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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 N-terminus binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • kidney development Source: RGD
  • peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan Source: Ensembl
  • placenta development Source: RGD
  • positive regulation of autophagy Source: Ensembl
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • skeletal muscle tissue development Source: RGD
  • wound healing Source: RGD
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
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Propeptidei17 – 30142 PublicationsPRO_0000032719Add
BLAST
Chaini31 – 354324DecorinPRO_0000032720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341O-linked (Xyl...) (glycosaminoglycan)By similarity
Disulfide bondi49 ↔ 55By similarity
Disulfide bondi53 ↔ 62By similarity
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence analysis
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.

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

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 interactions.
STRINGi10116.ENSRNOP00000006070.

Structurei

3D structure databases

ProteinModelPortaliQ01129.
SMRiQ01129. Positions 48-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati68 – 8821LRR 1Add
BLAST
Repeati89 – 11224LRR 2Add
BLAST
Repeati113 – 13624LRR 3Add
BLAST
Repeati137 – 15721LRR 4Add
BLAST
Repeati158 – 18124LRR 5Add
BLAST
Repeati182 – 20726LRR 6Add
BLAST
Repeati208 – 22821LRR 7Add
BLAST
Repeati229 – 25224LRR 8Add
BLAST
Repeati253 – 27624LRR 9Add
BLAST
Repeati277 – 29923LRR 10Add
BLAST
Repeati300 – 32930LRR 11Add
BLAST
Repeati330 – 35425LRR 12Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 6214Cys-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.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiQ01129.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG76739V.
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.
SMRiQ01129. Positions 48-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247822. 4 interactions.
STRINGi10116.ENSRNOP00000006070.

PTM databases

iPTMnetiQ01129.

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.
OrthoDBiEOG76739V.
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

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin)."
    Abramson S.R., Woessner J.F.
    Biochim. Biophys. Acta 1132:225-227(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Uterus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  3. "Molecular characterization of vascular smooth muscle decorin: deduced core protein structure and regulation of gene expression."
    Asundi V.K., Dreher K.L.
    Eur. J. Cell Biol. 59:314-321(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-354.
  4. "Purification and characterization of a small dermatan sulphate proteoglycan implicated in the dilatation of the rat uterine cervix."
    Kokenyesi R., Woessner J.F.
    Biochem. J. 260:413-419(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-48 AND 171-191.
    Strain: Sprague-Dawley.
    Tissue: Uterus.
  5. Cited for: CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-16, CLEAVAGE OF PROPEPTIDE AFTER GLU-30, IDENTIFICATION BY MASS SPECTROMETRY.

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: June 8, 2016
This is version 135 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.