ANXA6

Annexin A6

PDB rendering based on 1avc.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsANXA6 ; ANX6; CBP68
External IDsOMIM: 114070 MGI: 88255 HomoloGene: 55558 GeneCards: ANXA6 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez30911749
EnsemblENSG00000197043ENSMUSG00000018340
UniProtP08133P14824
RefSeq (mRNA)NM_001155NM_001110211
RefSeq (protein)NP_001146NP_001103681
Location (UCSC)Chr 5:
150.48 – 150.54 Mb		Chr 11:
54.98 – 55.03 Mb
PubMed search

Annexin A6 is a protein that in humans is encoded by the ANXA6 gene.[1]

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.[2]

Model organisms

Model organisms have been used in the study of ANXA6 function. A conditional knockout mouse line, called Anxa6tm1a(EUCOMM)Wtsi[9][10] 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.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] 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.[7]

Interactions

ANXA6 has been shown to interact with RAS p21 protein activator 1.[15]

References

  1. ↑ Crompton MR, Owens RJ, Totty NF, Moss SE, Waterfield MD, Crumpton MJ (May 1988). "Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family". EMBO J 7 (1): 21–7. PMC 454210. PMID 3258820.
  2. ↑ "Entrez Gene: ANXA6 annexin A6".
  3. ↑ "Dysmorphology data for Anxa6". Wellcome Trust Sanger Institute.
  4. ↑ "Haematology data for Anxa6". Wellcome Trust Sanger Institute.
  5. ↑ "Salmonella infection data for Anxa6". Wellcome Trust Sanger Institute.
  6. ↑ "Citrobacter infection data for Anxa6". Wellcome Trust Sanger Institute.
  7. ↑ 7.0 7.1 7.2 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.
  8. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. ↑ "International Knockout Mouse Consortium".
  10. ↑ "Mouse Genome Informatics".
  11. ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  12. ↑ Dolgin E (June 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  13. ↑ Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  14. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  15. ↑ Chow, A; Gawler D (Oct 1999). "Mapping the site of interaction between annexin VI and the p120GAP C2 domain". FEBS Lett. (NETHERLANDS) 460 (1): 166–72. doi:10.1016/S0014-5793(99)01336-8. ISSN 0014-5793. PMID 10571081.

Further reading

  • Moss SE, Jacob SM, Davies AA, Crumpton MJ (1992). "A growth-dependent post-translational modification of annexin VI.". Biochim. Biophys. Acta 1160 (1): 120–6. doi:10.1016/0167-4838(92)90045-f. PMID 1420329.
  • Barel M, Gauffre A, Lyamani F et al. (1991). "Intracellular interaction of EBV/C3d receptor (CR2) with p68, a calcium-binding protein present in normal but not in transformed B lymphocytes.". J. Immunol. 147 (4): 1286–91. PMID 1831222.
  • Yoshizaki H, Mizoguchi T, Arai K et al. (1990). "Structure and properties of calphobindin II, an anticoagulant protein from human placenta.". J. Biochem. 107 (1): 43–50. PMID 2139657.
  • Iwasaki A, Suda M, Watanabe M et al. (1989). "Structure and expression of cDNA for calphobindin II, a human placental coagulation inhibitor.". J. Biochem. 106 (1): 43–9. PMID 2528541.
  • Davies AA, Moss SE, Crompton MR et al. (1989). "The gene coding for the p68 calcium-binding protein is localised to bands q32-q34 of human chromosome 5, and to mouse chromosome 11.". Hum. Genet. 82 (3): 234–8. doi:10.1007/BF00291161. PMID 2731935.
  • Südhof TC, Slaughter CA, Leznicki I et al. (1988). "Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins.". Proc. Natl. Acad. Sci. U.S.A. 85 (3): 664–8. doi:10.1073/pnas.85.3.664. PMC 279615. PMID 2963335.
  • Warrington JA, Bengtsson U (1995). "High-resolution physical mapping of human 5q31-q33 using three methods: radiation hybrid mapping, interphase fluorescence in situ hybridization, and pulsed-field gel electrophoresis.". Genomics 24 (2): 395–8. doi:10.1006/geno.1994.1636. PMID 7698768.
  • Barel M, Balbo M, Gauffre A, Frade R (1995). "Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein.". Mol. Immunol. 32 (6): 389–97. doi:10.1016/0161-5890(95)00005-Y. PMID 7753047.
  • Smith PD, Davies A, Crumpton MJ, Moss SE (1994). "Structure of the human annexin VI gene.". Proc. Natl. Acad. Sci. U.S.A. 91 (7): 2713–7. doi:10.1073/pnas.91.7.2713. PMC 43440. PMID 8146179.
  • Benz J, Bergner A, Hofmann A et al. (1996). "The structure of recombinant human annexin VI in crystals and membrane-bound.". J. Mol. Biol. 260 (5): 638–43. doi:10.1006/jmbi.1996.0426. PMID 8709144.
  • Davis AJ, Butt JT, Walker JH et al. (1996). "The Ca2+-dependent lipid binding domain of P120GAP mediates protein-protein interactions with Ca2+-dependent membrane-binding proteins. Evidence for a direct interaction between annexin VI and P120GAP.". J. Biol. Chem. 271 (40): 24333–6. doi:10.1074/jbc.271.40.24333. PMID 8798684.
  • Barwise JL, Walker JH (1996). "Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts.". J. Cell. Sci. 109 (1): 247–55. PMID 8834809.
  • Kester HA, van der Leede BM, van der Saag PT, van der Burg B (1997). "Novel progesterone target genes identified by an improved differential display technique suggest that progestin-induced growth inhibition of breast cancer cells coincides with enhancement of differentiation.". J. Biol. Chem. 272 (26): 16637–43. doi:10.1074/jbc.272.26.16637. PMID 9195978.
  • Song G, Campos B, Wagoner LE et al. (1998). "Altered cardiac annexin mRNA and protein levels in the left ventricle of patients with end-stage heart failure.". J. Mol. Cell. Cardiol. 30 (3): 443–51. doi:10.1006/jmcc.1997.0608. PMID 9515022.
  • Garbuglia M, Verzini M, Donato R (1999). "Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments.". Cell Calcium 24 (3): 177–91. doi:10.1016/S0143-4160(98)90127-0. PMID 9883272.
  • Chow A, Gawler D (1999). "Mapping the site of interaction between annexin VI and the p120GAP C2 domain.". FEBS Lett. 460 (1): 166–72. doi:10.1016/S0014-5793(99)01336-8. PMID 10571081.
  • Dieudonné SC, Kerr JM, Xu T et al. (2000). "Differential display of human marrow stromal cells reveals unique mRNA expression patterns in response to dexamethasone.". J. Cell. Biochem. 76 (2): 231–43. doi:10.1002/(SICI)1097-4644(20000201)76:2<231::AID-JCB7>3.0.CO;2-X. PMID 10618640.
  • Pfander D, Swoboda B, Kirsch T (2001). "Expression of early and late differentiation markers (proliferating cell nuclear antigen, syndecan-3, annexin VI, and alkaline phosphatase) by human osteoarthritic chondrocytes.". Am. J. Pathol. 159 (5): 1777–83. doi:10.1016/S0002-9440(10)63024-6. PMC 1867060. PMID 11696438.
  • Takagi H, Asano Y, Yamakawa N et al. (2003). "Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains.". J. Cell. Sci. 115 (Pt 16): 3309–18. PMID 12140262.