Annexin A9

Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.[5][6][7]

ANXA9
Identifiers
Aliases	ANXA9, ANX31, annexin A9
External IDs	OMIM: 603319 MGI: 1923711 HomoloGene: 2643 GeneCards: ANXA9
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.3 Start 150,982,249 bp[1] End 150,995,634 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F2.1 Start 95,296,096 bp[2] End 95,307,176 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium-dependent phospholipid binding • calcium ion binding • acetylcholine receptor activity • phosphatidylserine binding • GO:0001948 protein binding • phospholipid binding • protein homodimerization activity Cellular component • cell surface • cytosol Biological process • signal transduction • cell-cell adhesion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8416	71790
Ensembl	ENSG00000143412	ENSMUSG00000015702
UniProt	O76027	Q9JHQ0
RefSeq (mRNA)	NM_003568	NM_001085383 NM_023628 NM_001379545 NM_001379546
RefSeq (protein)	NP_003559	NP_001078852 NP_076117 NP_001366474 NP_001366475
Location (UCSC)	Chr 1: 150.98 – 151 Mb	Chr 3: 95.3 – 95.31 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.[7]

Model organisms

Model organisms have been used in the study of ANXA9 function. A conditional knockout mouse line called Anxa9^{tm1b(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: - In-depth immunological phenotyping[14] - in-depth bone and cartilage phenotyping[15]

Anxa9 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[9][14][15]
Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Salmonella infection	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000143412 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000015702 - 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. Morgan RO, Fernandez MP (Sep 1998). "Expression profile and structural divergence of novel human annexin 31". FEBS Letters. 434 (3): 300–4. doi:10.1016/S0014-5793(98)00997-1. PMID 9742942.
6. Morgan RO, Bell DW, Testa JR, Fernandez MP (Feb 1999). "Human annexin 31 genetic mapping and origin". Gene. 227 (1): 33–8. doi:10.1016/S0378-1119(98)00597-6. PMID 9931420.
7. "Entrez Gene: ANXA9 annexin A9".
8. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
9. "International Mouse Phenotyping Consortium".
10. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
11. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
12. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
13. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
14. "Infection and Immunity Immunophenotyping (3i) Consortium".
15. "OBCD Consortium".

External links

• Human ANXA9 genome location and ANXA9 gene details page in the UCSC Genome Browser.

Further reading

• Benz J, Hofmann A (1997). "Annexins: from structure to function". Biological Chemistry. 378 (3–4): 177–83. PMID 9165068.
• Nguyen VT, Ndoye A, Grando SA (Sep 2000). "Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine". The Journal of Biological Chemistry. 275 (38): 29466–76. doi:10.1074/jbc.M003174200. PMID 10899159.
• Goebeler V, Ruhe D, Gerke V, Rescher U (Jul 2003). "Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins". FEBS Letters. 546 (2–3): 359–64. doi:10.1016/S0014-5793(03)00634-3. PMID 12832069.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.