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 https://www.uniprot.org/uniprot/F6QVC9.fasta
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. https://doi.org/10.1002/jcp.26123.
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. https://doi.org/10.1006/jmbi.2000.4423.
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 http://www.ncbi.nlm.nih.gov/pubmed/11058080.