Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Decorin

Gene

Dcn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

May affect the rate of fibrils formation.

GO - Molecular functioni

  • extracellular matrix binding Source: MGI
  • glycosaminoglycan binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_294584. CS/DS degradation.
REACT_314166. Chondroitin sulfate biosynthesis.
REACT_326072. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_343463. Dermatan sulfate biosynthesis.
REACT_354321. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Decorin
Alternative name(s):
Bone proteoglycan II
PG-S2
PG40
Gene namesi
Name:Dcn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:94872. Dcn.

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 – 1616Sequence AnalysisAdd
BLAST
Propeptidei17 – 3014PRO_0000032711Add
BLAST
Chaini31 – 354324DecorinPRO_0000032712Add
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

MaxQBiP28654.
PaxDbiP28654.
PRIDEiP28654.

PTM databases

PhosphoSiteiP28654.

Expressioni

Gene expression databases

BgeeiP28654.
CleanExiMM_DCN.
ExpressionAtlasiP28654. baseline and differential.
GenevisibleiP28654. MM.

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

Protein-protein interaction databases

IntActiP28654. 1 interaction.
MINTiMINT-4107388.
STRINGi10090.ENSMUSP00000100924.

Structurei

3D structure databases

ProteinModelPortaliP28654.
SMRiP28654. 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

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP28654.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG76739V.
PhylomeDBiP28654.
TreeFamiTF334562.

Family and domain databases

InterProiIPR028549. Decorin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
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. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATLIFFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP
60 70 80 90 100
YRCQCHLRVV QCSDLGLDKV PWDFPPDTTL LDLQNNKITE IKEGAFKNLK
110 120 130 140 150
DLHTLILVNN KISKISPEAF KPLVKLERLY LSKNQLKELP EKMPRTLQEL
160 170 180 190 200
RVHENEITKL RKSDFNGLNN VLVIELGGNP LKNSGIENGA FQGLKSLSYI
210 220 230 240 250
RISDTNITAI PQGLPTSLTE VHLDGNKITK VDAPSLKGLI NLSKLGLSFN
260 270 280 290 300
SITVMENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYIQ VVYLHNNNIS
310 320 330 340 350
AVGQNDFCRA GHPSRKASYS AVSLYGNPVR YWEIFPNTFR CVYVRSAIQL

GNYK
Length:354
Mass (Da):39,809
Last modified:December 1, 1992 - v1
Checksum:iF05B5CC08DCABF6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53929 mRNA. Translation: CAA37876.1.
CCDSiCCDS24141.1.
PIRiA55454.
RefSeqiNP_001177380.1. NM_001190451.1.
NP_031859.1. NM_007833.5.
UniGeneiMm.56769.

Genome annotation databases

EnsembliENSMUST00000105287; ENSMUSP00000100924; ENSMUSG00000019929.
ENSMUST00000163448; ENSMUSP00000131431; ENSMUSG00000019929.
GeneIDi13179.
KEGGimmu:13179.
UCSCiuc007gwx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53929 mRNA. Translation: CAA37876.1.
CCDSiCCDS24141.1.
PIRiA55454.
RefSeqiNP_001177380.1. NM_001190451.1.
NP_031859.1. NM_007833.5.
UniGeneiMm.56769.

3D structure databases

ProteinModelPortaliP28654.
SMRiP28654. Positions 48-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28654. 1 interaction.
MINTiMINT-4107388.
STRINGi10090.ENSMUSP00000100924.

PTM databases

PhosphoSiteiP28654.

Proteomic databases

MaxQBiP28654.
PaxDbiP28654.
PRIDEiP28654.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000105287; ENSMUSP00000100924; ENSMUSG00000019929.
ENSMUST00000163448; ENSMUSP00000131431; ENSMUSG00000019929.
GeneIDi13179.
KEGGimmu:13179.
UCSCiuc007gwx.2. mouse.

Organism-specific databases

CTDi1634.
MGIiMGI:94872. Dcn.

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiP28654.
KOiK04660.
OMAiPLGPVCP.
OrthoDBiEOG76739V.
PhylomeDBiP28654.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_294584. CS/DS degradation.
REACT_314166. Chondroitin sulfate biosynthesis.
REACT_326072. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_343463. Dermatan sulfate biosynthesis.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiDcn. mouse.
NextBioi283292.
PROiP28654.
SOURCEiSearch...

Gene expression databases

BgeeiP28654.
CleanExiMM_DCN.
ExpressionAtlasiP28654. baseline and differential.
GenevisibleiP28654. MM.

Family and domain databases

InterProiIPR028549. Decorin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
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. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Naitoh Y., Suzuki S.
    Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
    Tissue: Fibroblast.
  2. "The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation."
    Scholzen T., Solursh M., Suzuki S., Reiter R., Morgan J.L., Buchberg A.M., Siracusa L.D., Iozzo R.V.
    J. Biol. Chem. 269:28270-28281(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPGS2_MOUSE
AccessioniPrimary (citable) accession number: P28654
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 22, 2015
This is version 127 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.