ANXA9
Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.[4][5][6]
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.[6]
Model organisms
Model organisms have been used in the study of ANXA9 function. A conditional knockout mouse line called Anxa9tm1b(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[7] Male and female animals underwent a standardized phenotypic screen[8] to determine the effects of deletion.[9][10][11][12] Additional screens performed: - In-depth immunological phenotyping[13] - in-depth bone and cartilage phenotyping[14]
References
- ↑ "Diseases that are genetically associated with ANXA9 view/edit references on wikidata".
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ 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.
- ↑ 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.
- 1 2 "Entrez Gene: ANXA9 annexin A9".
- ↑ 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.
- 1 2 "International Mouse Phenotyping Consortium".
- ↑ 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. - ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ 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.
- ↑ 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.
- 1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".
- 1 2 "OBCD Consortium".
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.
