Search by BoMiProt ID - Bomi215

Primary Information

BoMiProt ID Bomi215
Protein Name Annexin A2
Organism Bos taurus
Uniprot IDP04272
Milk FractionMFGM, Exosome
Ref Sequence ID NP_777141.1
Aminoacid Length 339
Molecular Weight 38612
FASTA Sequence Download
Gene Name ANXA2
Gene ID 282689
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Protein Function member of the annexin family of Ca2+ dependent phospholipid binding proteins; AnxA2 significantly increases the phosphorylation of PI3K; regulates autophagy or cell resistance through the Akt/mTOR signaling pathway. Annexin A2 is a calcium-, actin-, and lipid-binding protein implicated in exocytosis in different cell types, such as neuroendocrine cells. 
Biochemical Properties After phosphorylation AnxA2 can be cleaved by mild chymotrypsin into a 33 kD C terminal core domain and 3 kD N terminal domain of 30 amino acids; Asparaginyl endopeptidase can cleave an N terminal peptide of bovine AnxA2 at a position between Asn31 and Phe32;
Significance in milk AnxA2 might response to amino acids and hormones to activate the mTOR pathway leading to milk synthesis and proliferation of bovine mammary epithelial cells
PTMs N terminus of AnxA2 contains several major sites for PTMs , including the phosphorylation sites Ser11, Ser25 and Tyr23; human placenta annexin A2 contains potential N-linked glycosylation site at the 61th residue of its amino terminal region
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
SCOP Class : All alpha proteins
Fold : Annexin
Superfamily : Annexin
Family : Annexin
Domain Name : 4X9P A:22-339

CATH Matched CATH superfamily
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs regulate the localisation and function of the multifunctional protein Annexin A2; Phosphorylation of Ser25 increases the accessibility of the mRNA- and G-actin-binding sites of AnxA2; Ser25 phosphorylated AnxA2 has been implicated in exocytosis, macro-pinosome motility, recycling of lipid rafts and the recruitment of protein kinase C (PKC) to phosphoinositide-4,5-biphosphate-rich membrane domains;
Bibliography 1. Aukrust, I., Rosenberg, L. A., Ankerud, M. M., Bertelsen, V., Hollås, H., Saraste, J., … Vedeler, A. (2017). Post-translational modifications of Annexin A2 are linked to its association with perinuclear nonpolysomal mRNP complexes. FEBS Open Bio, 7(2), 160–173.
2. 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. 3.Gabel M, Chasserot-Golaz S. Annexin A2, an essential partner of the exocytotic process in chromaffin cells. J Neurochem. 2016 Jun;137(6):890-6. doi: 10.1111/jnc.13628. Epub 2016 May 25. PMID: 27037794.