Reviewed, UniProtKB/Swiss-Prot P21793 (PGS2_BOVIN)

Names and origin

Protein names

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

Gene names

Name:

DCN

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	360 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. Ref.9 Ref.10 Ref.11
Subcellular location	Secreted › extracellular space › extracellular matrix.
Post-translational modification	The attached glycosaminoglycan chain can be either chondroitin 4-sulfate, chondroitin 6-sulfate or dermatan sulfate, depending upon the tissue of origin.
Sequence similarities	Belongs to the small leucine-rich proteoglycan (SLRP) family. Class I subfamily. Contains 12 LRR (leucine-rich) repeats.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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_0000032703

Chain

31 – 360

330

Decorin

PRO_0000032704

Regions

Repeat

74 – 94

21

LRR-S 1

Repeat

95 – 118

24

LRR-T 1

Repeat

119 – 142

24

LRR-T 2

Repeat

143 – 163

21

LRR-S 2

Repeat

164 – 187

24

LRR-T 3

Repeat

188 – 213

26

LRR-T 4

Repeat

214 – 234

21

LRR-S 3

Repeat

235 – 258

24

LRR-T 5

Repeat

259 – 282

24

LRR-T 6

Repeat

283 – 305

23

LRR-S 4

Repeat

306 – 335

30

LRR-T 7

Repeat

336 – 360

25

LRR-T 8

Compositional bias

55 – 68

14

Cys-rich

Amino acid modifications

Glycosylation

34

1

O-linked (Xyl...) (glycosaminoglycan) Ref.7 Ref.8

Glycosylation

212

1

N-linked (GlcNAc...) Ref.12

Glycosylation

263

1

N-linked (GlcNAc...) Ref.12

Glycosylation

304

1

N-linked (GlcNAc...) Ref.12

Disulfide bond

55 ↔ 61

Ref.12

Disulfide bond

59 ↔ 68

Ref.12

Disulfide bond

314 ↔ 347

Ref.12

Experimental info

Sequence conflict

283

1

V → A in CAA68702. Ref.1

Sequence conflict

289

1

L → V in CAA68702. Ref.1

Sequence conflict

308 – 310

3

IGS → NRL in BAC56458. Ref.5

Secondary structure

1

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360

Helix Strand Turn

Details...

