Annexin A2

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ANXA2
Protein ANXA2 PDB 1w7b.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesANXA2, ANX2, ANX2L4, CAL1H, HEL-S-270, LIP2, LPC2, LPC2D, P36, PAP-IV, annexin A2
External IDsOMIM: 151740 MGI: 88246 HomoloGene: 20857 GeneCards: ANXA2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001002857
NM_001002858
NM_001136015
NM_004039

NM_007585

RefSeq (protein)

NP_001002857
NP_001002858
NP_001129487
NP_004030

NP_031611

Location (UCSC)Chr 15: 60.35 – 60.4 MbChr 9: 69.45 – 69.49 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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,[8] CEACAM1,[9] S100A10,[10][11] PCNA,[12] complement Factor H,[13] and a number of viral factors including the HPV16 minor capsid protein L2.[14][15]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000182718 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032231 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (Nov 1994). "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption". The Journal of Biological Chemistry. 269 (46): 28696–701. doi:10.1016/S0021-9258(19)61961-7. PMID 7961821.
  6. ^ a b "Entrez Gene: ANXA2 annexin A2".
  7. ^ Kling T, Ferrarese R, Ó hAilín D, Johansson P, Heiland DH, Dai F, Vasilikos I, Weyerbrock A, Jörnsten R, Carro MS, Nelander S (Sep 2016). "Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma". EBioMedicine. 12: 72–85. doi:10.1016/j.ebiom.2016.08.050. PMC 5078587. PMID 27667176.
  8. ^ Bacher S, Achatz G, Schmitz ML, Lamers MC (Dec 2002). "Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2". Biochimie. 84 (12): 1207–20. doi:10.1016/S0300-9084(02)00027-5. PMID 12628297.
  9. ^ Kirshner J, Schumann D, Shively JE (Dec 2003). "CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis". The Journal of Biological Chemistry. 278 (50): 50338–45. doi:10.1074/jbc.M309115200. PMID 14522961.
  10. ^ Réty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A (Jan 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. PMID 9886297. S2CID 26400923.
  11. ^ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (Jul 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". The Journal of Biological Chemistry. 283 (28): 19192–200. doi:10.1074/jbc.M800100200. PMC 2443646. PMID 18434302.
  12. ^ Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (Oct 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". The Journal of Biological Chemistry. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
  13. ^ Leffler J, Herbert AP, Norström E, Schmidt CQ, Barlow PN, Blom AM, Martin M (Feb 2010). "Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells". The Journal of Biological Chemistry. 285 (6): 3766–76. doi:10.1074/jbc.M109.045427. PMC 2823518. PMID 19951950.
  14. ^ Woodham AW, Da Silva DM, Skeate JG, Raff AB, Ambroso MR, Brand HE, Isas JM, Langen R, Kast WM (2012). "The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection". PLOS ONE. 7 (8): e43519. doi:10.1371/journal.pone.0043519. PMC 3425544. PMID 22927980.
  15. ^ Woodham AW, Raff AB, Raff LM, Da Silva DM, Yan L, Skeate JG, Wong MK, Lin YG, Kast WM (May 2014). "Inhibition of Langerhans cell maturation by human papillomavirus type 16: a novel role for the annexin A2 heterotetramer in immune suppression". Journal of Immunology. 192 (10): 4748–57. doi:10.4049/jimmunol.1303190. PMC 4019435. PMID 24719459.

Further reading

External links