Primary Information |
|---|
| BoMiProt ID | Bomi95 |
|---|
| Protein Name | Annexin OS |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | F6QVC9 |
|---|
| Milk Fraction | Whey |
|---|
| Aminoacid Length | 321 |
|---|
| Molecular Weight | 36075 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | ANXA5 |
|---|
| Protein Existence Status | Unreviewed: Experimental evidence at protein level
|
|---|
Secondary 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 |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| |
|---|
| 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. |
|---|
