Annexin A4

Annexin A4 is a protein that in humans is encoded by the ANXA4 gene.

ANXA4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ZOC
Identifiers
Aliases	ANXA4, ANX4, HEL-S-274, PIG28, ZAP36, P32.5, PAP-II, PP4-X, annexin A4
External IDs	OMIM: 106491; MGI: 88030; HomoloGene: 68164; GeneCards: ANXA4; OMA:ANXA4 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p13.3 Start 69,644,425 bp End 69,827,112 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 D1|6 37.75 cM Start 86,713,822 bp End 86,770,566 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pancreatic ductal cell gallbladder jejunal mucosa duodenum body of pancreas mucosa of ileum islet of Langerhans bronchial epithelial cell mucosa of colon mucosa of sigmoid colon Top expressed in Paneth cell jejunum crypt of lieberkuhn of small intestine gastric mucosa epithelium of stomach ileum pyloric antrum mucous cell of stomach migratory enteric neural crest cell epithelium of small intestine More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phospholipase inhibitor activity calcium ion binding calcium-dependent protein binding NF-kappaB binding protein binding identical protein binding calcium-dependent phospholipid binding heparin binding chondroitin sulfate binding Cellular component cytoplasm nuclear membrane vesicle membrane plasma membrane cell surface perinuclear region of cytoplasm extracellular exosome nucleus cytosol collagen-containing extracellular matrix Biological process Notch signaling pathway epithelial cell differentiation regulation of transcription by RNA polymerase II negative regulation of apoptotic process negative regulation of NF-kappaB transcription factor activity signal transduction negative regulation of catalytic activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 307 11746 Ensembl ENSG00000196975 ENSMUSG00000029994 UniProt P09525 P97429 RefSeq (mRNA) NM_001153 NM_001320698 NM_001320700 NM_001320702 NM_001365496 NM_013471 NM_001331120 RefSeq (protein) NP_001144 NP_001307627 NP_001307629 NP_001307631 NP_001352425 NP_001318049 NP_038499 Location (UCSC) Chr 2: 69.64 – 69.83 Mb Chr 6: 86.71 – 86.77 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

Annexin IV (ANX4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane-related events along exocytotic and endocytotic pathways. ANX4 has 45 to 59% identity with other members of its family and shares a similar size and exon-intron organization. Isolated from human placenta, ANX4 encodes a protein that has possible interactions with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANX4 is almost exclusively expressed in epithelial cells.

External links

• Human ANXA4 genome location and ANXA4 gene details page in the UCSC Genome Browser.

