Search by BoMiProt ID - Bomi313

Primary Information

BoMiProt ID Bomi313
Protein Name decorin
Organism Bos taurus
Uniprot IDP21793
Milk FractionExosome
Ref Sequence ID NP_776331.2
Aminoacid Length 360
Molecular Weight 39879
FASTA Sequence Download
Gene Name DCN
Gene ID 280760
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Protein Function proteoglycan known to impact mammary cell proliferation in humans and rodents; regulate fibrillogenesis; positively or negatively affect cell proliferation.  Decorin is a prototype member of the SLRP family found in a variety of tissues and is expressed in the stroma of various forms of cancer. Decorin has gained recognition for its essential roles in inflammation, fibrotic disorders, and cancer, and due to its antitumor properties, it has been proposed to act as a "guardian from the matrix."
Biochemical Properties C-terminal region of decorin is cysteine-rich, the central region is made of twelve leucine-rich repeats and is generally recognized as a ligand-binding domain (discussed in further detail below), and the N-terminal region contains the single a single chondroitin/dermatan sulfate side chain and a distinct pattern of cystine residues
Significance in milk ECM proteoglycan known to impact mammary cell proliferation in humans and rodents
PTMs covalent linkage of GAG chains; specifically, the addition of a single chondroitin or dermatan sulfate side chain on a serine residue on the N-terminal side of decorin. Disulfide bond formation.Glycosylation at Asn-212; Asn-263 and Asn-304.
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
>sp|P21793|PGS2_BOVIN Decorin OS=Bos taurus OX=9913 GN=DCN PE=1 SV=2
SCOP Class : Alpha and beta proteins (a/b)
Fold : Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily : L domain-like
Family : Ngr ectodomain-like
Domain Name : 1XKU A:22-326

CATH Matched CATH superfamily
Predicted Disorder Regions (37-50)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs The attached glycosaminoglycan chain can be either chondroitin 4-sulfate, chondroitin 6-sulfate or dermatan sulfate, depending upon the tissue of origin.
Bibliography 1. Schaefer, L. and Iozzo, R. V. (2008) ‘Biological Functions of the Small Leucine-rich Proteoglycans: From Genetics to Signal Transduction’, Journal of Biological Chemistry, 283(31), pp. 21305–21309. doi: 10.1074/jbc.R800020200.
2. Reed, C. C. and Iozzo, R. V. (2002) ‘The role of decorin in collagen fibrillogenesis and skin homeostasis’, Glycoconjugate Journal, 19(4/5), pp. 249–255. doi: 10.1023/A:1025383913444.
3. Scott, J. E. (1995) ‘Extracellular matrix, supramolecular organisation and shape.’, Journal of anatomy, 187 ( Pt 2), pp. 259–69. Available at: (Accessed: 4 October 2019).
4. Moses, J. et al. (1997) ‘Biosynthesis of the proteoglycan decorin -- identification of intermediates in galactosaminoglycan assembly.’, European journal of biochemistry, 248(3), pp. 767–74. doi: 10.1111/j.1432-1033.1997.t01-1-00767.x. 5.Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15633-8. doi: 10.1073/pnas.0402976101. Epub 2004 Oct 22. PMID: 15501918; PMCID: PMC524833. 6.Baghy K, Reszegi A, Tátrai P, Kovalszky I. Decorin in the Tumor Microenvironment. Adv Exp Med Biol. 2020;1272:17-38. doi: 10.1007/978-3-030-48457-6_2. PMID: 32845500.