Ide insulin degrading enzyme [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ideprovided by MGI
Official Full Name: insulin degrading enzymeprovided by MGI
Primary source: MGI:MGI:96412
See related: Ensembl:ENSMUSG00000056999 AllianceGenome:MGI:96412
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 1300012G03Rik; 4833415K22Rik
Summary: Enables endopeptidase activity. Involved in insulin catabolic process and insulin receptor recycling. Acts upstream of or within amyloid-beta clearance and response to oxidative stress. Located in extracellular exosome. Is active in endosome lumen. Is expressed in several structures, including alimentary system; central nervous system; genitourinary system; respiratory system; and sensory organ. Human ortholog(s) of this gene implicated in Alzheimer's disease and type 2 diabetes mellitus. Orthologous to human IDE (insulin degrading enzyme). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in testis adult (RPKM 23.4), genital fat pad adult (RPKM 9.6) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 19 C2; 19 32.24 cM

Exon count:: 30

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	19	NC_000085.7 (37246140..37341664, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	19	NC_000085.6 (37268743..37334544, complement)

Chromosome 19 - NC_000085.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Insulin-degrading enzyme (IDE) as a modulator of microglial phenotypes in the context of Alzheimer's disease and brain aging.
Title: Insulin-degrading enzyme (IDE) as a modulator of microglial phenotypes in the context of Alzheimer's disease and brain aging.
Insulin-degrading enzyme ablation in mouse pancreatic alpha cells triggers cell proliferation, hyperplasia and glucagon secretion dysregulation.
Title: Insulin-degrading enzyme ablation in mouse pancreatic alpha cells triggers cell proliferation, hyperplasia and glucagon secretion dysregulation.
Evolutionary Origin of Insulin-Degrading Enzyme and Its Subcellular Localization and Secretion Mechanism: A Study in Microglial Cells.
Title: Evolutionary Origin of Insulin-Degrading Enzyme and Its Subcellular Localization and Secretion Mechanism: A Study in Microglial Cells.
Medium-Chain Length Fatty Acids Enhance Abeta Degradation by Affecting Insulin-Degrading Enzyme.
Title: Medium-Chain Length Fatty Acids Enhance Aβ Degradation by Affecting Insulin-Degrading Enzyme.
Hepatic insulin-degrading enzyme regulates glucose and insulin homeostasis in diet-induced obese mice.
Title: Hepatic insulin-degrading enzyme regulates glucose and insulin homeostasis in diet-induced obese mice.
isolated islets from B-IDE-KO mice showed constitutive insulin secretion, a hallmark of beta-cell functional immaturity
Title: Pancreatic β-cell-specific deletion of insulin-degrading enzyme leads to dysregulated insulin secretion and β-cell functional immaturity.
IDE plays an important role in determining the reproductive potential of males.
Title: Knockout of insulin-degrading enzyme leads to mice testicular morphological changes and impaired sperm quality.
s treatment with TUDCA reestablished plasma insulin to physiological concentrations in high fat diet (HFD) mice, a phenomenon associated with increased insulin clearance and liver IDE
Title: Bile acid TUDCA improves insulin clearance by increasing the expression of insulin-degrading enzyme in the liver of obese mice.
IDE is not a rate-limiting regulator of plasma insulin levels in vivo.
Title: Liver-specific ablation of insulin-degrading enzyme causes hepatic insulin resistance and glucose intolerance, without affecting insulin clearance in mice.
Study indicated that, in the type 2 diabetes (T2D) and Alzheimer's disease (AD) mice, cAMP/PKA signaling pathway and IDE may participate in the contribute role of T2D in accelerating the pathological process of AD via causing neuronal apoptosis.
Title: cAMP/PKA signaling pathway contributes to neuronal apoptosis via regulating IDE expression in a mixed model of type 2 diabetes and Alzheimer's disease.

