcellular locationi

GO - Cellular componenti

  • collagen type VI trimer Source: RGD
  • cytoplasm Source: GO_Central
  • extracellular space Source: Ensembl
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
PropeptideiPRO_000003271917 – 302 PublicationsAdd BLAST14
ChainiPRO_000003272031 – 354DecorinAdd BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34O-linked (Xyl...) (glycosaminoglycan)By similarity1
Disulfide bondi49 ↔ 55By similarity
Disulfide bondi53 ↔ 62By similarity
Glycosylationi206N-linked (GlcNAc...)Sequence analysis1
Glycosylationi241N-linked (GlcNAc...)Sequence analysis1
Glycosylationi257N-linked (GlcNAc...)Sequence analysis1
Glycosylationi298N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi308 ↔ 341By similarity

Post-translational modificationi

The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiQ01129.
PRIDEiQ01129.

PTM databases

iPTMnetiQ01129.
PhosphoSitePlusiQ01129.

Expressioni

Developmental stagei

The amount of DSPG per cervix increases 4-fold during pregnancy, then falls precipitously within 1 day post partum.

Gene expression databases

BgeeiENSRNOG00000004554.
GenevisibleiQ01129. RN.

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 (By similarity).By similarity

GO - Molecular functioni

  • collagen binding Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi247822. 4 interactors.
STRINGi10116.ENSRNOP00000006070.

Structurei

3D structure databases

ProteinModelPortaliQ01129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati68 – 88LRR 1Add BLAST21
Repeati89 – 112LRR 2Add BLAST24
Repeati113 – 136LRR 3Add BLAST24
Repeati137 – 157LRR 4Add BLAST21
Repeati158 – 181LRR 5Add BLAST24
Repeati182 – 207LRR 6Add BLAST26
Repeati208 – 228LRR 7Add BLAST21
Repeati229 – 252LRR 8Add BLAST24
Repeati253 – 276LRR 9Add BLAST24
Repeati277 – 299LRR 10Add BLAST23
Repeati300 – 329LRR 11Add BLAST30
Repeati330 – 354LRR 12Add BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi49 – 62Cys-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.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiQ01129.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG091G044B.
PhylomeDBiQ01129.
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.

Q01129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATLVLFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP
60 70 80 90 100
YRCQCHLRVV QCSDLGLDKV PWEFPPDTTL LDLQNNKITE IKEGAFKNLK
110 120 130 140 150
DLHTLILVNN KISKISPEAF KPLVKLERLY LSKNHLKELP EKLPKTLQEL
160 170 180 190 200
RLHDNEITKL KKSVFNGLNR MIVIELGGNP LKNSGIENGA LQGMKGLGYI
210 220 230 240 250
RISDTNITAI PQGLPTSISE LHLDGNKIAK VDAASLKGMS NLSKLGLSFN
260 270 280 290 300
SITVVENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYVQ VVYLHNNNIS
310 320 330 340 350
EVGQHDFCLP SYQTRKTSYT AVSLYSNPVR YWQIHPHTFR CVFGRSTIQL

GNYK
Length:354
Mass (Da):39,805
Last modified:April 1, 1993 - v1
Checksum:i152D92F42D9F5A5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12298 mRNA. Translation: CAA78170.1.
BC083750 mRNA. Translation: AAH83750.1.
X59859 mRNA. Translation: CAA42519.1.
PIRiS29145.
RefSeqiNP_077043.1. NM_024129.1.
XP_006241347.1. XM_006241285.1.
UniGeneiRn.106103.

Genome annotation databases

EnsembliENSRNOT00000006070; ENSRNOP00000006070; ENSRNOG00000004554.
GeneIDi29139.
KEGGirno:29139.
UCSCiRGD:61895. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12298 mRNA. Translation: CAA78170.1.
BC083750 mRNA. Translation: AAH83750.1.
X59859 mRNA. Translation: CAA42519.1.
PIRiS29145.
RefSeqiNP_077043.1. NM_024129.1.
XP_006241347.1. XM_006241285.1.
UniGeneiRn.106103.

3D structure databases

ProteinModelPortaliQ01129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247822. 4 interactors.
STRINGi10116.ENSRNOP00000006070.

PTM databases

iPTMnetiQ01129.
PhosphoSitePlusiQ01129.

Proteomic databases

PaxDbiQ01129.
PRIDEiQ01129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006070; ENSRNOP00000006070; ENSRNOG00000004554.
GeneIDi29139.
KEGGirno:29139.
UCSCiRGD:61895. rat.

Organism-specific databases

CTDi1634.
RGDi61895. Dcn.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiQ01129.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG091G044B.
PhylomeDBiQ01129.
TreeFamiTF334562.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ01129.

Gene expression databases

BgeeiENSRNOG00000004554.
GenevisibleiQ01129. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q01129
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.