|Protein Name||Bone morphogenetic protein 3|
|Ref Sequence ID||NP_001179197.1|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Protein Function||multifunctional cytokines that elicit pleiotropic effects on biological processes such as cell proliferation, cell differentiation and tissue morphogenesis; can exert either mitogenic or anti-mitogenic activities; recognized roles in bone formation during mammalian development. The assembly of BMP-3 and 3b are important in various developmental processes and organogenesis.|
|Biochemical Properties||BMPs dimeric molecules are constituted by about 120 amino acids, including seven conserved cysteine residues, from which six are highly conserved, comprising a cysteine knot motif linked by three intramolecular disulfide bonds; BMP3 may form non-covalent dimers due to the lack of this cysteine|
|Significance in milk||BMP 4 potentiates growth factor-induced proliferation of mammary epithelial cells|
|PTMs||As found in human kidney, BMP 2 Glycosylated: high-mannose and complex N-linked oligosaccharides; contains five Glycosylated: potential N-linked glycosylation sites (Asn-Xaa-Ser/Thr) at the N135, N163, N164, N200 and N338 positions, four in the prosegment domain and one in the mature region|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
|Significance of PTMs||essential for protein and induces osteoblast differentiation|
|Additional Comments||Loss-of-function analysis demonstrates that coordinated activity of xBMP-3b and cerberus, a head inducer, are required for head formation in Xenopus embryos.|
|Bibliography||1. Liao, W. X. et al. (2003) ‘Effect of intracellular interactions on the processing and secretion of bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9. Implication of the aberrant ovarian phenotype of BMP-15 mutant sheep.’, The Journal of biological chemistry, 278(6), pp. 3713–9. doi: 10.1074/jbc.M210598200. |
2. Hang, Q. et al. (2014) ‘Asparagine-linked glycosylation of bone morphogenetic protein-2 is required for secretion and osteoblast differentiation’, Glycobiology, 24(3), pp. 292–304. doi: 10.1093/glycob/cwt110.
3. Heinecke, K. et al. (2009) ‘Receptor oligomerization and beyond: a case study in bone morphogenetic proteins’, BMC Biology, 7(1), p. 59. doi: 10.1186/1741-7007-7-59.
4. Montesano, R., Sarközi, R. and Schramek, H. (2008) ‘Bone morphogenetic protein-4 strongly potentiates growth factor-induced proliferation of mammary epithelial cells’, Biochemical and Biophysical Research Communications, 374(1), pp. 164–168. doi: 10.1016/j.bbrc.2008.07.007. 5.Hino J, Kangawa K, Matsuo H, Nohno T, Nishimatsu S. Bone morphogenetic protein-3 family members and their biological functions. Front Biosci. 2004 May 1;9:1520-9. doi: 10.2741/1355. PMID: 14977563.