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
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Amino Acid Sequence
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Animals
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Aspartic Acid Endopeptidases / biosynthesis
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Aspartic Acid Endopeptidases / chemistry
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Aspartic Acid Endopeptidases / genetics*
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Base Sequence
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Cell Line
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Enzyme Precursors / biosynthesis
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Enzyme Precursors / chemistry
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Enzyme Precursors / genetics*
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Glycosylation
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HeLa Cells
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Humans
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Kidney / enzymology
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Lung / enzymology
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Mice
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Molecular Sequence Data
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Neoplasms / enzymology
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Neoplasms / genetics
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Oligopeptides
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Organ Specificity
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Pepsinogen A / chemistry
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Protein Biosynthesis
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Alignment
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Sequence Homology, Amino Acid
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Sequence Homology, Nucleic Acid
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Swine
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Tumor Cells, Cultured
Substances
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Enzyme Precursors
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Oligopeptides
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Recombinant Proteins
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arginyl-glycyl-aspartic acid
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Pepsinogen A
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Aspartic Acid Endopeptidases
Associated data
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GENBANK/AF090386
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GENBANK/AF090387