Annexin A3

ANXA3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1AII, 1AXN
Identifiers
Aliases	ANXA3, ANX3, annexin A3
External IDs	OMIM: 106490 MGI: 1201378 HomoloGene: 68445 GeneCards: ANXA3
Gene location (Human)
Chr.	Chromosome 4 (human)[1]
End	78,610,451 bp[1]
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)[2]
End	96,845,966 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• phospholipase inhibitor activity; • calcium ion binding; • phospholipase A2 inhibitor activity; • calcium-dependent protein binding; • calcium-dependent phospholipid binding;
Cellular component	• cytoplasm; • phagocytic vesicle membrane; • membrane; • cell membrane; • axon; • neuronal cell body; • dendrite; • specific granule; • extracellular exosome; • cytosol;
Biological process	• GO:0048553 negative regulation of catalytic activity; • positive regulation of DNA metabolic process; • neutrophil degranulation; • positive regulation of sequence-specific DNA binding transcription factor activity; • response to glucocorticoid; • positive regulation of angiogenesis; • positive regulation of endothelial cell migration; • defense response to bacterium; • animal organ regeneration; • phagocytosis; • response to growth factor; • hippocampus development; • homophilic cell adhesion via plasma membrane adhesion molecules; • regulation of NMDA receptor activity;
	Sources:Amigo / QuickGO
Orthologs
	306
	11745
	ENSG00000138772
	ENSMUSG00000029484
	P12429
	O35639
	NM_005139
	NM_013470
	NP_005130
	NP_038498
	Wikidata
View/Edit Human	View/Edit Mouse

Annexin A3 is a protein that in humans is encoded by the ANXA3 gene.[5][6]

It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART.[7]

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.[6]

References

GRCh38: Ensembl release 89: ENSG00000138772 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000029484 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"Entrez Gene: ANXA3 annexin A3".
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. S2CID 206362532.

External links

Human ANXA3 genome location and ANXA3 gene details page in the UCSC Genome Browser.

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.
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. S2CID 195213008.
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.
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. S2CID 23783563.
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.
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. S2CID 26007149.
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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138772 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029484 - 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.

[pmid1830024-5] 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.

[entrez-6] "Entrez Gene: ANXA3 annexin A3".

[zhang-7] 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. S2CID 206362532.

Annexin A3

References

External links

Further reading