Evolutionary analysis of the mammalian M1 aminopeptidases reveals conserved exon structure and gene death

The members of the M1 aminopeptidase family share conserved domains, yet show functional divergence within the family as a whole. In order to better understand this family, this study analyzed the mammalian members in depth at exon, gene, and protein levels. The twelve human members, eleven rat members, and eleven mouse members were first analyzed in multiple alignments to visualize both reported and unreported conserved domains. Phylogenetic trees were then generated for humans, rats, mice, and all mammals to determine how closely related the homologs were and to gain insight to the divergence in the family members. This produced three groups with similarity within the family. Next, a synteny study was completed to determine the present locations of the genes and changes that had occurred. It became apparent that gene death likely resulted in the lack of one member in mouse and rat. Finally, an in-depth analysis of the exon structure revealed that nine members of the human family and eight in mouse, are highly conserved within the exon structure. Taken together, these results indicate that the M1 aminopeptidase family is a divergent family with three subgroups and that genetic evidence mirrors categorization of the family by enzymatic function. [Display omitted] •Phylogenetic analysis of M1 peptidases shows three groups.•Exon structure is conserved in nine human and eight mouse M1 aminopeptidases.•Aminopeptidase exon conservation mirrors function and phylogenetic analysis.•A chromosomal rearrangement in mouse and rat may have caused the absence of ERAP2.