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P28654

- PGS2_MOUSE

UniProt

P28654 - PGS2_MOUSE

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

Functioni

May affect the rate of fibrils formation.

GO - Molecular functioni

  1. extracellular matrix binding Source: MGI
  2. glycosaminoglycan binding Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. kidney development Source: Ensembl
  3. peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan Source: MGI
  4. placenta development Source: Ensembl
  5. response to lipopolysaccharide Source: Ensembl
  6. response to mechanical stimulus Source: Ensembl
  7. skeletal muscle tissue development Source: Ensembl
  8. wound healing Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_196514. Chondroitin sulfate biosynthesis.
REACT_196540. Dermatan sulfate biosynthesis.
REACT_196606. ECM proteoglycans.
REACT_198981. CS/DS degradation.
REACT_199052. Degradation of the extracellular matrix.

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: Chromosome 10

Organism-specific databases

MGIiMGI:94872. Dcn.

Subcellular locationi

GO - Cellular componenti

  1. collagen type VI trimer Source: Ensembl
  2. extracellular space Source: Ensembl
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 3014
PRO_0000032711Add
BLAST
Chaini31 – 354324Decorin
PRO_0000032712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341O-linked (Xyl...) (glycosaminoglycan) By similarity
Disulfide bondi49 ↔ 55 By similarity
Disulfide bondi53 ↔ 62 By similarity
Glycosylationi206 – 2061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi241 – 2411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi257 – 2571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi298 – 2981N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi308 ↔ 341 By 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

ArrayExpressiP28654.
BgeeiP28654.
CleanExiMM_DCN.
GenevestigatoriP28654.

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.

Protein-protein interaction databases

IntActiP28654. 1 interaction.
MINTiMINT-4107388.

Structurei

3D structure databases

ProteinModelPortaliP28654.
SMRiP28654. Positions 48-350.

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 6214Cys-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
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

MKATLIFFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP    50
YRCQCHLRVV QCSDLGLDKV PWDFPPDTTL LDLQNNKITE IKEGAFKNLK 100
DLHTLILVNN KISKISPEAF KPLVKLERLY LSKNQLKELP EKMPRTLQEL 150
RVHENEITKL RKSDFNGLNN VLVIELGGNP LKNSGIENGA FQGLKSLSYI 200
RISDTNITAI PQGLPTSLTE VHLDGNKITK VDAPSLKGLI NLSKLGLSFN 250
SITVMENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYIQ VVYLHNNNIS 300
AVGQNDFCRA GHPSRKASYS AVSLYGNPVR YWEIFPNTFR CVYVRSAIQL 350
GNYK 354
Length:354
Mass (Da):39,809
Last modified:December 1, 1992 - v1
Checksum:iF05B5CC08DCABF6F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X53929 mRNA. Translation: CAA37876.1 .
CCDSi CCDS24141.1.
PIRi A55454.
RefSeqi NP_001177380.1. NM_001190451.1.
NP_031859.1. NM_007833.5.
UniGenei Mm.56769.

3D structure databases

ProteinModelPortali P28654.
SMRi P28654. Positions 48-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P28654. 1 interaction.
MINTi MINT-4107388.

PTM databases

PhosphoSitei P28654.

Proteomic databases

MaxQBi P28654.
PaxDbi P28654.
PRIDEi P28654.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000105287 ; ENSMUSP00000100924 ; ENSMUSG00000019929 .
ENSMUST00000163448 ; ENSMUSP00000131431 ; ENSMUSG00000019929 .
GeneIDi 13179.
KEGGi mmu:13179.
UCSCi uc007gwx.2. mouse.

Organism-specific databases

CTDi 1634.
MGIi MGI:94872. Dcn.

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000261690.
HOVERGENi HBG016052.
InParanoidi P28654.
KOi K04660.
OMAi PLGPVCP.
OrthoDBi EOG76739V.
PhylomeDBi P28654.
TreeFami TF334562.

Enzyme and pathway databases

Reactomei REACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_196514. Chondroitin sulfate biosynthesis.
REACT_196540. Dermatan sulfate biosynthesis.
REACT_196606. ECM proteoglycans.
REACT_198981. CS/DS degradation.
REACT_199052. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSi DCN. mouse.
NextBioi 283292.
PROi P28654.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28654.
Bgeei P28654.
CleanExi MM_DCN.
Genevestigatori P28654.

Family and domain databases

InterProi IPR028549. Decorin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view ]
PANTHERi PTHR24369:SF5. PTHR24369:SF5. 1 hit.
Pfami PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view ]
PIRSFi PIRSF002490. SLRP_I. 1 hit.
SMARTi SM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 8 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 117 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

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