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P07585 (PGS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Decorin
Alternative name(s):
Bone proteoglycan II
PG-S2
PG40
Gene names
Name:DCN
Synonyms:SLRR1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May affect the rate of fibrils formation.

Subunit structure

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.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Post-translational modification

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

Involvement in disease

Corneal dystrophy, congenital stromal (CSCD) [MIM:610048]: A corneal dystrophy characterized by congenital corneal opacification consisting of a large number of flakes and spots throughout all layers of the stroma. It results in progressive, painless visual loss. Corneal erosions and photophobia are absent.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.

Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCorneal dystrophy
   DomainLeucine-rich repeat
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate biosynthetic process

Traceable author statement. Source: Reactome

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

dermatan sulfate biosynthetic process

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

kidney development

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Traceable author statement PubMed 7961765. Source: ProtInc

peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan

Inferred from electronic annotation. Source: Ensembl

placenta development

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

collagen type VI

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

lysosomal lumen

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P07585-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P07585-2)

The sequence of this isoform differs from the canonical sequence as follows:
     71-179: Missing.
Isoform C (identifier: P07585-3)

The sequence of this isoform differs from the canonical sequence as follows:
     73-219: Missing.
Isoform D (identifier: P07585-4)

The sequence of this isoform differs from the canonical sequence as follows:
     109-295: Missing.
Isoform E (identifier: P07585-5)

The sequence of this isoform differs from the canonical sequence as follows:
     72-75: LDKV → CLPS
     76-359: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 3014
PRO_0000032709
Chain31 – 359329Decorin
PRO_0000032710

Regions

Repeat73 – 9321LRR 1
Repeat94 – 11724LRR 2
Repeat118 – 14124LRR 3
Repeat142 – 16221LRR 4
Repeat163 – 18624LRR 5
Repeat187 – 21226LRR 6
Repeat213 – 23321LRR 7
Repeat234 – 25724LRR 8
Repeat258 – 28124LRR 9
Repeat282 – 30423LRR 10
Repeat305 – 33430LRR 11
Repeat335 – 35925LRR 12
Compositional bias54 – 6714Cys-rich

Amino acid modifications

Glycosylation341O-linked (Xyl...) (glycosaminoglycan) Ref.1
Glycosylation2111N-linked (GlcNAc...) Ref.11
Glycosylation2621N-linked (GlcNAc...) Ref.11
Glycosylation3031N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 60 By similarity
Disulfide bond58 ↔ 67 By similarity
Disulfide bond313 ↔ 346 By similarity

Natural variations

Alternative sequence71 – 179109Missing in isoform B.
VSP_006172
Alternative sequence72 – 754LDKV → CLPS in isoform E.
VSP_006175
Alternative sequence73 – 219147Missing in isoform C.
VSP_006173
Alternative sequence76 – 359284Missing in isoform E.
VSP_006176
Alternative sequence109 – 295187Missing in isoform D.
VSP_006174
Natural variant2681T → M. Ref.6
Corresponds to variant rs3138268 [ dbSNP | Ensembl ].
VAR_014351
Natural variant2731E → Q.
Corresponds to variant rs1803344 [ dbSNP | Ensembl ].
VAR_011975

Experimental info

Sequence conflict371G → A AA sequence Ref.9
Sequence conflict451D → P AA sequence Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: FF511E871A1A52DD

FASTA35939,747
        10         20         30         40         50         60 
MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC 

        70         80         90        100        110        120 
HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV 

       130        140        150        160        170        180 
SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE 

       190        200        210        220        230        240 
LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS 

       250        260        270        280        290        300 
LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH 

       310        320        330        340        350 
NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYK 

« Hide

Isoform B [UniParc].

Checksum: 5AA599BE479F68D9
Show »

FASTA25027,353
Isoform C [UniParc].

Checksum: 0BCF8BC8CBA92CA9
Show »

FASTA21223,278
Isoform D [UniParc].

Checksum: 7EA011E351163971
Show »

FASTA17219,243
Isoform E [UniParc].

