Primary Information | |
|---|---|
| BoMiProt ID | Bomi215 |
| Protein Name | Annexin A2 |
| Organism | Bos taurus |
| Uniprot ID | P04272 |
| Milk Fraction | MFGM, 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, Phosphorylation | |
| SCOP | Class : All alpha proteins Fold : Annexin Superfamily : Annexin Family : Annexin Domain Name : 4X9P A:22-339 |
| CATH | Matched CATH superfamily 1.10.220.10 |
| 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; |
| PDB ID | 4X9P, |
| 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. https://doi.org/10.1002/2211-5463.12173. 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. https://doi.org/10.1002/jcp.26123. 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. |