ISOLATION AND SEQUENCE-ANALYSIS OF A HUMAN CDNA CLONE (XPNPEPL) HOMOLOGOUS TO X-PROLYL AMINOPEPTIDASE (AMINOPEPTIDASE-P)

A novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exh ibiting 44% sequence identity and 62% sequence similarity to pig kidne y X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase chain reaction of phytohemaggluti nin-stimulated lymphocyte mRNA. Conserved sequences were found with th e prokaryotic X-prolyl aminopeptidase encoding gene (pepP). The human gene translation product exhibits a high sequence homology to the Schi zosaccharomyces pombe chromosome I hypothetical protein C22G7.01c and to the S. cerevisiae ORF y11029w. Northern blot analysis indicates an ubiquitous expression of the human XPNPEPL sequence.