Beta strand

63 – 67

5

Beta strand

86 – 88

3

Turn

99 – 104

6

Beta strand

110 – 112

3

Turn

123 – 128

6

Beta strand

134 – 136

3

Beta strand

155 – 157

3

Helix

168 – 171

4

Beta strand

179 – 181

3

Helix

189 – 191

3

Turn

194 – 199

6

Beta strand

205 – 207

3

Beta strand

225 – 228

4

Turn

239 – 244

6

Beta strand

250 – 252

3

Turn

263 – 265

3

Helix

266 – 268

3

Beta strand

274 – 276

3

Turn

287 – 291

5

Beta strand

297 – 299

3

Beta strand

312 – 314

3

Beta strand

326 – 329

4

Beta strand

332 – 334

3

Helix

337 – 339

3

Helix

342 – 345

4

Turn

351 – 353

3

Sequences

	Sequence		Length	Mass (Da)
	P21793-1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: F7B5B61C2A67CB5E	FASTA	360	39,879
	10 20 30 40 50 60 MKATIIFLLV AQVSWAGPFQ QKGLFDFMLE DEASGIGPEE HFPEVPEIEP MGPVCPFRCQ 70 80 90 100 110 120 CHLRVVQCSD LGLEKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK 130 140 150 160 170 180 ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKSV FNGLNQMIVV 190 200 210 220 230 240 ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA 250 260 270 280 290 300 SLKGLNNLAK LGLSFNSISA VDNGSLANTP HLRELHLNNN KLVKVPGGLA DHKYIQVVYL 310 320 330 340 350 360 HNNNISAIGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RAAVQLGNYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of the cDNA for small proteoglycan II of bovine bone." Day A.A., McQuillan C.I., Termine J.D., Young M.R. Biochem. J. 248:801-805(1987) [PubMed: 3435485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence of the bovine decorin gene." Khatib H. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.
[5]	"Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray." Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K. Mol. Reprod. Dev. 65:9-18(2003) [PubMed: 12658628] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 AND 214-360.
[6]	"Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography." Choi H.U., Johnson T.L., Pal S., Tang L.H., Rosenberg L.C., Neame P.J. J. Biol. Chem. 264:2876-2884(1989) [PubMed: 2914936] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-54.
[7]	"The NH2-terminal amino acid sequence of bovine skin proteodermatan sulfate." Pearson C.H., Winterbottom N., Fackre D.S., Scott P.G., Carpenter M.R. J. Biol. Chem. 258:15101-15104(1983) [PubMed: 6654908] [Abstract] Cited for: GLYCOSYLATION AT SER-34.
[8]	"Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans." Chopra R.K., Pearson C.H., Pringle G.A., Fackre D.S., Scott P.G. Biochem. J. 232:277-279(1985) [PubMed: 3936484] [Abstract] Cited for: GLYCOSYLATION AT SER-34.
[9]	"Extracellular matrix 22-kDa protein interacts with decorin core protein and is expressed in cutaneous fibrosis." Okamoto O., Suzuki Y., Kimura S., Shinkai H. J. Biochem. 119:106-114(1996) [PubMed: 8907183] [Abstract] Cited for: INTERACTION WITH DPT.
[10]	"Dermatopontin interacts with transforming growth factor beta and enhances its biological activity." Okamoto O., Fujiwara S., Abe M., Sato Y. Biochem. J. 337:537-541(1999) [PubMed: 9895299] [Abstract] Cited for: INTERACTION WITH DPT.
[11]	"Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1." Reinboth B., Hanssen E., Cleary E.G., Gibson M.A. J. Biol. Chem. 277:3950-3957(2002) [PubMed: 11723132] [Abstract] Cited for: INTERACTION WITH MFAP2 AND ELN.
[12]	"Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan." Scott P.G., McEwan P.A., Dodd C.M., Bergmann E.M., Bishop P.N., Bella J. Proc. Natl. Acad. Sci. U.S.A. 101:15633-15638(2004) [PubMed: 15501918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 31-360, DISULFIDE BONDS, GLYCOSYLATION AT ASN-212; ASN-263 AND ASN-304.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00712 mRNA. Translation: CAA68702.1.
AY781101 mRNA. Translation: AAV37207.1.
BT021076 mRNA. Translation: AAX09093.1.
BC105175 mRNA. Translation: AAI05176.1.
AB098914 mRNA. Translation: BAC56404.1.
AB098955 mRNA. Translation: BAC56445.1.
AB098968 mRNA. Translation: BAC56458.1.
AB099051 mRNA. Translation: BAC56541.1.
AB099061 mRNA. Translation: BAC56551.1.

IPI

IPI00688608.

PIR

S06280.

RefSeq

NP_776331.2.

UniGene

Bt.23178

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XCD	X-ray	2.31	A	31-359	[»]
1XEC	X-ray	2.30	A/B	31-359	[»]
1XKU	X-ray	2.15	A	31-360	[»]

DisProt

DP00489.

ModBase

Search...

Protein-protein interaction databases

STRING

P21793.

Genome annotation databases

Ensembl

ENSBTAT00000004560; ENSBTAP00000004560; ENSBTAG00000003505; Bos taurus. [Genome view]
ENSBTAT00000004562; ENSBTAP00000004562; ENSBTAG00000003505; Bos taurus. [Genome view]

GeneID

280760.

KEGG

bta:280760.

Organism-specific databases

CTD

280760.

Phylogenomic databases

HOVERGEN

P21793.

OMA

GSNDFCP.

Family and domain databases

InterPro

IPR001611. Leu-rich_rpt.
IPR000372. Leu-rich_rpt_Cys-rich-dom_N.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]

Pfam

PF00560. LRR_1. 5 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]

PIRSF

PIRSF002490. SLRP_I. 1 hit.

SMART

SM00369. LRR_TYP. 2 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PGS2_BOVIN

Accession

Primary (citable) accession number: P21793
Secondary accession number(s): Q3MHN1 , Q5U7W0, Q861V7, Q862D9, Q862E8, Q862L4, Q862R5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	July 5, 2005
Last modified:	November 3, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)