Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2gene.[5]
Annexin 2 is involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane-associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel formation, and cell matrix interactions.
It is a calcium-dependent phospholipid-binding protein whose function is to help organize exocytosis of intracellular proteins to the extracellular domain. Annexin II is a pleiotropic protein meaning that its function is dependent on place and time in the body.
Gene
The ANXA2 gene, located at 15q22.2, has three pseudogenes located on chromosomes 4, 9 and 10, respectively. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[6]
Function
This protein is a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions as an autocrine factor which heightens osteoclast formation and bone resorption.[6] Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.[7] Maternal deficiency of the ANXA2 gene contributes to shallow decidual invasion by placental cytotrophoblast cells. These findings highlight the maternal contribution to the pathogenesis of severe preeclampsia.[8]
Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.
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^Réty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, et al. (January 1999). "The crystal structure of a complex of p11 with the annexin II N-terminal peptide". Nature Structural Biology. 6 (1): 89–95. doi:10.1038/4965. PMID9886297. S2CID26400923.
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Wright JF, Kurosky A, Wasi S (February 1994). "An endothelial cell-surface form of annexin II binds human cytomegalovirus". Biochemical and Biophysical Research Communications. 198 (3): 983–989. doi:10.1006/bbrc.1994.1140. PMID8117306.
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