Annexin A9: Difference between revisions
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{{Short description|Protein-coding gene in the species Homo sapiens}} |
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{{Infobox_gene}} |
{{Infobox_gene}} |
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'''Annexin A9''' is a [[protein]] that in humans is encoded by the ''ANXA9'' [[gene]].<ref name="pmid9742942">{{cite journal | vauthors = Morgan RO, Fernandez MP | title = Expression profile and structural divergence of novel human annexin 31 | journal = FEBS Letters | volume = 434 | issue = 3 | pages = 300–4 | date = Sep 1998 | pmid = 9742942 |
'''Annexin A9''' is a [[protein]] that in humans is encoded by the ''ANXA9'' [[gene]].<ref name="pmid9742942">{{cite journal | vauthors = Morgan RO, Fernandez MP | title = Expression profile and structural divergence of novel human annexin 31 | journal = FEBS Letters | volume = 434 | issue = 3 | pages = 300–4 | date = Sep 1998 | pmid = 9742942 | doi = 10.1016/S0014-5793(98)00997-1 | s2cid = 13751169 | doi-access = free }}</ref><ref name="pmid9931420">{{cite journal | vauthors = Morgan RO, Bell DW, Testa JR, Fernandez MP | title = Human annexin 31 genetic mapping and origin | journal = Gene | volume = 227 | issue = 1 | pages = 33–8 | date = Feb 1999 | pmid = 9931420 | doi = 10.1016/S0378-1119(98)00597-6 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ANXA9 annexin A9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8416}}</ref> |
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== Function == |
== Function == |
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The [[annexin]]s 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.<ref name="entrez" /> |
The [[annexin]]s 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.<ref name="entrez" /> |
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==Model organisms== |
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[[Model organism]]s have been used in the study of ANXA9 function. A conditional [[knockout mouse]] line called ''Anxa9<sup>tm1b(EUCOMM)Wtsi</sup>'' was generated at the [[Wellcome Trust Sanger Institute]].<ref name="mgp_reference">{{cite journal |title=The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice |author=Gerdin AK |year=2010 |journal=Acta Ophthalmologica|volume=88 |pages=925–7|doi=10.1111/j.1755-3768.2010.4142.x }}</ref> Male and female animals underwent a standardized [[phenotypic screen]]<ref name="IMPCsearch_ref">{{cite web |url=http://www.mousephenotype.org/data/search?q=Anxa9#fq=*:*&facet=gene |title=International Mouse Phenotyping Consortium}}</ref> to determine the effects of deletion.<ref name="pmid21677750">{{cite journal | vauthors = 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 | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref><ref name="pmid23870131">{{cite journal | vauthors = 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 | title = Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes | journal = Cell | volume = 154 | issue = 2 | pages = 452–64 | date = Jul 2013 | pmid = 23870131 | pmc = 3717207 | doi = 10.1016/j.cell.2013.06.022 }}</ref> Additional screens performed: - In-depth immunological phenotyping<ref name="iii_ref">{{cite web |url= http://www.immunophenotyping.org/data/search?keys=Anxa9&field_gene_construct_tid=All |title=Infection and Immunity Immunophenotyping (3i) Consortium}}</ref> - in-depth bone and cartilage phenotyping<ref name="obcd_ref">{{cite web |url=http://www.boneandcartilage.com/ |title=OBCD Consortium}}</ref> |
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{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: left;" | |
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|+ ''Anxa9'' knockout mouse phenotype |
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! Characteristic!! Phenotype |
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| colspan=2; style="text-align: center;" | All data available at.<ref name="IMPCsearch_ref"/><ref name="iii_ref" /><ref name="obcd_ref"/> |
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| Insulin || bgcolor="#488ED3"|Normal |
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| Homozygous viability at P14 || bgcolor="#488ED3"|Normal |
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| Homozygous Fertility || bgcolor="#488ED3"|Normal |
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| Body weight || bgcolor="#488ED3"|Normal |
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| Neurological assessment || bgcolor="#488ED3"|Normal |
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| Grip strength || bgcolor="#488ED3"|Normal |
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| [[Dysmorphology]] || bgcolor="#488ED3"|Normal |
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| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal |
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| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal |
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| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal |
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| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal |
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| [[Radiography]] || bgcolor="#488ED3"|Normal |
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| Eye morphology || bgcolor="#488ED3"|Normal |
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| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal |
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| ''[[Haematology]]'' 16 Weeks || bgcolor="#488ED3"|Normal |
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| Peripheral blood leukocytes 16 Weeks || bgcolor="#488ED3"|Normal |
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| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal |
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== References == |
== References == |
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== Further reading == |
== Further reading == |
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{{refbegin | 2}} |
{{refbegin | 2}} |
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* {{cite journal | vauthors = Benz J, Hofmann A | title = Annexins: from structure to function | journal = Biological Chemistry | volume = 378 | issue = |
* {{cite journal | vauthors = Benz J, Hofmann A | title = Annexins: from structure to function | journal = Biological Chemistry | volume = 378 | issue = 3–4 | pages = 177–83 | year = 1997 | pmid = 9165068 }} |
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* {{cite journal | vauthors = Nguyen VT, Ndoye A, Grando SA | title = Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine | journal = The Journal of Biological Chemistry | volume = 275 | issue = 38 | pages = 29466–76 | date = Sep 2000 | pmid = 10899159 | doi = 10.1074/jbc.M003174200 }} |
* {{cite journal | vauthors = Nguyen VT, Ndoye A, Grando SA | title = Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine | journal = The Journal of Biological Chemistry | volume = 275 | issue = 38 | pages = 29466–76 | date = Sep 2000 | pmid = 10899159 | doi = 10.1074/jbc.M003174200 | doi-access = free }} |
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* {{cite journal | vauthors = Goebeler V, Ruhe D, Gerke V, Rescher U | title = Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins | journal = FEBS Letters | volume = 546 | issue = |
* {{cite journal | vauthors = Goebeler V, Ruhe D, Gerke V, Rescher U | title = Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins | journal = FEBS Letters | volume = 546 | issue = 2–3 | pages = 359–64 | date = Jul 2003 | pmid = 12832069 | doi = 10.1016/S0014-5793(03)00634-3 | s2cid = 13433731 | doi-access = free }} |
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* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }} |
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 | bibcode = 2004PNAS..10112130B | doi-access = free }} |
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{{refend}} |
{{refend}} |
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Latest revision as of 15:13, 3 December 2023
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | ANXA9, ANX31, annexin A9 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 603319; MGI: 1923711; HomoloGene: 2643; GeneCards: ANXA9; OMA:ANXA9 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.[5][6][7]
Function
[edit]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]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000143412 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015702 – 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.
- ^ 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. S2CID 13751169.
- ^ 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.
- ^ a b "Entrez Gene: ANXA9 annexin A9".
External links
[edit]- Human ANXA9 genome location and ANXA9 gene details page in the UCSC Genome Browser.
Further reading
[edit]- 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. S2CID 13433731.
- 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. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.