Abstract

Annexin A2, a Ca2+-regulating and phospholipid-binding protein, distributing in most of cells which plays roles in the inflammatory regulation and pathogenic resistance. It performs membrane binding function in various physiological processes such as membrane repair, vesicular transportation and autophagy. In the present study, Annexin A2a and Annexin A2b gene were cloned from Ctenopharyngodon Idella (grass carp). The open reading frame (ORF) of Annexin A2a and Annexin A2b encoded 337 and 338 amino acid residues, respectively. The gene phylogenetic tree showed that Annexin A2a and Annexin A2b gene in grass carp had a great evolutionary conservation compared with their orthologues in danio rerio. The predicted 3D models presented that Annexin A2a equipped calcium ion binding sites, and its structure identity was 66.96% compared with human Annexin A2. However, Annexin A2b possessed no calcium ion binding sites, but it still had 64.79% identity compared with human Annexin A2.

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