IDE
entrez
3416
canonical
uniprot
P14735
canonical
ensembl
ENSG00000119912
resolver
ensp
ENSP00000265986
resolver
ensp
ENSP00000360637
resolver
ensp
ENSP00000497272
resolver
ensp
ENSP00000503025
resolver
ensp
ENSP00000503274
resolver
ensp
ENSP00000504053
resolver
enst
ENST00000496903
resolver
enst
ENST00000650060
resolver
enst
ENST00000677434
resolver
enst
ENST00000678715
resolver
genesymbol
IDE
resolver
hgnc
HGNC:5381
resolver
uniprot
A0A3B3ISG5
resolver
uniprot
A0A7I2V2P6
resolver
uniprot
A0A7I2V373
resolver
uniprot
A0A7I2V4P3
resolver
uniprot
B2R721
resolver
uniprot
B3KSB8
resolver
uniprot
B7ZAU2
resolver
uniprot
D3DR35
resolver
uniprot
Q5T5N2
resolver
uniprot_entry
A0A3B3ISG5_HUMAN
resolver
uniprot_entry
A0A7I2V2P6_HUMAN
resolver
uniprot_entry
A0A7I2V373_HUMAN
resolver
uniprot_entry
A0A7I2V4P3_HUMAN
resolver
uniprot_entry
B3KSB8_HUMAN
resolver
uniprot_entry
IDE_HUMAN
resolver
uniprot_sec
B2R721
resolver
uniprot_sec
B7ZAU2
resolver
uniprot_sec
D3DR35
resolver
uniprot_sec
Q5T5N2
resolver
activity_regulation
ACTIVITY REGULATION: Activated by small peptides (By similarity). Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi (PubMed:17613531). Inhibited by bacitracin (PubMed:17055432, PubMed:17613531). In vitro modification of Cys residues impairs enzyme activity (PubMed:18986166). {ECO:0000250, ECO:0000269|PubMed:17055432, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166}.
uniprot
proteins
amino_acid_sequence
MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL
uniprot
proteins
ec_number
3.4.24.56
uniprot
proteins
function
FUNCTION: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:10684867, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:21098034, PubMed:2293021, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:26968463, PubMed:29596046). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed:23922390, PubMed:26394692, PubMed:29596046). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (Probable) (PubMed:26394692, PubMed:9830016). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (PubMed:21098034). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (PubMed:21098034). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I. {ECO:0000250|UniProtKB:Q9JHR7, ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:2293021, ECO:0000269|PubMed:23922390, ECO:0000269|PubMed:24847884, ECO:0000269|PubMed:26394692, ECO:0000269|PubMed:26968463, ECO:0000269|PubMed:29596046, ECO:0000269|PubMed:9830016, ECO:0000305|PubMed:23922390}.; FUNCTION: (Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV). {ECO:0000269|PubMed:17055432, ECO:0000269|PubMed:17553876}.
uniprot
proteins
mass_dalton
117968
uniprot
proteins
mutagenesis
MUTAGEN 111; /note="E->Q: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446"; MUTAGEN 132; /note="S->C: Increases catalytic rate towards INS and amyloid; when associated with C-817."; /evidence="ECO:0000269|PubMed:17051221"; MUTAGEN 184; /note="N->C: Increases catalytic rate towards INS and amyloid; when associated with C-828."; /evidence="ECO:0000269|PubMed:17051221"; MUTAGEN 286; /note="P->G: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:23922390"; MUTAGEN 366..369; /note="GARG->AARA: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:23922390"; MUTAGEN 426; /note="D->C: Increases catalytic rate towards INS and amyloid; when associated with C-899."; /evidence="ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531"; MUTAGEN 496; /note="Y->A: Strongly reduced enzyme activity."; /evidence="ECO:0000269|PubMed:23922390"; MUTAGEN 530; /note="F->A: Strongly increased enzyme activity."; /evidence="ECO:0000269|PubMed:23922390"; MUTAGEN 767; /note="R->A: Decreases dimerization. No effect on degradation of ANP. Retains the ability to degrade an aberrant form of ANP, when in the presence of both ANP and the aberrant ANP."; /evidence="ECO:0000269|PubMed:23922390"; MUTAGEN 817; /note="E->C: Increases catalytic rate towards INS and amyloid; when associated with C-132."; /evidence="ECO:0000269|PubMed:17051221"; MUTAGEN 828; /note="Q->C: Increases catalytic rate towards INS and amyloid; when associated with C-184."; /evidence="ECO:0000269|PubMed:17051221"; MUTAGEN 831; /note="Y->F: No effect on catalytic activity."; MUTAGEN 899; /note="K->C: Increases catalytic rate towards INS and amyloid; when associated with C-426."; /evidence="ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked.
uniprot
proteins
protein_family
Peptidase M16 family
uniprot
proteins
pubmed
10684867
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17051221
uniprot
proteins
pubmed
17055432
uniprot
proteins
pubmed
17553876
uniprot
proteins
pubmed
17613531
uniprot
proteins
pubmed
18986166
uniprot
proteins
pubmed
19321446
uniprot
proteins
pubmed
20364150
uniprot
proteins
pubmed
21098034
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2293021
uniprot
proteins
pubmed
23922390
uniprot
proteins
pubmed
24847884
uniprot
proteins
pubmed
26394692
uniprot
proteins
pubmed
26968463
uniprot
proteins
pubmed
29596046
uniprot
proteins
pubmed
3059494
uniprot
proteins
pubmed
9830016
uniprot
proteins
sequence_length
1019
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:9830016}. Cell membrane {ECO:0000250|UniProtKB:P35559}. Secreted {ECO:0000269|PubMed:9830016}. Note=Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.
uniprot
proteins