Protein name:
Insulin-degrading enzyme ;
Alternative:
Insulin protease (Insulinase) ;Abeta-degrading protease ;Insulysin ;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Homodimer. Can form higher oligomers. Interacts (via N-terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform may function as an entry receptor for this virus.
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.
Subcellular Location:
Cytoplasm
Cell surface
Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.
Protein Attributes:
50:
MRYRLAWLLH | PALPSTFRSV | LGARLPPPER | LCGFQKKTYS | KMNNPAIKRI |
100:
GNHITKSPED | KREYRGLELA | NGIKVLLISD | PTTDKSSAAL | DVHIGSLSDP |
150:
PNIAGLSHFC | EHMLFLGTKK | YPKENEYSQF | LSEHAGSSNA | FTSGEHTNYY |
200:
FDVSHEHLEG | ALDRFAQFFL | CPLFDESCKD | REVNAVDSEH | EKNVMNDAWR |
250:
LFQLEKATGN | PKHPFSKFGT | GNKYTLETRP | NQEGIDVRQE | LLKFHSAYYS |
300:
SNLMAVCVLG | RESLDDLTNL | VVKLFSEVEN | KNVPLPEFPE | HPFQEEHLKQ |
350:
LYKIVPIKDI | RNLYVTFPIP | DLQKYYKSNP | GHYLGHLIGH | EGPGSLLSEL |
400:
KSKGWVNTLV | GGQKEGARGF | MFFIINVDLT | EEGLLHVEDI | ILHMFQYIQK |
450:
LRAEGPQEWV | FQECKDLNAV | AFRFKDKERP | RGYTSKIAGI | LHYYPLEEVL |
500:
TAEYLLEEFR | PDLIEMVLDK | LRPENVRVAI | VSKSFEGKTD | RTEEWYGTQY |
550:
KQEAIPDEVI | KKWQNADLNG | KFKLPTKNEF | IPTNFEILPL | EKEATPYPAL |
600:
IKDTAMSKLW | FKQDDKFFLP | KACLNFEFFS | PFAYVDPLHC | NMAYLYLELL |
650:
KDSLNEYAYA | AELAGLSYDL | QNTIYGMYLS | VKGYNDKQPI | LLKKIIEKMA |
700:
TFEIDEKRFE | IIKEAYMRSL | NNFRAEQPHQ | HAMYYLRLLM | TEVAWTKDEL |
750:
KEALDDVTLP | RLKAFIPQLL | SRLHIEALLH | GNITKQAALG | IMQMVEDTLI |
800:
EHAHTKPLLP | SQLVRYREVQ | LPDRGWFVYQ | QRNEVHNNCG | IEIYYQTDMQ |
850:
STSENMFLEL | FCQIISEPCF | NTLRTKEQLG | YIVFSGPRRA | NGIQGLRFII |
900:
QSEKPPHYLE | SRVEAFLITM | EKSIEDMTEE | AFQKHIQALA | IRRLDKPKKL |
950:
SAECAKYWGE | IISQQYNFDR | DNTEVAYLKT | LTKEDIIKFY | KEMLAVDAPR |
1000:
RHKVSVHVLA | REMDSCPVVG | EFPCQNDINL | SQAPALPQPE | VIQNMTEFKR |
1019:
GLPLFPLVKP | HINFMAAKL
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Mouse
Human
Rat
Bovine
ELISA Kit for Human Insulin-degrading enzyme
ELISA Kit for Human Insulin-degrading enzyme
ELISA Kit for Human Insulin-degrading enzyme
ELISA Kit for Human Insulin-degrading enzyme
CLIA Kit for Human Insulin-degrading enzyme
CLIA Kit for Human Insulin-degrading enzyme
CLIA Kit for Human Insulin-degrading enzyme
CLIA Kit for Human Insulin-degrading enzyme
Polyclonal Antibody for Human Insulin-degrading enzyme
Polyclonal Antibody for Human Insulin-degrading enzyme
Polyclonal Antibody for Human Insulin-degrading enzyme
Polyclonal Antibody for Human Insulin-degrading enzyme
Monoclonal Antibody for Human Insulin-degrading enzyme
Monoclonal Antibody for Human Insulin-degrading enzyme
Monoclonal Antibody for Human Insulin-degrading enzyme
Monoclonal Antibody for Human Insulin-degrading enzyme
Protein for Human Insulin-degrading enzyme
Protein for Human Insulin-degrading enzyme
Protein for Human Insulin-degrading enzyme
Protein for Human Insulin-degrading enzyme
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);SEQUENCE REVISION
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Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)
tissue :
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;SUBCELLULAR LOCATION
8.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : SUBCELLULAR LOCATION;INTERACTION WITH VZV GLYCOPROTEIN E
9.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH VZV GLYCOPROTEIN E
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Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
11.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
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Proc. Natl. Acad. Sci. U.S.A.109:12449-12454(2012)
[
PubMed ]
[
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[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
13.
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Cited for : X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-1019 OF MUTANT GLN-111 IN COMPLEXES WITH ZINC IONS; IAPP; INSULIN; AMYLOID AND GLUCAGON;MUTAGENESIS OF GLU-111; SER-132; ASN-184; ASP-426; GLU-817; GLN-828 AND LYS-899;COFACTOR;SUBUNIT;ACTIVE SITE
14.
"Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE."
Im H.
,
Manolopoulou M.
,
Malito E.
,
Shen Y.
,
Zhao J.
,
Neant-Fery M.
,
Sun C.-Y.
,
Meredith S.C.
,
Sisodia S.S.
,
Leissring M.A.
,
Tang W.-J.
J. Biol. Chem.282:25453-25463(2007)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
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Cited for : X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 43-1018 OF MUTANT PHE-831 IN COMPLEX WITH ZINC IONS AND SUBSTRATE PEPTIDE;CATALYTIC ACTIVITY;ENZYME REGULATION;ATP-BINDING;SUBUNIT;MUTAGENESIS OF ASP-426 AND LYS-899;FUNCTION
15.
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Cited for : X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 42-1019 OF MUTANT GLN-111 IN COMPLEX WITH BRADYKININ;FUNCTION;ENZYME REGULATION