Search by BoMiProt ID - Bomi95

Primary Information

BoMiProt ID Bomi95
Protein Name Annexin OS
Organism Bos taurus
Uniprot IdF6QVC9
Milk FractionWhey
Amino Acid Lenth 321
Molecular Weight 36075
Fasta Sequence
Gene Name ANXA5
Protein Existence Status Unreviewed: Experimental evidence at protein level

Secondry Information

Protein Function Similar to annexin A5; family of Ca2+/lipid-binding proteins; implicated in Ca2+- regulated exocytotic events, endocytosis and stabilization of specific domains of organelle membranes and the plasma membrane; has RNA-binding capacity; participate in cell proliferation, growth, movement, metabolism, apoptosis, and they also play important roles in cytoskeletal organization, exocytosis, endocytosis, invasion, and metastasis;
Biochemical Properties soluble, hydrophilic proteins that bind to negatively charged phospholipids in a Ca2 -dependent manner; highly α-helical and forms a compact, slightly curved disc that has a convex surface harboring the Ca2+- and membrane binding sites and a concave side that points away from the membrane and is thereby available for other types of interaction/regulation; Annexin complexes with EF hand-type Ca2 binding proteins
Significance in milk AnxA2 could be involved in milk synthesis and proliferation of bovine mammary epithelial cells
PTMs Phosphorylated; phosphorylation sites are unique NH2-terminal domains
Significance of PTMs After phosphorylation undergoes proteolytic cleavage which show an altered sensitivity toward Ca2+/phospholipid
Bibliography 1. Zhang, M., Chen, D., Zhen, Z., Ao, J., Yuan, X., & Gao, X. (2018). Annexin A2 positively regulates milk synthesis and proliferation of bovine mammary epithelial cells through the mTOR signaling pathway. Journal of Cellular Physiology, 233(3), 2464–2475.
2. Rosengarth, A., Gerke, V., & Luecke, H. (2001). X-ray structure of full-length annexin 1 and implications for membrane aggregation. Journal of Molecular Biology, 306(3), 489–498.
3. Rescher, U., Zobiack, N., & Gerke, V. (2000). Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells. Journal of Cell Science, 113 ( Pt 22), 3931–3938. Retrieved from