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Carbonic anhydrases (CAs) are a family of metalloenzymes that can catalyze the reversible interconversion of CO 2 /HCO 3  – , ubiquitously present in both prokaryotes and eukaryotes. In the present study, a CA II (designated as  HdhCA II ) was sequenced and characterized from the mantle tissue of the Pacific abalone. The complete sequence of  HdhCA II  was 1,169 bp, encoding a polypeptide of 349 amino acids with a NH 2 -terminal signal peptide and a CA architectural domain. The predicted protein shared 98.57% and 68.59% sequence identities with CA II of  Haliotis gigantea  and  Haliotis tuberculata , respectively. Two putative N-linked glycosylation motifs and two cysteine residues could potentially form intramolecular disulfide bond present in  HdhCA II . The phylogenetic analysis indicated that  HdhCA II  was placed in a gastropod clade and robustly clustered with CA II of  H. gigantea  and  H. tuberculata . The highest level of  HdhCA II  mRNA expression was detected in the shell forming mantle tissue. During ontogenesis, the mRNA of  HdhCA II  was detected in all stages, with larval shell formation stage showing the highest expression level. The  in situ  hybridization results detected the  HdhCA II  mRNA expression in the epithelial cells of the dorsal mantle pallial, an area known to express genes involved in the formation of a nacreous layer in the shell. This is the first report of  HdhCA II  in the Pacific abalone, and the results of this study indicate that this gene might play a role in the shell formation of abalone.

frontiers in molecular biosciences

Molecular Characterization of Carbonic Anhydrase II (CA II) and Its Potential Involvement in Regulating Shell Formation in the Pacific Abalone, Haliotis discus hannai