Aquaporins (AQPs) are a group of proteins that evolved to mediate specific permeation of water and other small solutes, playing important roles in osmoregulation and nutrition, especially for aquatic animals. Genome-wide characterization of the AQP family in a typical mollusc, Pacific abalone, suggested that tandem duplication and retroduplication led to the dramatic expansion and diversification of AQP genes. Structural analysis indicated that tandem duplicated AQPs showed abnormal characteristics. The conserved amino acids in the key site of the Ar/R region were replaced by the others. These substitutions altered the pore diameter and properties of the inner surface and could accommodate the pass through of other molecules except water. Functional analysis indicated that abnormal Ar/R region of the tandemly adjacent members led to the different permeability, suggesting the neofunctionalization of tandemly duplicated genes. Mutation analysis indicated that at the key site of Ar/R region, just a single amino acid substitute could alter the permeability of HdAQPs, further explaining the mechanism of neofunctionalization between the tandem duplicated HdAQPs. Our observations provided strong evidence that duplication and subsequent neofunctionalization have led to structural and functional diversity of AQPs in Pacific abalone, providing insights into the evolution of AQPs in molluscs.
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