Annexin A2

Annexin A2also known asannexin IIis aproteinthat in humans is encoded by theANXA2gene.

ANXA2
Available structures PDB Ortholog search:PDBeRCSB List of PDB id codes 1W7B,1XJL,2HYU,2HYV,2HYW,4DRW,4FTG,4HRH
Identifiers
Aliases	ANXA2,ANX2, ANX2L4, CAL1H, HEL-S-270, LIP2, LPC2, LPC2D, P36, PAP-IV, annexin A2
External IDs	OMIM:151740;MGI:88246;HomoloGene:20857;GeneCards:ANXA2;OMA:ANXA2 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) Band 15q22.2 Start 60,347,134bp End 60,402,883bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 C|9 38.58 cM Start 69,360,902bp End 69,399,077bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in bronchial epithelial cell amniotic fluid nasal epithelium epithelium of nasopharynx synovial joint mucosa of pharynx visceral pleura parietal pleura oral cavity hair follicle Top expressed in corneal stroma endothelial cell of lymphatic vessel granulocyte gastrula calvaria skin of external ear dermis umbilical cord conjunctival fornix right lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phospholipase inhibitor activity calcium ion binding S100 protein binding phospholipase A2 inhibitor activity calcium-dependent protein binding protease binding cytoskeletal protein binding protein binding calcium-dependent phospholipid binding phosphatidylinositol-4,5-bisphosphate binding cadherin binding involved in cell-cell adhesion RNA binding identical protein binding bone sialoprotein binding molecular function regulator phosphatidylserine binding calcium channel activity virion binding voltage-gated calcium channel activity involved in regulation of cytosolic calcium levels Cellular component vesicle cytosol endosome membrane late endosome membrane melanosome ruffle plasma membrane lipid droplet myelin sheath adaxonal region Schmidt-Lanterman incisure PCSK9-AnxA2 complex macropinosome basement membrane cell surface lysosomal membrane basolateral plasma membrane cell cortex midbody early endosome perinuclear region of cytoplasm sarcolemma extrinsic component of plasma membrane extracellular exosome nucleus extracellular space azurophil granule lumen cytoplasm membrane raft extracellular matrix extracellular region protein-containing complex collagen-containing extracellular matrix Biological process negative regulation of low-density lipoprotein particle receptor catabolic process positive regulation of protein phosphorylation protein heterotetramerization fibrinolysis body fluid secretion collagen fibril organization positive regulation of fibroblast proliferation response to thyroid hormone positive regulation of binding positive regulation of vesicle fusion membrane raft assembly angiogenesis vesicle budding from membrane osteoclast development cell-cell adhesion negative regulation of catalytic activity positive regulation of receptor recycling neutrophil degranulation positive regulation of low-density lipoprotein particle clearance positive regulation of low-density lipoprotein particle receptor binding positive regulation of low-density lipoprotein receptor activity positive regulation of receptor-mediated endocytosis involved in cholesterol transport negative regulation of formation of structure involved in a symbiotic process positive regulation of vacuole organization interleukin-12-mediated signaling pathway protein localization to plasma membrane growth plate cartilage development regulation of plasminogen activation biomineral tissue development positive regulation of chondrocyte differentiation positive regulation by host of viral process regulation of cytosolic calcium ion concentration positive regulation of calcium ion transport endocardial cell differentiation calcium ion transmembrane transport positive regulation of viral life cycle Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 302 12306 Ensembl ENSG00000182718 ENSMUSG00000032231 UniProt P07355 P07356 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 Mb Chr 9: 69.36 – 69.4 Mb PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Annexin 2 is involved in diverse cellular processes such ascell motility(especially that of theepithelial cells), linkage of membrane-associated protein complexes to the actincytoskeleton,endocytosis,fibrinolysis,ion channelformation, andcell matrixinteractions. It is a calcium-dependent phospholipid-binding protein whose function is to help organizeexocytosisof intracellular proteins to the extracellular domain. Annexin II is apleiotropicprotein meaning that its function is dependent on place and time in the body.

Gene

TheANXA2gene, located at 15q22.2, has threepseudogeneslocated 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 theannexinfamily. 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.Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.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 severepreeclampsia.

Annexin A2 has been proposed to function inside the cell in sorting ofendosomesand outside the cell inanticoagulantreactions.

