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    Cytogenet Cell Genet. 1997;78(3-4):275-80.

    Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P).

    Vanhoof G, Goossens F, Juliano MA, Juliano L, Hendriks D, Schatteman K, Lin AH, Scharpé S.

    Department of Clinical Biochemistry, University of Antwerp, Wilrijk, Belgium. gvhoof@uia.ua.ac.be

    A novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exhibiting 44% sequence identity and 62% sequence similarity to pig kidney X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase chain reaction of phytohemagglutinin-stimulated lymphocyte mRNA. Conserved sequences were found with the prokaryotic X-prolyl aminopeptidase encoding gene (pepP). The human gene translation product exhibits a high sequence homology to the Schizosaccharomyces 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.

    PMID: 9465902 [PubMed - indexed for MEDLINE]

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