Annexin A6

Annexin A6 is a protein that in humans is encoded by the ANXA6 gene.[5]

ANXA6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesANXA6, ANX6, CBP68, annexin A6, CPB-II, p70, p68
External IDsOMIM: 114070 MGI: 88255 HomoloGene: 55558 GeneCards: ANXA6
Gene location (Human)
Chr.Chromosome 5 (human)[1]
Band5q33.1Start151,100,706 bp[1]
End151,157,785 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

309

11749

Ensembl

ENSG00000197043

ENSMUSG00000018340

UniProt

P08133

P14824

RefSeq (mRNA)

NM_001155
NM_001193544
NM_004033
NM_001363114

NM_001110211
NM_013472

RefSeq (protein)

NP_001146
NP_001180473
NP_001350043

NP_001103681
NP_038500

Location (UCSC)Chr 5: 151.1 – 151.16 MbChr 11: 54.98 – 55.03 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

Annexin VI belongs to a family of calcium-dependent membrane and phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane-related events along exocytotic and endocytotic pathways. The annexin VI gene is approximately 60 kbp long and contains 26 exons. It encodes a protein of about 68 kDa that consists of eight 68-amino acid repeats separated by linking sequences of variable lengths. It is highly similar to human annexins I and II sequences, each of which contain four such repeats. Exon 21 of annexin VI is alternatively spliced, giving rise to two isoforms that differ by a 6-amino acid insertion at the start of the seventh repeat. Annexin VI has been implicated in mediating the endosome aggregation and vesicle fusion in secreting epithelia during exocytosis.[6]

Model organisms

Model organisms have been used in the study of ANXA6 function. A conditional knockout mouse line, called Anxa6tm1a(EUCOMM)Wtsi[13][14] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[15][16][17]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[11][18] Twenty six tests were carried out on mutant mice and one significant abnormality was observed: female homozygous mutant animals had an increased susceptibility to Citrobacter infection.[11]

Interactions

ANXA6 has been shown to interact with RAS p21 protein activator 1.[19]

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gollark: That affects other people, so I think most libertarians would say something should be done about that.
gollark: I mean, there was this person who said that "any technology which takes away jobs from humans should be banned", and I don't see how you would reasonably end up thinking that.
gollark: I feel the same about some views. Some make some sense to me, some... don't really.
gollark: It is, admittedly, not particularly interactive.

References
  1. GRCh38: Ensembl release 89: ENSG00000197043 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000018340 - 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. Crompton MR, Owens RJ, Totty NF, Moss SE, Waterfield MD, Crumpton MJ (Jan 1988). "Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family". The EMBO Journal. 7 (1): 21–7. doi:10.1002/j.1460-2075.1988.tb02779.x. PMC 454210. PMID 3258820.
  6. "Entrez Gene: ANXA6 annexin A6".
  7. "Dysmorphology data for Anxa6". Wellcome Trust Sanger Institute.
  8. "Haematology data for Anxa6". Wellcome Trust Sanger Institute.
  9. "Salmonella infection data for Anxa6". Wellcome Trust Sanger Institute.
  10. "Citrobacter infection data for Anxa6". Wellcome Trust Sanger Institute.
  11. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  12. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  13. "International Knockout Mouse Consortium".
  14. "Mouse Genome Informatics".
  15. 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.
  16. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  17. 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.
  18. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  19. Chow A, Gawler D (Oct 1999). "Mapping the site of interaction between annexin VI and the p120GAP C2 domain". FEBS Letters. 460 (1): 166–72. doi:10.1016/S0014-5793(99)01336-8. PMID 10571081.

Further reading
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