Replication Protein A (RPA) is a single stranded DNA-binding protein involved in DNA metabolic activities such as replication, repair, and recombination. RPA-Interacting Protein $alpha$ ($RIP{alpha}$) was originally identified as a nuclear transporter of RPA in Xenopus. The human $RIP{alpha}$ gene encodes several splice isoforms, of which $hRIP{alpha}$ and $hRIP{eta}$ are the major translation products in vivo. However, limited information is available about the alternative splicing of $RIP{alpha}$ in eukaryotes, apart from that in humans. In this study, we examined the alternative splicing of RIP{alpha} in the Drosophila, Xenopus, and mouse system. We showed that the number of splice isoforms of RIP{alpha} was species-specific, and displayed a tendency to increase in higher eukaryotes. Moreover, a mouse ortholog of $hRIP{alpha}$, $mRIP{eta}2$, was not SUMOylated, in contrast to $hRIP{alpha}$. Based on these results, we suggest that the $RIP{alpha}$ gene gains more splice isoforms and additional modifications after molecular evolution.