PMID:3059494

Citation	Affholter, JA, Fried, VA and Roth, RA (1988) Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242:1415-8
Abstract	A proteinase with high affinity for insulin has been proposed to play a role in the cellular processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been isolated and sequenced. The deduced amino acid sequence of the enzyme contained the sequences of 13 peptides derived from the isolated protein. The cDNA could be transcribed in vitro to yield a synthetic RNA that in cell-free translations produced a protein that coelectrophoresed with the native proteinase and could be immunoprecipitated with monoclonal antibodies to this enzyme. The deduced sequence of this proteinase did not contain the consensus sequences for any of the known classes of proteinases (that is, metallo, cysteine, aspartic, or serine), but it did show homology to an Escherichia coli proteinase (called protease III), which also cleaves insulin and is present in the periplasmic space. Thus, these two proteins may be members of a family of proteases that are involved in intercellular peptide signaling.
Links	PubMed
Keywords	Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA/genetics; Endopeptidases/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Humans; Insulysin/genetics; Metalloendopeptidases; Molecular Sequence Data; Peptide Hydrolases/genetics; Sequence Homology, Nucleic Acid
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:IDE	involved_in	GO:0008286: insulin receptor signaling pathway	ECO:0000303: author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete

References

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