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
Amino Acid Lenth 360
Molecular Weight 39879
Fasta Sequence https://www.uniprot.org/uniprot/P21793.fasta
Gene Name DCN
Gene Id 280760
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function proteoglycan known to impact mammary cell proliferation in humans and rodents; regulate fibrillogenesis; positively or negatively affect cell proliferation
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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P21793|PGS2_BOVIN Decorin OS=Bos taurus OX=9913 GN=DCN PE=1 SV=2
MKATIIFLLVAQVSWAGPFQQKGLFDFMLEDEAS*34GIGPEEHFPEVPEIEPMGPVCPFRCQCHLRVVQCSD LGLEKVPKDLPPDTALLDLQNNKITEIKDGDFKNLKNLHTLILINNKISKISPGAFAPLVKLERLYLSKN QLKELPEKMPKTLQELRVHENEITKVRKSVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTN*212ITTIPQGLPPSLTELHLDGNKITKVDAASLKGLNNLAKLGLSFNSISAVDN*263GSLANTPHLRELHLNNNKLVKVPGGLADHKYIQVVYLHNNN*304ISAIGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRAAVQLGNYK
PDB ID 1XCD, 1XEC, 1XKU,
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: http://www.ncbi.nlm.nih.gov/pubmed/7591990 (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.