Further reading

• Römisch J, Heimburger N (May 1990). "Purification and characterization of six annexins from human placenta". Biological Chemistry Hoppe-Seyler. 371 (5): 383–8. doi:10.1515/bchm3.1990.371.1.383. PMID 2143074.
• Römisch J, Grote M, Weithmann KU, Heimburger N, Amann E (Nov 1990). "Annexin proteins PP4 and PP4-X. Comparative characterization of biological activities of placental and recombinant proteins". The Biochemical Journal. 272 (1): 223–9. doi:10.1042/bj2720223. PMC 1149680. PMID 2148260.
• Freemont PS, Driessen HP, Verbi W, Crumpton MJ (Nov 1990). "Crystallization and preliminary X-ray crystallographic studies of human placental annexin IV". Journal of Molecular Biology. 216 (2): 219–21. doi:10.1016/S0022-2836(05)80310-9. PMID 2254922.
• Hauptmann R, Maurer-Fogy I, Krystek E, Bodo G, Andree H, Reutelingsperger CP (Oct 1989). "Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding protein that inhibits coagulation and phospholipase A2 activity. Its molecular cloning, expression and comparison with VAC-alpha". European Journal of Biochemistry. 185 (1): 63–71. doi:10.1111/j.1432-1033.1989.tb15082.x. PMID 2530088.
• Grundmann U, Amann E, Abel KJ, Küpper HA (Apr 1988). "Isolation and expression of cDNA coding for a new member of the phospholipase A2 inhibitor family". Behring Institute Mitteilungen (82): 59–67. PMID 2970257.
• Ahn NG, Teller DC, Bienkowski MJ, McMullen BA, Lipkin EW, de Haën C (Dec 1988). "Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor". The Journal of Biological Chemistry. 263 (35): 18657–63. doi:10.1016/S0021-9258(18)37335-6. PMID 2974032.
• Tait JF, Sakata M, McMullen BA, Miao CH, Funakoshi T, Hendrickson LE, Fujikawa K (Aug 1988). "Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family". Biochemistry. 27 (17): 6268–76. doi:10.1021/bi00417a011. PMID 2975506.
• Sjölin C, Stendahl O, Dahlgren C (Jun 1994). "Calcium-induced translocation of annexins to subcellular organelles of human neutrophils". The Biochemical Journal. 300 ( Pt 2) (Pt 2): 325–30. doi:10.1042/bj3000325. PMC 1138165. PMID 8002935.
• Kojima K, Yamamoto K, Irimura T, Osawa T, Ogawa H, Matsumoto I (Mar 1996). "Characterization of carbohydrate-binding protein p33/41: relation with annexin IV, molecular basis of the doublet forms (p33 and p41), and modulation of the carbohydrate binding activity by phospholipids". The Journal of Biological Chemistry. 271 (13): 7679–85. doi:10.1074/jbc.271.13.7679. PMID 8631806.
• Davis AJ, Butt JT, Walker JH, Moss SE, Gawler DJ (Oct 1996). "The Ca2+-dependent lipid binding domain of P120GAP mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins. Evidence for a direct interaction between annexin VI and P120GAP". The Journal of Biological Chemistry. 271 (40): 24333–6. doi:10.1074/jbc.271.40.24333. PMID 8798684.
• Satoh A, Takayama E, Kojima K, Ogawa H, Yamori T, Sato S, Kawaguchi T, Tsuruo T, Katsura Y, Kina T, Matsumoto I (Feb 1996). "Expression of carbohydrate-binding protein p33/41 in human tumor cell lines". Journal of Biochemistry. 119 (2): 346–53. doi:10.1093/oxfordjournals.jbchem.a021246. PMID 8882729.
• Satoh A, Takayama E, Kojima K, Ogawa H, Katsura Y, Kina T, Matsumoto I (Mar 1997). "Characterization of human p33/41 (annexin IV), a Ca2+ dependent carbohydrate-binding protein with monoclonal anti-annexin IV antibodies, AS11 and AS17". Biological & Pharmaceutical Bulletin. 20 (3): 224–9. doi:10.1248/bpb.20.224. PMID 9084877.
• Dreier R, Schmid KW, Gerke V, Riehemann K (Aug 1998). "Differential expression of annexins I, II and IV in human tissues: an immunohistochemical study". Histochemistry and Cell Biology. 110 (2): 137–48. doi:10.1007/s004180050275. PMID 9720986. S2CID 19597353.
• Chow A, Davis AJ, Gawler DJ (Mar 2000). "Identification of a novel protein complex containing annexin VI, Fyn, Pyk2, and the p120(GAP) C2 domain". FEBS Letters. 469 (1): 88–92. doi:10.1016/S0014-5793(00)01252-7. PMID 10708762. S2CID 21394463.
• Han EK, Tahir SK, Cherian SP, Collins N, Ng SC (Jul 2000). "Modulation of paclitaxel resistance by annexin IV in human cancer cell lines". British Journal of Cancer. 83 (1): 83–8. doi:10.1054/bjoc.2000.1311. PMC 2374538. PMID 10883672.
• Radau B, Otto A, Müller EC, Westermann P (Jul 2000). "Protein kinase C alpha-dependent phosphorylation of Golgi proteins". Electrophoresis. 21 (13): 2684–7. doi:10.1002/1522-2683(20000701)21:13<2684::AID-ELPS2684>3.0.CO;2-G. PMID 10949146. S2CID 84800747.
• Gerner C, Frohwein U, Gotzmann J, Bayer E, Gelbmann D, Bursch W, Schulte-Hermann R (Dec 2000). "The Fas-induced apoptosis analyzed by high throughput proteome analysis". The Journal of Biological Chemistry. 275 (50): 39018–26. doi:10.1074/jbc.M006495200. PMID 10978337.
• Tsujii-Hayashi Y, Kitahara M, Yamagaki T, Kojima-Aikawa K, Matsumoto I (Dec 2002). "A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes". The Journal of Biological Chemistry. 277 (49): 47493–9. doi:10.1074/jbc.M206572200. PMID 12324456.