Pathways & interactions
Annexin A10 (IPR008156)
Short name: ANX10
Overlapping homologous superfamilies
- Annexin (IPR001464)
- Annexin A10 (IPR008156)
The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [PMID: 1646719]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebrates are classified into families B (in invertebrates), C (in fungi and some groups of unicellular eukaryotes), D (in plants), and E (in protists) [PMID: 15059252]. Annexins are absent from yeasts and prokaryotes [PMID: 15059252].
Most eukaryotic species have 1-20 annexin (ANX) genes. All annexins share a core domain made up of four similar repeats, each approximately 70 amino acids long [PMID: 1646719]. Each individual annexin repeat (sometimes referred to as endonexin folds) is folded into five alpha-helices, and in turn are wound into a right-handed super-helix; they usually contain a characteristic 'type 2' motif for binding calcium ions with the sequence 'GxGT-[38 residues]-D/E'. Animal and fungal annexins also have variable amino-terminal domains. The core domains of most vertebrate annexins have been analysed by X-ray crystallography, revealing conservation of their secondary and tertiary structures despite only 45-55% amino-acid identity among individual members. The four repeats pack into a structure that resembles a flattened disc, with a slightly convex surface on which the Ca 2+ -binding loops are located and a concave surface at which the amino and carboxyl termini come into close apposition.
Annexins are traditionally thought of as calcium-dependent phospholipid-binding proteins, but recent work suggests a more complex set of functions. The famiy has been linked with inhibition of phospholipase activity, exocytosis and endoctyosis, signal transduction, organisation of the extracellular matrix, resistance to reactive oxygen species and DNA replication [PMID: 9797403].
Human annexin A10 (annexin 14) was first identified in silico by searches of dbEST with a number of divergent annexins [PMID: 10458909]. The analysis revealed single human and mouse ESTs corresponding to a novel and rarely expressed annexin in which three of the four tetrad core repeats lack the calcium-binding domain. It was proposed that this subtype, together with A5 annexin, gave rise to the Type VI octad through a process of gene duplication and fusion in early chordate evolution [PMID: 10458909].