Annexin A6

ANXA6
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1M9I
Identifiers
Aliases	ANXA6, ANX6, CBP68, annexin A6, CPB-II, p70, p68
External IDs	OMIM: 114070 MGI: 88255 HomoloGene: 55558 GeneCards: ANXA6
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	151,157,785 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	55,033,445 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding; • protein homodimerization activity; • GTP binding; • calcium-dependent protein binding; • cholesterol binding; • GO:0001948 protein binding; • ligand-gated ion channel activity; • calcium-dependent phospholipid binding; • lipid binding; • phosphatidylserine binding; • calcium channel activity; • heparin binding; • enzyme binding; • chondroitin sulfate binding; • signaling receptor activity; • GO:0032403 macromolecular complex binding; • actin filament binding;
Cellular component	• cytoplasm; • membrane; • late endosome membrane; • focal adhesion; • melanosome; • lysosomal membrane; • mitochondrion; • perinuclear region of cytoplasm; • extracellular exosome; • collagen-containing extracellular matrix;
Biological process	• regulation of muscle contraction; • mitochondrial calcium ion homeostasis; • ion transmembrane transport; • apoptotic signaling pathway; • protein homooligomerization; • calcium ion transport; • neural crest cell migration; • plasma membrane repair; • growth plate cartilage chondrocyte differentiation; • biomineral tissue development; • negative regulation of sequestering of calcium ion; • calcium ion import; • calcium ion transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	309
	11749
	ENSG00000197043
	ENSMUSG00000018340
	P08133
	P14824
	NM_001155; NM_001193544; NM_004033; NM_001363114
	NM_001110211; NM_013472
	NP_001146; NP_001180473; NP_001350043
	NP_001103681; NP_038500
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

*Anxa6* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal[7]
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal[8]
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[9]
Citrobacter infection	Abnormal[10]
All tests and analysis from[11][12]

Model organisms have been used in the study of ANXA6 function. A conditional knockout mouse line, called Anxa6^{tm1a(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]

References

GRCh38: Ensembl release 89: ENSG00000197043 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000018340 - 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.
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.
"Entrez Gene: ANXA6 annexin A6".
"Dysmorphology data for Anxa6". Wellcome Trust Sanger Institute.
"Haematology data for Anxa6". Wellcome Trust Sanger Institute.
"Salmonella infection data for Anxa6". Wellcome Trust Sanger Institute.
"Citrobacter infection data for Anxa6". Wellcome Trust Sanger Institute.
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. S2CID 85911512.
Mouse Resources Portal, Wellcome Trust Sanger Institute.
"International Knockout Mouse Consortium".
"Mouse Genome Informatics".
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. S2CID 18872015.
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.
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. S2CID 42114086.

External links

Human ANXA6 genome location and ANXA6 gene details page in the UCSC Genome Browser.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000197043 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid3258820-5] 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.

[entrez-6] "Entrez Gene: ANXA6 annexin A6".

[Dysmorphology-7] "Dysmorphology data for Anxa6". Wellcome Trust Sanger Institute.

[Haematology-8] "Haematology data for Anxa6". Wellcome Trust Sanger Institute.

[''Salmonella''_infection-9] "Salmonella infection data for Anxa6". Wellcome Trust Sanger Institute.

[''Citrobacter''_infection-10] "Citrobacter infection data for Anxa6". Wellcome Trust Sanger Institute.

[mgp_reference-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. S2CID 85911512.

[12] Mouse Resources Portal, Wellcome Trust Sanger Institute.

[allele_ref-13] "International Knockout Mouse Consortium".

[mgi_allele_ref-14] "Mouse Genome Informatics".

[pmid21677750-15] 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.

[mouse_library-16] Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-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. S2CID 18872015.

[pmid21722353-18] 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.

[pmid10571081-19] 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. S2CID 42114086.