ANXA6

Annexin A6

PDB rendering based on 1avc.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ANXA6 ; ANX6; CBP68
External IDs OMIM: 114070 MGI: 88255 HomoloGene: 55558 GeneCards: ANXA6 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 309 11749
Ensembl ENSG00000197043 ENSMUSG00000018340
UniProt P08133 P14824
RefSeq (mRNA) NM_001155 NM_001110211
RefSeq (protein) NP_001146 NP_001103681
Location (UCSC) Chr 5:
151.1 – 151.16 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]

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.[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 (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. 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. 1 2 3 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 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.
  12. ↑ Dolgin E (Jun 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 (Jan 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 Biology 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 Letters 460 (1): 166–72. doi:10.1016/S0014-5793(99)01336-8. PMID 10571081.

Further reading

  • Moss SE, Jacob SM, Davies AA, Crumpton MJ (Nov 1992). "A growth-dependent post-translational modification of annexin VI". Biochimica et Biophysica Acta 1160 (1): 120–6. doi:10.1016/0167-4838(92)90045-f. PMID 1420329. 
  • Barel M, Gauffre A, Lyamani F, Fiandino A, Hermann J, Frade R (Aug 1991). "Intracellular interaction of EBV/C3d receptor (CR2) with p68, a calcium-binding protein present in normal but not in transformed B lymphocytes". Journal of Immunology 147 (4): 1286–91. PMID 1831222. 
  • Yoshizaki H, Mizoguchi T, Arai K, Shiratsuchi M, Shidara Y, Maki M (Jan 1990). "Structure and properties of calphobindin II, an anticoagulant protein from human placenta". Journal of Biochemistry 107 (1): 43–50. PMID 2139657. 
  • Iwasaki A, Suda M, Watanabe M, Nakao H, Hattori Y, Nagoya T, Saino Y, Shidara Y, Maki M (Jul 1989). "Structure and expression of cDNA for calphobindin II, a human placental coagulation inhibitor". Journal of Biochemistry 106 (1): 43–9. PMID 2528541. 
  • Davies AA, Moss SE, Crompton MR, Jones TA, Spurr NK, Sheer D, Kozak C, Crumpton MJ (Jun 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". Human Genetics 82 (3): 234–8. doi:10.1007/BF00291161. PMID 2731935. 
  • Südhof TC, Slaughter CA, Leznicki I, Barjon P, Reynolds GA (Feb 1988). "Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins". Proceedings of the National Academy of Sciences of the United States of America 85 (3): 664–8. doi:10.1073/pnas.85.3.664. PMC 279615. PMID 2963335. 
  • Warrington JA, Bengtsson U (Nov 1994). "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 (Apr 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". Molecular Immunology 32 (6): 389–97. doi:10.1016/0161-5890(95)00005-Y. PMID 7753047. 
  • Smith PD, Davies A, Crumpton MJ, Moss SE (Mar 1994). "Structure of the human annexin VI gene". Proceedings of the National Academy of Sciences of the United States of America 91 (7): 2713–7. doi:10.1073/pnas.91.7.2713. PMC 43440. PMID 8146179. 
  • Benz J, Bergner A, Hofmann A, Demange P, Göttig P, Liemann S, Huber R, Voges D (Aug 1996). "The structure of recombinant human annexin VI in crystals and membrane-bound". Journal of Molecular Biology 260 (5): 638–43. doi:10.1006/jmbi.1996.0426. PMID 8709144. 
  • Davis AJ, Butt JT, Walker JH, Moss SE, Gawler DJ (Oct 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". The Journal of Biological Chemistry 271 (40): 24333–6. doi:10.1074/jbc.271.40.24333. PMID 8798684. 
  • Barwise JL, Walker JH (Jan 1996). "Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts". Journal of Cell Science 109 (1): 247–55. PMID 8834809. 
  • Kester HA, van der Leede BM, van der Saag PT, van der Burg B (Jun 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". The Journal of Biological Chemistry 272 (26): 16637–43. doi:10.1074/jbc.272.26.16637. PMID 9195978. 
  • Song G, Campos B, Wagoner LE, Dedman JR, Walsh RA (Mar 1998). "Altered cardiac annexin mRNA and protein levels in the left ventricle of patients with end-stage heart failure". Journal of Molecular and Cellular Cardiology 30 (3): 443–51. doi:10.1006/jmcc.1997.0608. PMID 9515022. 
  • Garbuglia M, Verzini M, Donato R (Sep 1998). "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 (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. 
  • Dieudonné SC, Kerr JM, Xu T, Sommer B, DeRubeis AR, Kuznetsov SA, Kim IS, Gehron Robey P, Young MF (Dec 1999). "Differential display of human marrow stromal cells reveals unique mRNA expression patterns in response to dexamethasone". Journal of Cellular Biochemistry 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 (Nov 2001). "Expression of early and late differentiation markers (proliferating cell nuclear antigen, syndecan-3, annexin VI, and alkaline phosphatase) by human osteoarthritic chondrocytes". The American Journal of Pathology 159 (5): 1777–83. doi:10.1016/S0002-9440(10)63024-6. PMC 1867060. PMID 11696438. 
  • Takagi H, Asano Y, Yamakawa N, Matsumoto I, Kimata K (Aug 2002). "Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains". Journal of Cell Science 115 (Pt 16): 3309–18. PMID 12140262. 
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