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FLASH GENE
Symbol IDE contributors: mct/npt - updated : 12-10-2016
HGNC name insulin-degrading enzyme
HGNC id 5381
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • an N terminal catalytic domain
  • a C terminus facilitating substrate recognition as well as playing a key role in the oligomerization of IDE
  • conjugated MetalloP
    mono polymer homomer , dimer
    HOMOLOGY
    Homologene
    FAMILY
  • peptidase M16 family
  • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,peroxisome
    intracellular,cytoplasm,cytosolic
    text zinc metalloprotease found in the cytosol of all cells (Carpenter 2010)
    basic FUNCTION
  • may play a role in the cellular processing of insulin
  • may be involved in intercellular peptide signaling
  • involved in the termination of the insulin response
  • involved in the clearance of insulin and amyloid-beta
  • acting as a zinc metalloprotease involved in the degradation of the amyloid beta-peptide (Carpenter 2010)
  • exhibits a remarkable specificity to degrade insulin without breaking the disulfide bonds that hold the insulin A and B chains together (Manolopoulou 2009)
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • complex with four substrates (insulin B chain, amyloid-beta peptide (1-40), amylin and glucagon)
  • INTERACTION
    DNA
    RNA
    small molecule metal binding,
  • one zinc ion per subunit
  • protein
  • binds to the nonglycosylated precursor of varicella-zoster virus gE protein found in the endoplasmic reticulum (Carpenter 2010)
  • IAPP is also a known substrate of the protease insulin-degrading enzyme (IDE)
  • cell & other
    REGULATION
    inhibited by potently by physiologically relevant concentrations of S-nitrosylation and oxidation agents (Malito 2008)
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    reduction in MME and IDE activity is not the primary cause of APP accumulation in Alzheimer disease, but rather a late-stage phenomenon secondary to neurodegeneration
    Susceptibility to type 2 diabetes
    Variant & Polymorphism other
  • polymorphisms increasing the risk of type 2 diabetes
  • association of IDE polymorphisms with T2DM (Rudovich 2009)
  • Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    diabetetype 2 
    inhibition of IDE may represent an approach to improve glucose metabolism in human type 2 diabetes, without inducing amyloid deposition and its deleterious effects
    ANIMAL & CELL MODELS