Annexin A2

Annexin A2
PDB rendering based on 1w7b.
Available structures PDB 1W7B, 1XJL, 2HYU, 2HYV, 2HYW
Identifiers
Symbols	ANXA2; ANX2; ANX2L4; CAL1H; LIP2; LPC2; LPC2D; P36; PAP-IV
External IDs	OMIM: 151740 MGI: 88246 HomoloGene: 20857 GeneCards: ANXA2 Gene
Gene Ontology Molecular function • phospholipase inhibitor activity • calcium ion binding • protein binding • calcium-dependent phospholipid binding • phosphatidylinositol-4,5-bisphosphate binding • cytoskeletal protein binding • Rab GTPase binding Cellular component • extracellular region • basement membrane • soluble fraction • cytoplasm • early endosome • plasma membrane • extrinsic to plasma membrane • midbody • sarcolemma • melanosome • protein complex • perinuclear region of cytoplasm Biological process • skeletal system development • angiogenesis • body fluid secretion • collagen fibril organization • positive regulation of vesicle fusion • fibrinolysis • positive regulation of binding • cellular response to acid Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	302	12306
Ensembl	ENSG00000182718	ENSMUSG00000032231
UniProt	B3KRQ1	Q3UCD3
RefSeq (mRNA)	NM_001002857.1	NM_007585.3
RefSeq (protein)	NP_001002857.1	NP_031611.1
Location (UCSC)	Chr 15: 60.64 – 60.69 Mb	Chr 9: 69.3 – 69.34 Mb
PubMed search	[1]	[2]

Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.

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 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.

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.

Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.

Interactions

Annexin A2 has been shown to interact with Prohibitin, CEACAM1, S100A10 and PCNA.

See also

• Annexin

Further reading

• Kwon M, MacLeod TJ, Zhang Y, Waisman DM (2006). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors.". Front. Biosci. 10 (1-3): 300–25. doi:10.2741/1529. PMID 15574370. 
• Babiychuk EB, Draeger A (2006). "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?". Biochem. Soc. Trans. 34 (Pt 3): 374–6. doi:10.1042/BST0340374. PMID 16709165. 
• Bohn E, Gerke V, Kresse H, et al. (1992). "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase.". FEBS Lett. 296 (3): 237–40. doi:10.1016/0014-5793(92)80294-Q. PMID 1531641. 
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151. 
• Jindal HK, Chaney WG, Anderson CW, et al. (1991). "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha.". J. Biol. Chem. 266 (8): 5169–76. PMID 1825830. 
• Filipek A, Gerke V, Weber K, Kuźnicki J (1991). "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography.". Eur. J. Biochem. 195 (3): 795–800. doi:10.1111/j.1432-1033.1991.tb15768.x. PMID 1999197. 
• Becker T, Weber K, Johnsson N (1991). "Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11.". EMBO J. 9 (13): 4207–13. PMC 552202. PMID 2148288. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=552202. 
• Spano F, Raugei G, Palla E, et al. (1991). "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication.". Gene 95 (2): 243–51. doi:10.1016/0378-1119(90)90367-Z. PMID 2174397. 
• Johnsson N, Johnsson K, Weber K (1988). "A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins.". FEBS Lett. 236 (1): 201–4. doi:10.1016/0014-5793(88)80314-4. PMID 2456953. 
• Gould KL, Woodgett JR, Isacke CM, Hunter T (1987). "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo.". Mol. Cell. Biol. 6 (7): 2738–44. PMC 367834. PMID 2946940. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=367834. 
• Huebner K, Cannizzaro LA, Frey AZ, et al. (1988). "Chromosomal localization of the human genes for lipocortin I and lipocortin II.". Oncogene Res. 2 (4): 299–310. PMID 2969496. 
• Huang KS, Wallner BP, Mattaliano RJ, et al. (1986). "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase.". Cell 46 (2): 191–9. doi:10.1016/0092-8674(86)90736-1. PMID 3013422. 
• Buday L, Egan SE, Rodriguez Viciana P, et al. (1994). "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells.". J. Biol. Chem. 269 (12): 9019–23. PMID 7510700. 
• Chung CY, Erickson HP (1994). "Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.". J. Cell Biol. 126 (2): 539–48. doi:10.1083/jcb.126.2.539. PMC 2200039. PMID 7518469. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2200039. 
• Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789. 
• Richard I, Broux O, Chiannilkulchai N, et al. (1995). "Regional localization of human chromosome 15 loci.". Genomics 23 (3): 619–27. doi:10.1006/geno.1994.1550. PMID 7851890. 
• Takahashi S, Reddy SV, Chirgwin JM, et al. (1994). "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption.". J. Biol. Chem. 269 (46): 28696–701. PMID 7961821. 
• Hyatt SL, Liao L, Chapline C, Jaken S (1994). "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells.". Biochemistry 33 (5): 1223–8. doi:10.1021/bi00171a023. PMID 8110754. 
• Wright JF, Kurosky A, Wasi S (1994). "An endothelial cell-surface form of annexin II binds human cytomegalovirus.". Biochem. Biophys. Res. Commun. 198 (3): 983–9. doi:10.1006/bbrc.1994.1140. PMID 8117306. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 

External links

• MeSH Annexin+A2