Checksum: 781856DC9E377479
Show »

FASTA758,266

References

« Hide 'large scale' references
[1]"Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA."
Krusius T., Ruoslahti E.
Proc. Natl. Acad. Sci. U.S.A. 83:7683-7687(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human decorin gene: intron-exon junctions and chromosomal localization."
Vetter U., Vogel W., Just W., Young M.F., Fisher L.W.
Genomics 15:161-168(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[3]"The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5' untranslated region, and mapping of the gene to chromosome 12q23."
Danielson K.G., Fazzio A., Cohen I.R., Cannizzaro L., Iozzo R.V.
Genomics 15:146-160(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
[4]"Alternative splicing of human decorin."
Cs-Szabo G., Glant T.T.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[6]SeattleSNPs variation discovery resource
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-268.
[7]"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: Liver.
[8]"Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II."
Roughley P.J., White R.J.
Biochem. J. 262:823-827(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-50.
[9]"Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-49.
[10]"Congenital stromal dystrophy of the cornea caused by a mutation in the decorin gene."
Bredrup C., Knappskog P.M., Majewski J., Rodahl E., Boman H.
Invest. Ophthalmol. Vis. Sci. 46:420-426(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CONGENITAL STROMAL CORNEAL DYSTROPHY.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-211 AND ASN-262.
Tissue: Liver.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14219 mRNA. Translation: AAB00774.1.
L01131 expand/collapse EMBL AC list , L01125, L01126, L01127, L01129, L01130 Genomic DNA. Translation: AAA52301.1. Sequence problems.
AH005442 Genomic DNA. Translation: AAB60901.1.
AF138300 mRNA. Translation: AAD44713.1.
AF138301 mRNA. Translation: AAF61437.1.
AF138302 mRNA. Translation: AAD44714.1.
AF138303 mRNA. Translation: AAF61438.1.
AF138304 mRNA. Translation: AAD44715.1.
BT019800 mRNA. Translation: AAV38603.1.
AF491944 Genomic DNA. Translation: AAL92176.1.
BC005322 mRNA. Translation: AAH05322.1.
PIRNBHUC8. A45016.
B28457.
RefSeqNP_001911.1. NM_001920.3.
NP_598010.1. NM_133503.2.
NP_598011.1. NM_133504.2.
NP_598012.1. NM_133505.2.
NP_598013.1. NM_133506.2.
NP_598014.1. NM_133507.2.
XP_005268750.1. XM_005268693.1.
UniGeneHs.156316.

3D structure databases

ProteinModelPortalP07585.
SMRP07585. Positions 51-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108002. 14 interactions.
STRING9606.ENSP00000052754.

PTM databases

PhosphoSiteP07585.

Polymorphism databases

DMDM129951.

Proteomic databases

PaxDbP07585.
PRIDEP07585.

Protocols and materials databases

DNASU1634.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000052754; ENSP00000052754; ENSG00000011465. [P07585-1]
ENST00000228329; ENSP00000228329; ENSG00000011465. [P07585-2]
ENST00000303320; ENSP00000302031; ENSG00000011465. [P07585-4]
ENST00000393155; ENSP00000376862; ENSG00000011465. [P07585-1]
ENST00000420120; ENSP00000413723; ENSG00000011465. [P07585-2]
ENST00000425043; ENSP00000401021; ENSG00000011465. [P07585-3]
ENST00000441303; ENSP00000399815; ENSG00000011465. [P07585-4]
ENST00000456569; ENSP00000398514; ENSG00000011465. [P07585-5]
ENST00000547568; ENSP00000447674; ENSG00000011465. [P07585-3]
ENST00000552962; ENSP00000447654; ENSG00000011465. [P07585-1]
GeneID1634.
KEGGhsa:1634.
UCSCuc001tbo.3. human. [P07585-2]
uc001tbp.3. human. [P07585-3]
uc001tbq.3. human. [P07585-4]
uc001tbr.3. human. [P07585-5]
uc001tbt.3. human. [P07585-1]

Organism-specific databases

CTD1634.
GeneCardsGC12M091472.
HGNCHGNC:2705. DCN.
HPACAB017118.
HPA003315.
MIM125255. gene.
610048. phenotype.
neXtProtNX_P07585.
Orphanet101068. Congenital stromal corneal dystrophy.
PharmGKBPA27177.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000261690.
HOVERGENHBG016052.
InParanoidP07585.
KOK04660.
OMASNDFCPP.
OrthoDBEOG76739V.
PhylomeDBP07585.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP07585.
BgeeP07585.
CleanExHS_DCN.
GenevestigatorP07585.

Family and domain databases

InterProIPR028549. Decorin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERPTHR24369:SF40. PTHR24369:SF40. 1 hit.
PfamPF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFPIRSF002490. SLRP_I. 1 hit.
SMARTSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCN. human.
GeneWikiDecorin.
GenomeRNAi1634.
NextBio6702.
PMAP-CutDBP07585.
PROP07585.
SOURCESearch...

Entry information

Entry namePGS2_HUMAN
AccessionPrimary (citable) accession number: P07585
Secondary accession number(s): Q9P0Z0 expand/collapse secondary AC list , Q9P0Z1, Q9Y5N8, Q9Y5N9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM