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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Vanhoof, G. et al.

Vanhoof, Goossens, Juliano, Juliano, Hendriks, Schatteman, Lin, Scharpé,

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 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.[1]

References

Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P). Vanhoof, G., Goossens, F., Juliano, M.A., Juliano, L., Hendriks, D., Schatteman, K., Lin, A.H., Scharpé, S. Cytogenet. Cell Genet. (1997) [Pubmed]

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