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Reviewed, UniProtKB/Swiss-Prot P14735 (IDE_HUMAN)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Insulin-degrading enzyme
    EC=3.4.24.56
Alternative name(s):
    Insulin protease
      Short name=Insulinase
    Insulysin
Gene names
Name: IDE
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1019 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May play a role in the cellular processing of insulin. May be involved in intercellular peptide signaling.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peptidase M16 family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Traceable author statement. Source: ProtInc

sex differentiation

Traceable author statement. Source: ProtInc

signal transduction Ref.2

Non-traceable author statement. Source: ProtInc

   Cellular componentextracellular space

Traceable author statement. Source: ProtInc

peroxisome

Traceable author statement. Source: ProtInc

soluble fraction

Traceable author statement. Source: ProtInc

   Molecular functionmetalloendopeptidase activity Ref.2

Traceable author statement. Source: ProtInc

signal transducer activity Ref.1 Ref.2

Traceable author statement. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 10191018Insulin-degrading enzyme
PRO_0000074404

Sites

Active site1111Proton acceptor By similarity
Metal binding1081Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1891Zinc By similarity

Natural variations

Natural variant6121E → K: dbSNP rs2229708.
VAR_051571

Experimental info

Sequence conflict781I → M in AAA52712. Ref.2
Sequence conflict5551A → V in AAA52712. Ref.2
Sequence conflict567 – 5693FFL → KKK in AAA52712. Ref.2
Sequence conflict8451G → S in AAA52712. Ref.2

Secondary structure

1 ................................................................................................................................................. 1019
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14735-1 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 8A28AEF75EDA0EDA

FASTA1,019117,968
        10         20         30         40         50         60 
MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED 

        70         80         90        100        110        120 
KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK 

       130        140        150        160        170        180 
YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD 

       190        200        210        220        230        240 
REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE 

       250        260        270        280        290        300 
LLKFHSAYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ 

       310        320        330        340        350        360 
LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV 

       370        380        390        400        410        420 
GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV 

       430        440        450        460        470        480 
AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI 

       490        500        510        520        530        540 
VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL 

       550        560        570        580        590        600 
EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL 

       610        620        630        640        650        660 
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE 

       670        680        690        700        710        720 
IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL 

       730        740        750        760        770        780 
SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ 

       790        800        810        820        830        840 
QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA 

       850        860        870        880        890        900 
NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL 

       910        920        930        940        950        960 
SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR RHKVSVHVLA 

       970        980        990       1000       1010 
REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR GLPLFPLVKP HINFMAAKL

« Hide

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References

« Hide 'large scale' references
[1]"Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III."
Affholter J.A., Fried V.A., Roth R.A.
Science 242:1415-1418(1988) [PubMed: 3059494] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes."
Affholter J.A., Hsieh C.L., Francke U., Roth R.A.
Mol. Endocrinol. 4:1125-1135(1990) [PubMed: 2293021] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M21188 mRNA. Translation: AAA52712.1.
AL356128 Genomic DNA. Translation: CAI13670.1.
CH471066 Genomic DNA. Translation: EAW50090.1.
BC096336 mRNA. Translation: AAH96336.1.
BC096337 mRNA. Translation: AAH96337.1.
BC096339 mRNA. Translation: AAH96339.1.
IPIIPI00220373.
PIRSNHUIN. A40119.
RefSeqNP_004960.2.
UniGeneHs.500546

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2G47X-ray2.10A/B42-1019[»]
2G48X-ray2.60A/B42-1019[»]
2G49X-ray2.50A/B42-1019[»]
2G54X-ray2.25A/B42-1019[»]
2G56X-ray2.20A/B42-1019[»]
2JBUX-ray3.00A/B42-1019[»]
2JG4X-ray2.80A/B43-1018[»]
2WBYX-ray2.60A/B42-1019[»]
2WC0X-ray2.80A/B42-1019[»]
3CWWX-ray1.96A/B42-1019[»]
ModBaseSearch...

Proteomic databases

PRIDEP14735.

Genome annotation databases

EnsemblENSG00000119912. Homo sapiens. [Contig view]
GeneID3416.
KEGGhsa:3416.
NMPDRfig|9606.3.peg.4351.

Organism-specific databases

GeneCardsGC10M094201.
H-InvDBHIX0009042.
HGNCHGNC:5381. IDE.
HPACAB012303.
MIM146680. gene.
PharmGKBPA29629.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP14735.
HOVERGENP14735.
OMAP14735. FYIQSPT.

Enzyme and pathway databases

BRENDA3.4.24.56. 247.

Gene expression databases

ArrayExpressP14735.
BgeeP14735.
CleanExHS_IDE.
GermOnlineENSG00000119912. Homo sapiens.

Family and domain databases

InterProIPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 1 hit.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00626. Bacitracin.
DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.
SOURCESearch...

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Entry information

Entry nameIDE_HUMAN
AccessionPrimary (citable) accession number: P14735
Secondary accession number(s): Q5T5N2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: June 16, 2009
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents