Napsins: new human aspartic proteinases. Distinction between two closely related genes

FEBS Lett. 1998 Dec 11;441(1):43-8. doi: 10.1016/s0014-5793(98)01522-1.

Abstract

cDNA sequences were elucidated for two closely related human genes which encode the precursors of two hitherto unknown aspartic proteinases. The (pro)napsin A gene is expressed predominantly in lung and kidney and its translation product is predicted to be a fully functional, glycosylated aspartic proteinase (precursor) containing an RGD motif and an additional 18 residues at its C-terminus. The (pro)napsin B gene is transcribed exclusively in cells related to the immune system but lacks an in-frame stop codon and contains a number of polymorphisms, one of which replaces a catalytically crucial Gly residue with an Arg. Consideration is given to whether (pro)napsin B may be a transcribed pseudogene or whether its putative protein product undergoes rapid intracellular degradation.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartic Acid Endopeptidases / biosynthesis
  • Aspartic Acid Endopeptidases / chemistry
  • Aspartic Acid Endopeptidases / genetics*
  • Base Sequence
  • Cell Line
  • Enzyme Precursors / biosynthesis
  • Enzyme Precursors / chemistry
  • Enzyme Precursors / genetics*
  • Glycosylation
  • HeLa Cells
  • Humans
  • Kidney / enzymology
  • Lung / enzymology
  • Mice
  • Molecular Sequence Data
  • Neoplasms / enzymology
  • Neoplasms / genetics
  • Oligopeptides
  • Organ Specificity
  • Pepsinogen A / chemistry
  • Protein Biosynthesis
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Swine
  • Tumor Cells, Cultured

Substances

  • Enzyme Precursors
  • Oligopeptides
  • Recombinant Proteins
  • arginyl-glycyl-aspartic acid
  • Pepsinogen A
  • Aspartic Acid Endopeptidases

Associated data

  • GENBANK/AF090386
  • GENBANK/AF090387