title: Expression profile and structural divergence of novel human annexin 31.
abstract: Systematic analysis of expressed sequence tags in dbEST yielded an expression profile of the ten known human annexins and led to the discovery of a novel subfamily expressed mainly in differentiating tissues. Full-length cDNAs encoded a 338-amino acid protein with less than 40% identity to other annexins, an atypical amino acid composition, and an insertion and deletion in internal repeat 3. The most striking feature was a complete ablation of all four type II calcium-binding sites in the conserved tetrad core. Annexin 31 thus constitutes a unique, natural probe for investigating the role of membrane binding in annexin function.
authors.affiliation: Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Oviedo, Spain.
authors.forename: R O
authors.initials: RO
authors.lastname: Morgan
authors.forename: M P
authors.initials: MP
authors.lastname: Fernandez
mesh_terms: D000595:Amino Acid Sequence; D017302:Annexins / Q000737:chemistry / Q000235:genetics*; D018076:DNA, Complementary; D006801:Humans; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
chemical_list: C114643:ANXA9 protein, human; D017302:Annexins; D018076:DNA, Complementary