The structures of the bovine and porcine proacrosin genes and their conservation among mammals.

Abstract

Sperm acrosin is a serine protease that is involved in the recognition, binding and penetration of the sperm of the zona pellucida of the ovum. The bovine and porcine genes were cloned and characterized. Alignment of the intron/exon structure of both genes with the previously characterized human, rat and mouse genes and with other serine protease genes reveals that the coded sequence of the mammalian proacrosin is distributed in 5 exons and the splice junction types are identical to the exons encoding the catalytic domain of other serine protease genes. A comparison of the bovine, porcine, human, guinea pig, rabbit, rat and mouse preproprotein sequences shows that the catalytic domain is highly conserved, while the sequence of the proline rich domain is very variable among the species, ranging from 28.9% to 68.8%.