Names & Taxonomy

Uniprot ID:
P14735
Entry Name:
IDE_HUMAN
Status:
reviewed
Protein Names:
Insulin-degrading enzyme (EC 3.4.24.56) (Abeta-degrading protease) (Insulin protease) (Insulinase) (Insulysin)
Gene Names:
IDE
Gene Names Primary:
IDE
Organism:
Homo sapiens (Human)

Structure

Length:
1019
Sequence:
MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Cytoplasm. Cell membrane. Secreted

Function

Function:
Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.
Catalytic Activity:
Degradation of insulin, glucagon and other polypeptides. No action on proteins.
Cofactor:
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Enzyme Regulation:
ENZYME REGULATION: Activated by small peptides (By similarity). Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi. Inhibited by bacitracin. Inhibited by S-nitrosylation and oxidation agents.
Active Site:
ACT_SITE 111 111 Proton acceptor.
Cross Reference Drug Bank:
DB00626 DB00030
Gene Ontology Go:
cell surface
cytoplasm
cytosol
cytosolic proteasome complex
extracellular space
mitochondrion
nucleoplasm
nucleus
peroxisomal matrix
peroxisome
plasma membrane
ATP binding
ATPase activity
beta-amyloid binding
beta-endorphin binding
glycoprotein binding
insulin binding
metalloendopeptidase activity
peptide binding
protein homodimerization activity
receptor binding
ubiquitin binding
virus receptor activity
zinc ion binding
beta-amyloid metabolic process
bradykinin catabolic process
determination of adult lifespan
hormone catabolic process
insulin catabolic process
insulin metabolic process
insulin receptor signaling pathway
negative regulation of proteolysis
positive regulation of protein oligomerization
protein heterooligomerization
protein homooligomerization
protein homotetramerization
protein processing
proteolysis
proteolysis involved in cellular protein catabolic process
ubiquitin homeostasis
Gene Ontology Biological Process:
beta-amyloid metabolic process
bradykinin catabolic process
determination of adult lifespan
hormone catabolic process
insulin catabolic process
insulin metabolic process
insulin receptor signaling pathway
negative regulation of proteolysis
positive regulation of protein oligomerization
protein heterooligomerization
protein homooligomerization
protein homotetramerization
protein processing
proteolysis
proteolysis involved in cellular protein catabolic process
ubiquitin homeostasis
Gene Ontology Molecular Function:
ATPase activity
ATP binding
beta-amyloid binding
beta-endorphin binding
glycoprotein binding
insulin binding
metalloendopeptidase activity
peptide binding
protein homodimerization activity
receptor binding
ubiquitin binding
virus receptor activity
zinc ion binding
Gene Ontology Cellular Component:
cell surface
cytoplasm
cytosol
cytosolic proteasome complex
extracellular space
mitochondrion
nucleoplasm
nucleus
peroxisomal matrix
peroxisome
plasma membrane
Keywords:
3D-structure
ATP-binding
Allosteric enzyme
Alternative splicing
Cell membrane
Complete proteome
Cytoplasm
Direct protein sequencing
Host cell receptor for virus entry
Host-virus interaction
Hydrolase
Membrane
Metal-binding
Metalloprotease
Nucleotide-binding
Polymorphism
Protease
Receptor
Reference proteome
Secreted
Zinc
Interacts With:
P10147

Publication

PubMed ID:
3059494 2293021 14702039 15164054 15489334 10684867 17055432 17553876 21269460 17051221 17613531 18986166