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Protein

Insulin-degrading enzyme

Gene

IDE

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Degradation of insulin, glucagon and other polypeptides. No action on proteins.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Activated by ATP, other nucleotide triphosphates and small peptides. Inhibited by bacitracin (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081ZincPROSITE-ProRule annotation
Active sitei111 – 1111Proton acceptorPROSITE-ProRule annotation
Metal bindingi112 – 1121ZincPROSITE-ProRule annotation
Metal bindingi189 – 1891ZincPROSITE-ProRule annotation
Binding sitei429 – 4291ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi895 – 9017ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPSiM16.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-degrading enzyme (EC:3.4.24.56)
Alternative name(s):
Insulin protease
Short name:
Insulinase
Insulysin
Gene namesi
Name:IDE
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 26

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10191019Insulin-degrading enzymePRO_0000283041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-succinyllysineBy similarity
Modified residuei697 – 6971N6-succinyllysineBy similarity

Proteomic databases

PRIDEiQ24K02.

Interactioni

Subunit structurei

Homodimer. Can form higher oligomers (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000026332.

Structurei

3D structure databases

ProteinModelPortaliQ24K02.
SMRiQ24K02. Positions 43-1016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi853 – 8586SlyX motif

Domaini

The SlyX motif may be involved in the non-conventional secretion of the protein.By similarity

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Phylogenomic databases

eggNOGiCOG1025.
GeneTreeiENSGT00530000063327.
HOGENOMiHOG000161331.
HOVERGENiHBG106799.
InParanoidiQ24K02.
KOiK01408.
OMAiQPRKQLK.
OrthoDBiEOG7HHWRD.
TreeFamiTF106275.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24K02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYRLAWLLH SALPSTFRSV LGARLPPSER LCGFQKKTYS KMNNPAIKRI
60 70 80 90 100
GHHIIKSHED KREYRGLELA NGIKVLLVSD PTTDKSSAAL DVHIGSLSDP
110 120 130 140 150
PNIAGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY
160 170 180 190 200
FDVSHEHLEG ALDRFAQFFL CPLFDESCKD REVNAVDSEH EKNVMNDAWR
210 220 230 240 250
LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE LLKFHSTYYS
260 270 280 290 300
SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ
310 320 330 340 350
LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL
360 370 380 390 400
KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK
410 420 430 440 450
LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGI LHYYPLEEVL
460 470 480 490 500
TAEYLLEEFR PDLIEMVLDK LRPENVRVAI VSKSFEGKTD RTEEWYGTQY
510 520 530 540 550
KQEAIPDEVI KKWQNADLNG KFKLPMKNEF IPTNFEILSL EKEATPYPSL
560 570 580 590 600
IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL
610 620 630 640 650
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA
660 670 680 690 700
TFEIDEKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL
710 720 730 740 750
KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG IMQMVEDTLI
760 770 780 790 800
EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ
810 820 830 840 850
STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII
860 870 880 890 900
QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL
910 920 930 940 950
SAECAKYWGE IISQQYNFDR DNIEVAYLKT LTKEDIIKFY KEMLAVDAPR
960 970 980 990 1000
RHKVSVHVLA REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR
1010
GLPLFPLVKP HINFMAAKL
Length:1,019
Mass (Da):118,102
Last modified:April 18, 2006 - v1
Checksum:iE3B589575B95C861
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114105 mRNA. Translation: AAI14106.1.
RefSeqiNP_001069317.1. NM_001075849.1.
UniGeneiBt.6675.

Genome annotation databases

EnsembliENSBTAT00000026332; ENSBTAP00000026332; ENSBTAG00000019759.
GeneIDi523752.
KEGGibta:523752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC114105 mRNA. Translation: AAI14106.1.
RefSeqiNP_001069317.1. NM_001075849.1.
UniGeneiBt.6675.

3D structure databases

ProteinModelPortaliQ24K02.
SMRiQ24K02. Positions 43-1016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000026332.

Protein family/group databases

MEROPSiM16.982.

Proteomic databases

PRIDEiQ24K02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000026332; ENSBTAP00000026332; ENSBTAG00000019759.
GeneIDi523752.
KEGGibta:523752.

Organism-specific databases

CTDi3416.

Phylogenomic databases

eggNOGiCOG1025.
GeneTreeiENSGT00530000063327.
HOGENOMiHOG000161331.
HOVERGENiHBG106799.
InParanoidiQ24K02.
KOiK01408.
OMAiQPRKQLK.
OrthoDBiEOG7HHWRD.
TreeFamiTF106275.

Miscellaneous databases

NextBioi20873816.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiIDE_BOVIN
AccessioniPrimary (citable) accession number: Q24K02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 18, 2006
Last modified: May 27, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

ATP-binding induces a conformation change.By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.