Submit: New GeneRIF Correction See all GeneRIFs (36)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1)
Gene trapped (1)
Targeted (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI507533 (e-PCR)
- UniSTS:164656

NoName (e-PCR)
- UniSTS:237931

Ide (e-PCR), detects polymorphism
- UniSTS:506987

RH124457 (e-PCR)
- UniSTS:161279

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATP binding	ISO Inferred from Sequence Orthology more info
enables ATP binding	ISS Inferred from Sequence or Structural Similarity more info
enables ATP hydrolysis activity	ISO Inferred from Sequence Orthology more info
enables amyloid-beta binding	ISO Inferred from Sequence Orthology more info
enables beta-endorphin binding	ISO Inferred from Sequence Orthology more info
enables endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables endopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables insulin binding	ISO Inferred from Sequence Orthology more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	ISO Inferred from Sequence Orthology more info
enables metalloendopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables peptide binding	ISO Inferred from Sequence Orthology more info
enables peptide hormone binding	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within amyloid-beta clearance	IDA Inferred from Direct Assay more info	PubMed
involved_in amyloid-beta clearance	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in amyloid-beta clearance	ISO Inferred from Sequence Orthology more info
involved_in amyloid-beta clearance by cellular catabolic process	ISO Inferred from Sequence Orthology more info
involved_in amyloid-beta metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in amyloid-beta metabolic process	ISO Inferred from Sequence Orthology more info
involved_in amyloid-beta metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in antigen processing and presentation of endogenous peptide antigen via MHC class I	ISO Inferred from Sequence Orthology more info
involved_in antigen processing and presentation of endogenous peptide antigen via MHC class I	ISS Inferred from Sequence or Structural Similarity more info
involved_in bradykinin catabolic process	ISO Inferred from Sequence Orthology more info
involved_in bradykinin catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in hormone catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in hormone catabolic process	ISO Inferred from Sequence Orthology more info
involved_in hormone catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in insulin catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in insulin catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in insulin catabolic process	ISO Inferred from Sequence Orthology more info
involved_in insulin catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in insulin metabolic process	ISO Inferred from Sequence Orthology more info
involved_in insulin receptor recycling	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of proteolysis	ISO Inferred from Sequence Orthology more info
involved_in peptide catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in peptide catabolic process	ISO Inferred from Sequence Orthology more info
involved_in peptide catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein binding	ISO Inferred from Sequence Orthology more info
involved_in protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in protein catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in proteolysis	ISO Inferred from Sequence Orthology more info
involved_in proteolysis involved in protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis involved in protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in regulation of aerobic respiration	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed
involved_in ubiquitin recycling	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in basolateral plasma membrane	ISO Inferred from Sequence Orthology more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity more info
part_of cytosolic proteasome complex	ISO Inferred from Sequence Orthology more info
is_active_in endosome lumen	IDA Inferred from Direct Assay more info	PubMed
located_in external side of plasma membrane	ISO Inferred from Sequence Orthology more info
located_in extracellular exosome	IMP Inferred from Mutant Phenotype more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
is_active_in peroxisomal matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info
located_in peroxisome	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: insulin-degrading enzyme

Names: insulin protease; insulinase; insulysin

NP_112419.4

EC 3.4.24.56

XP_036017334.1

EC 3.4.24.56

XP_036017335.1

EC 3.4.24.56

XP_036017336.1

EC 3.4.24.56

XP_036017337.1

EC 3.4.24.56

XP_036017338.1

EC 3.4.24.56

XP_036017339.1

EC 3.4.24.56

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_031156.4 → NP_112419.4 insulin-degrading enzyme

Status: VALIDATED

Source sequence(s)

AA163502, AJ278422, AK004972, AK078930, BU698019

UniProtKB/Swiss-Prot

Q9JHR7

UniProtKB/TrEMBL

F6RPJ9, Q8CGB9

Related

ENSMUSP00000121358.3, ENSMUST00000131070.3

Conserved Domains (1) summary

COG1025
Location:45 → 958

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000085.7 Reference GRCm39 C57BL/6J

Range

37246140..37341664 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_036161446.1 → XP_036017339.1 insulin-degrading enzyme isoform X2

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:70 → 983

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
XM_036161441.1 → XP_036017334.1 insulin-degrading enzyme isoform X1

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:4 → 917

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
XM_036161444.1 → XP_036017337.1 insulin-degrading enzyme isoform X1

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:4 → 917

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
XM_036161443.1 → XP_036017336.1 insulin-degrading enzyme isoform X1

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:4 → 917

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
XM_036161445.1 → XP_036017338.1 insulin-degrading enzyme isoform X1

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:4 → 917

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]
XM_036161442.1 → XP_036017335.1 insulin-degrading enzyme isoform X1

UniProtKB/Swiss-Prot

Q9JHR7

Conserved Domains (1) summary

COG1025
Location:4 → 917

Ptr; Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones]