Search by BoMiProt ID - Bomi238


Primary Information

BoMiProt ID Bomi238
Protein Name Bone morphogenetic protein 3
Organism Bos taurus
Uniprot IdP22444
Milk FractionWhey
Ref Sequence Id NP_001179197.1
Aminoacid Length 475
Molecular Weight 53501
Fasta Sequence https://www.uniprot.org/uniprot/P22444.fasta
Gene Name BMP3
Gene Id 539527
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

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)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
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.