P07585 (PGS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Decorin

Alternative name(s):
Bone proteoglycan II
PG-S2
PG40

Gene names

Name:	DCN
Synonyms:	SLRR1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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 component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Corneal dystrophy
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging 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_component	Golgi 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_function	extracellular 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Propeptide	17 – 30	14			PRO_0000032709
	Chain	31 – 359	329	Decorin		PRO_0000032710
Regions
	Repeat	73 – 93	21	LRR 1
	Repeat	94 – 117	24	LRR 2
	Repeat	118 – 141	24	LRR 3
	Repeat	142 – 162	21	LRR 4
	Repeat	163 – 186	24	LRR 5
	Repeat	187 – 212	26	LRR 6
	Repeat	213 – 233	21	LRR 7
	Repeat	234 – 257	24	LRR 8
	Repeat	258 – 281	24	LRR 9
	Repeat	282 – 304	23	LRR 10
	Repeat	305 – 334	30	LRR 11
	Repeat	335 – 359	25	LRR 12
	Compositional bias	54 – 67	14	Cys-rich
Amino acid modifications
	Glycosylation	34	1	O-linked (Xyl...) (glycosaminoglycan) Ref.1
	Glycosylation	211	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	262	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	303	1	N-linked (GlcNAc...) Potential
	Disulfide bond	54 ↔ 60		By similarity
	Disulfide bond	58 ↔ 67		By similarity
	Disulfide bond	313 ↔ 346		By similarity
Natural variations
	Alternative sequence	71 – 179	109	Missing in isoform B.		VSP_006172
	Alternative sequence	72 – 75	4	LDKV → CLPS in isoform E.		VSP_006175
	Alternative sequence	73 – 219	147	Missing in isoform C.		VSP_006173
	Alternative sequence	76 – 359	284	Missing in isoform E.		VSP_006176
	Alternative sequence	109 – 295	187	Missing in isoform D.		VSP_006174
	Natural variant	268	1	T → M. Ref.6 Corresponds to variant rs3138268 [ dbSNP | Ensembl ].		VAR_014351
	Natural variant	273	1	E → Q. Corresponds to variant rs1803344 [ dbSNP | Ensembl ].		VAR_011975
Experimental info
	Sequence conflict	37	1	G → A AA sequence Ref.9
	Sequence conflict	45	1	D → P AA sequence Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified April 1, 1988. Version 1. Checksum: FF511E871A1A52DD	FASTA	359	39,747
	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
	Isoform B [UniParc]. Checksum: 5AA599BE479F68D9	FASTA	250	27,353
	10 20 30 40 50 60 MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC 70 80 90 100 110 120 HLRVVQCSDL ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD 130 140 150 160 170 180 GNKISRVDAA SLKGLNNLAK LGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA 190 200 210 220 230 240 EHKYIQVVYL HNNNISVVGS SDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV 250 RSAIQLGNYK
	Isoform C [UniParc]. Checksum: 0BCF8BC8CBA92CA9	FASTA	212	23,278
	10 20 30 40 50 60 MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC 70 80 90 100 110 120 HLRVVQCSDL GLPPSLTELH LDGNKISRVD AASLKGLNNL AKLGLSFNSI SAVDNGSLAN 130 140 150 160 170 180 TPHLRELHLD NNKLTRVPGG LAEHKYIQVV YLHNNNISVV GSSDFCPPGH NTKKASYSGV 190 200 210 SLFSNPVQYW EIQPSTFRCV YVRSAIQLGN YK
	Isoform D [UniParc]. Checksum: 7EA011E351163971	FASTA	172	19,243
	10 20 30 40 50 60 MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC 70 80 90 100 110 120 HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHVV YLHNNNISVV 130 140 150 160 170 GSSDFCPPGH NTKKASYSGV SLFSNPVQYW EIQPSTFRCV YVRSAIQLGN YK
	Isoform E [UniParc]. Checksum: 781856DC9E377479	FASTA	75	8,266
	10 20 30 40 50 60 MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPSL GPVCPFRCQC 70 HLRVVQCSDL GCLPS

References

	« Hide 'large scale' referencesShow '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

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M14219 mRNA. Translation: AAB00774.1. L01131 , 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.
PIR	NBHUC8. A45016. B28457.
RefSeq	NP_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.
UniGene	Hs.156316.
3D structure databases
ProteinModelPortal	P07585.
SMR	P07585. Positions 51-355.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	108002. 14 interactions.
STRING	9606.ENSP00000052754.
PTM databases
PhosphoSite	P07585.
Polymorphism databases
DMDM	129951.
Proteomic databases
PaxDb	P07585.
PRIDE	P07585.
Protocols and materials databases
DNASU	1634.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000052754; 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]
GeneID	1634.
KEGG	hsa:1634.
UCSC	uc001tbo.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
CTD	1634.
GeneCards	GC12M091472.
HGNC	HGNC:2705. DCN.
HPA	CAB017118. HPA003315.
MIM	125255. gene. 610048. phenotype.
neXtProt	NX_P07585.
Orphanet	101068. Congenital stromal corneal dystrophy.
PharmGKB	PA27177.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000261690.
HOVERGEN	HBG016052.
InParanoid	P07585.
KO	K04660.
OMA	SNDFCPP.
OrthoDB	EOG76739V.
PhylomeDB	P07585.
TreeFam	TF334562.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P07585.
Bgee	P07585.
CleanEx	HS_DCN.
Genevestigator	P07585.
Family and domain databases
InterPro	IPR028549. Decorin. IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR000372. LRR-contain_N. IPR016352. SLRP_I_decor/aspor/byglycan. [Graphical view]
PANTHER	PTHR24369:SF40. PTHR24369:SF40. 1 hit.
Pfam	PF01462. LRRNT. 1 hit. [Graphical view]
PIRSF	PIRSF002490. SLRP_I. 1 hit.
SMART	SM00369. LRR_TYP. 1 hit. SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 8 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DCN. human.
GeneWiki	Decorin.
GenomeRNAi	1634.
NextBio	6702.
PMAP-CutDB	P07585.
PRO	P07585.
SOURCE	Search...

Entry information

Entry name

PGS2_HUMAN

Accession

Primary (citable) accession number: P07585
Secondary accession number(s): Q9P0Z0 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.