Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.[5][6][7]
Function
The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.[7]
References
External links
Further reading
- Benz J, Hofmann A (1997). "Annexins: from structure to function". Biological Chemistry. 378 (3–4): 177–83. PMID 9165068.
- Nguyen VT, Ndoye A, Grando SA (Sep 2000). "Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine". The Journal of Biological Chemistry. 275 (38): 29466–76. doi:10.1074/jbc.M003174200. PMID 10899159.
- Goebeler V, Ruhe D, Gerke V, Rescher U (Jul 2003). "Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins". FEBS Letters. 546 (2–3): 359–64. doi:10.1016/S0014-5793(03)00634-3. PMID 12832069. S2CID 13433731.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.