Interactions

Annexin A2 has been shown tointeractwithProhibitin,CEACAM1,S100A10,PCNA,complementFactor H,and a number of viral factors including theHPV16minorcapsid protein L2.

See also

• Annexin

Further reading

• Kwon M, MacLeod TJ, Zhang Y, Waisman DM (January 2005)."S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors".Frontiers in Bioscience.10(1–3): 300–325.doi:10.2741/1529.PMID15574370.
• Babiychuk EB, Draeger A (June 2006). "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?".Biochemical Society Transactions.34(Pt 3): 374–376.doi:10.1042/BST0340374.PMID16709165.
• Bohn E, Gerke V, Kresse H, Löffler BM, Kunze H (January 1992)."Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase".FEBS Letters.296(3): 237–240.doi:10.1016/0014-5793(92)80294-Q.PMID1531641.S2CID19633878.
• Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin".The Journal of Infection.24(3): 317–320.doi:10.1016/S0163-4453(05)80037-4.PMID1602151.
• Jindal HK, Chaney WG, Anderson CW, Davis RG, Vishwanatha JK (March 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".The Journal of Biological Chemistry.266(8): 5169–5176.doi:10.1016/S0021-9258(19)67770-7.PMID1825830.
• Filipek A, Gerke V, Weber K, Kuźnicki J (February 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".European Journal of Biochemistry.195(3): 795–800.doi:10.1111/j.1432-1033.1991.tb15768.x.PMID1999197.
• Becker T, Weber K, Johnsson N (December 1990)."Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11".The EMBO Journal.9(13): 4207–4213.doi:10.1002/j.1460-2075.1990.tb07868.x.PMC552202.PMID2148288.
• Spano F, Raugei G, Palla E, Colella C, Melli M (November 1990). "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): 243–251.doi:10.1016/0378-1119(90)90367-Z.PMID2174397.
• Johnsson N, Johnsson K, Weber K (August 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 Letters.236(1): 201–204.doi:10.1016/0014-5793(88)80314-4.PMID2456953.S2CID38734898.
• Gould KL, Woodgett JR, Isacke CM, Hunter T (July 1986)."The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo".Molecular and Cellular Biology.6(7): 2738–2744.doi:10.1128/mcb.6.7.2738.PMC367834.PMID2946940.
• Huebner K, Cannizzaro LA, Frey AZ, Hecht BK, Hecht F, Croce CM, Wallner BP (May 1988). "Chromosomal localization of the human genes for lipocortin I and lipocortin II".Oncogene Research.2(4): 299–310.PMID2969496.
• Huang KS, Wallner BP, Mattaliano RJ, Tizard R, Burne C, Frey A, et al. (July 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): 191–199.doi:10.1016/0092-8674(86)90736-1.PMID3013422.S2CID24557024.
• Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J (March 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".The Journal of Biological Chemistry.269(12): 9019–9023.doi:10.1016/S0021-9258(17)37070-9.PMID7510700.
• Chung CY, Erickson HP (July 1994)."Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C".The Journal of Cell Biology.126(2): 539–548.doi:10.1083/jcb.126.2.539.PMC2200039.PMID7518469.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, et al. (December 1994). "Construction of a human full-length cDNA bank".Gene.150(2): 243–250.doi:10.1016/0378-1119(94)90433-2.PMID7821789.
• Richard I, Broux O, Chiannilkulchai N, Fougerousse F, Allamand V, Bourg N, et al. (October 1994). "Regional localization of human chromosome 15 loci".Genomics.23(3): 619–627.doi:10.1006/geno.1994.1550.PMID7851890.
• Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (November 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): 28696–28701.doi:10.1016/S0021-9258(19)61961-7.PMID7961821.
• Hyatt SL, Liao L, Chapline C, Jaken S (February 1994). "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells".Biochemistry.33(5): 1223–1228.doi:10.1021/bi00171a023.PMID8110754.
• 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.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides".Gene.138(1–2): 171–174.doi:10.1016/0378-1119(94)90802-8.PMID8125298.

External links

• Annexin+A2at the U.S. National Library of MedicineMedical Subject Headings(MeSH)
• HumanANXA2genome location andANXA2gene details page in theUCSC Genome Browser.