Annexin A3

PDB rendering based on 1aii.

Available structures
PDB	1AII, 1AXN

Identifiers

Symbols

ANXA3; ANX3

External IDs

OMIM: 106490 MGI: 1201378 HomoloGene: 68445 GeneCards: ANXA3 Gene

EC number

3.1.4.43

Gene Ontology
Molecular function	• calcium ion binding • calcium-dependent phospholipid binding • phospholipase A2 inhibitor activity
Cellular component	• cytoplasm • plasma membrane • membrane • axon • dendrite • phagocytic vesicle membrane • specific granule • neuronal cell body
Biological process	• phagocytosis • positive regulation of endothelial cell migration • hippocampus development • organ regeneration • defense response to bacterium • neutrophil degranulation • positive regulation of angiogenesis • positive regulation of DNA metabolic process • positive regulation of sequence-specific DNA binding transcription factor activity • response to glucocorticoid stimulus • response to growth factor stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
79.47 – 79.53 Mb

Chr 5:
97.22 – 97.27 Mb

PubMed search

[1]

[2]

Annexin A3 is a protein that in humans is encoded by the ANXA3 gene.^[1]^[2]

It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART.^[3]

This gene encodes 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 in the inhibition of phospholipase A2 and cleavage of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. This protein may also play a role in anti-coagulation.^[2]

References

^ Tait JF, Frankenberry DA, Miao CH, Killary AM, Adler DA, Disteche CM (Aug 1991). "Chromosomal localization of the human annexin III (ANX3) gene". Genomics 10 (2): 441–8. doi:10.1016/0888-7543(91)90330-H. PMID 1830024.
^ ^a ^b "Entrez Gene: ANXA3 annexin A3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306.
^ Zhang Y, Zhang YL, Feng C, et al. (September 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics 8 (20): 4344–56. doi:10.1002/pmic.200800294. PMID 18792929.

Ernst JD, Hoye E, Blackwood RA, Jaye D (1990). "Purification and characterization of an abundant cytosolic protein from human neutrophils that promotes Ca2(+)-dependent aggregation of isolated specific granules.". J. Clin. Invest. 85 (4): 1065–71. doi:10.1172/JCI114537. PMC 296536. PMID 2138632. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296536.
Ross TS, Tait JF, Majerus PW (1990). "Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III.". Science 248 (4955): 605–7. doi:10.1126/science.2159184. PMID 2159184.
Pepinsky RB, Tizard R, Mattaliano RJ, et al. (1988). "Five distinct calcium and phospholipid binding proteins share homology with lipocortin I.". J. Biol. Chem. 263 (22): 10799–811. PMID 2968983.
Tait JF, Sakata M, McMullen BA, et al. (1989). "Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family.". Biochemistry 27 (17): 6268–76. doi:10.1021/bi00417a011. PMID 2975506.
Tait JF, Smith C, Xu L, Cookson BT (1994). "Structure and polymorphisms of the human annexin III (ANX3) gene.". Genomics 18 (1): 79–86. doi:10.1006/geno.1993.1428. PMID 8276419.
Sekar MC, Sambandam V, Grizzle WE, McDonald JM (1996). "Dissociation of cyclic inositol phosphohydrolase activity from annexin III.". J. Biol. Chem. 271 (14): 8295–9. doi:10.1074/jbc.271.14.8295. PMID 8626524.
Favier-Perron B, Lewit-Bentley A, Russo-Marie F (1996). "The high-resolution crystal structure of human annexin III shows subtle differences with annexin V.". Biochemistry 35 (6): 1740–4. doi:10.1021/bi952092o. PMID 8639653.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Cargill M, Altshuler D, Ireland J, et al. (1999). "Characterization of single-nucleotide polymorphisms in coding regions of human genes.". Nat. Genet. 22 (3): 231–8. doi:10.1038/10290. PMID 10391209.
Bödeker H, Keim V, Fiedler F, et al. (2000). "PAP I interacts with itself, PAP II, PAP III, and lithostathine/regIalpha.". Mol. Cell Biol. Res. Commun. 2 (3): 150–4. doi:10.1006/mcbr.1999.0166. PMID 10662590.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis.". Proteomics 5 (15): 3876–84. doi:10.1002/pmic.200401239. PMID 16130169.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
Park JE, Lee DH, Lee JA, et al. (2005). "Annexin A3 is a potential angiogenic mediator.". Biochem. Biophys. Res. Commun. 337 (4): 1283–7. doi:10.1016/j.bbrc.2005.10.004. PMID 16236264.

PDB gallery

1aii: ANNEXIN III

1axn: THE HIGH RESOLUTION STRUCTURE OF ANNEXIN III SHOWS DIFFERENCES WITH ANNEXIN V

Annexin A3

References

Further reading