ANXA6

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Annexin A6
PDB rendering based on 1avc.
Available structures: 1avc, 1m9i
Identifiers
Symbol(s) ANXA6; ANX6; CBP68
External IDs OMIM: 114070 MGI: 88255 HomoloGene: 55558
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 309 11749
Ensembl ENSG00000197043 ENSMUSG00000018340
Uniprot P08133 Q3TUI1
Refseq NM_001155 (mRNA)
NP_001146 (protein)		 NM_013472 (mRNA)
NP_038500 (protein)
Location Chr 5: 150.46 - 150.5 Mb Chr 11: 54.82 - 54.88 Mb
Pubmed search [1] [2]

Annexin A6, also known as ANXA6, is a human gene.

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.[1]

[edit] References

  1. ^ Entrez Gene: ANXA6 annexin A6.

[edit] 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. 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. 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. PMID 2963335. 
  • Crompton MR, Owens RJ, Totty NF, et al. (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. PMID 3258820. 
  • 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. 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. 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. 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 ( Pt 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. 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. 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. 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. 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. 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. 
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