Abstract
Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans, SPP activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. We have identified human SPP as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. SPP and potential eukaryotic homologs may represent another family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Amyloid Precursor Protein Secretases
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Animals
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Aspartic Acid Endopeptidases / chemistry*
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Aspartic Acid Endopeptidases / genetics
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Aspartic Acid Endopeptidases / isolation & purification
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Aspartic Acid Endopeptidases / metabolism*
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Azirines / chemical synthesis
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Azirines / pharmacology
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Binding Sites
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Biotin / analogs & derivatives
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Biotin / chemical synthesis
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Biotin / pharmacology
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Cloning, Molecular
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Conserved Sequence
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Endopeptidases / metabolism
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Endoplasmic Reticulum / enzymology
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Glycosylation
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Humans
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Membrane Proteins / chemistry*
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Membrane Proteins / genetics
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Mutation
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Presenilin-1
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Presenilin-2
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Protease Inhibitors / chemical synthesis
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Protease Inhibitors / pharmacology
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Azirines
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Membrane Proteins
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PSEN1 protein, human
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PSEN2 protein, human
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Presenilin-1
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Presenilin-2
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Protease Inhibitors
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Recombinant Proteins
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TBL(4)K compound
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Biotin
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Amyloid Precursor Protein Secretases
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Endopeptidases
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Aspartic Acid Endopeptidases
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signal peptide peptidase
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BACE1 protein, human