Ide
entrez
25700
canonical
uniprot
P35559
canonical
ensembl
ENSRNOG00000016833
resolver
ensembl
ENSRNOG00055027358
resolver
ensembl
ENSRNOG00065028018
resolver
ensp
ENSRNOP00000074304
resolver
ensp
ENSRNOP00000087605
resolver
ensp
ENSRNOP00000088595
resolver
ensp
ENSRNOP00000089992
resolver
ensp
ENSRNOP00055038987
resolver
ensp
ENSRNOP00065039691
resolver
enst
ENSRNOT00000085303
resolver
enst
ENSRNOT00000098836
resolver
enst
ENSRNOT00000110995
resolver
enst
ENSRNOT00000119683
resolver
enst
ENSRNOT00055047407
resolver
enst
ENSRNOT00065048381
resolver
genesymbol
Ide
resolver
uniprot
A0A8I6A841
resolver
uniprot
A0A8I6A860
resolver
uniprot_entry
A0A8I6A841_RAT
resolver
uniprot_entry
A0A8I6A860_RAT
resolver
uniprot_entry
IDE_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated by ATP, other nucleotide triphosphates and small peptides (PubMed:14527953, PubMed:21731629, PubMed:22049080). Inhibited by bacitracin (PubMed:12941771). {ECO:0000269|PubMed:12941771, ECO:0000269|PubMed:14527953, ECO:0000269|PubMed:21731629, ECO:0000269|PubMed:22049080}.
uniprot
proteins
amino_acid_sequence
MRNGLVWLLHPALPSTLHSILGARPPPVKRLCGFPKQIYSTMNNPAIQRIEDHIVKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIPGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDASCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVREELLKFHSTYYSSNLMAICVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQQYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGKLHYYPLNGVLTAEYLLEEFRPDLIDMVLDKLRPENVRVAIVSKSFEGKTDRTEQWYGTQYKQEAIPEDVIQKWQNADLNGKFKLPTKNEFIPTNFEILALEKDATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKITEKMATFEIDKKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGVMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQRRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKAIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNYDRDNIEVAYLKTLSKDDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPSQNDINLSEAPPLPQPEVIHNMTEFKRGLPLFPLVKPHINFMAAKL
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:12941771, PubMed:1445854, PubMed:14527953, PubMed:1836994, PubMed:22049080). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (By similarity). 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 (PubMed:10684867). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (By similarity). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (By similarity). 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:P14735, ECO:0000250|UniProtKB:Q9JHR7, ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:12941771, ECO:0000269|PubMed:1445854, ECO:0000269|PubMed:14527953, ECO:0000269|PubMed:1836994, ECO:0000269|PubMed:22049080}.
uniprot
proteins
mass_dalton
117710
uniprot
proteins
mutagenesis
MUTAGEN 111; /note="E->F: Expected to abolish catalytic activity."; /evidence="ECO:0000269|PubMed:21731629"; MUTAGEN 111; /note="E->V: Abolishes catalytic activity. No effect on substrate binding."; /evidence="ECO:0000269|PubMed:14527953"; MUTAGEN 112; /note="H->Q: Abolishes catalytic activity. Decreases substrate binding affinity."; /evidence="ECO:0000269|PubMed:14527953"; MUTAGEN 360; /note="V->S: Strongly reduced catalytic activity. Strongly reduced stimulation of activity by ATP."; /evidence="ECO:0000269|PubMed:21731629"; MUTAGEN 374; /note="I->S: Strongly reduced catalytic activity. Abolishes stimulation of activity by ATP."; /evidence="ECO:0000269|PubMed:21731629"; MUTAGEN 429; /note="R->S: Greatly decreased activation by polyphosphate anions."; /evidence="ECO:0000269|PubMed:22049080"; MUTAGEN 609; /note="Y->F: Strongly reduced catalytic activity. Abolishes stimulation of activity by ATP."; /evidence="ECO:0000269|PubMed:21731629"; MUTAGEN 898; /note="K->A: Greatly decreased activation by polyphosphate anions, and deficient in activation by small peptides; when associated with A-899 and A-901."; /evidence="ECO:0000269|PubMed:22049080"; MUTAGEN 899; /note="K->A: Greatly decreased activation by polyphosphate anions, and deficient in activation by small peptides; when associated with A-898 and A-901."; /evidence="ECO:0000269|PubMed:22049080"; MUTAGEN 901; /note="S->A: Greatly decreased activation by polyphosphate anions, and deficient in activation by small peptides; when associated with A-898 and A-899."; /evidence="ECO:0000269|PubMed:22049080
uniprot
proteins
protein_family
Peptidase M16 family
uniprot
proteins
pubmed
10684867
uniprot
proteins
pubmed
12941771
uniprot
proteins
pubmed
1445854
uniprot
proteins
pubmed
14527953
uniprot
proteins
pubmed
1836994
uniprot
proteins
pubmed
21731629
uniprot
proteins
pubmed
22049080
uniprot
proteins
pubmed
7678795
uniprot
proteins
pubmed
8425612
uniprot
proteins
sequence_length
1019
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:1836994}. Cell membrane {ECO:0000269|PubMed:10684867}. Secreted {ECO:0000269|PubMed:10684867}.
uniprot
proteins