Mouse Kallikrein Arginyl-esteropeptidase Genes: Analysis of Cloned cDNAs Suggests Rapid Functional Divergence from a Common Ancestral Sequence

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Abstract
A previously-cloned cDNA coding for a member of the kallikrein arginyl-esteropeptidase group of serine proteases, (pMK-1), was used as a hybridization probe to identify a second partial cDNA clone (pMK-2) from mouse submaxillary gland. pMK-2 shares more than a 98% nucleotide sequence homology with pMK-1; the 3′ untranslated regions are identical and there are only two predicted amino acid changes over the C-terminal 66 amino acids. The site of one change is implicated in determining substrate specificity, while the other may affect the catalytic mechanism. Thus despite the marked similarity of pMK-1 and pMK-2, the differences probably give rise to functionally distinct enzymes and are not simply polymorphic alleles.