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P22817 (IDE_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:CG5517
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length990 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can cleave insulin and TGF-alpha. Ref.6

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Induction

Inhibited by bacitracin and sulfhydryl-specific reagents. Ref.6

Sequence similarities

Belongs to the peptidase M16 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7-8. Ref.6

Temperature dependence:

Optimum temperature is 37 degrees Celsius.

Sequence caution

The sequence AAL28563.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAO74689.1 differs from that shown. Reason: Erroneous initiation.

The sequence ACM16704.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 990989Insulin-degrading enzyme
PRO_0000074407

Sites

Active site841Proton acceptor By similarity
Metal binding811Zinc By similarity
Metal binding851Zinc By similarity
Metal binding1621Zinc By similarity

Experimental info

Sequence conflict111A → V in AAA28439. Ref.1
Sequence conflict1781N → D in AAO74689. Ref.4
Sequence conflict3841F → L in AAA28439. Ref.1
Sequence conflict402 – 4032QP → ES in AAA28439. Ref.1
Sequence conflict4151Q → K in AAA28439. Ref.1
Sequence conflict4331R → S in AAA28439. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22817 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 32D19736CB497DCB

FASTA990113,684
        10         20         30         40         50         60 
MTIAESSQKS ATRKPDSMEP ILRLNNIEKS LQDTRDYRGL QLENGLKVLL ISDPNTDVSA 

        70         80         90        100        110        120 
AALSVQVGHM SDPTNLPGLA HFCEHMLFLG TEKYPHENGY TTYLSQSGGS SNAATYPLMT 

       130        140        150        160        170        180 
KYHFHVAPDK LDGALDRFAQ FFIAPLFTPS ATEREINAVN SEHEKNLPSD LWRIKQVNRH 

       190        200        210        220        230        240 
LAKPDHAYSK FGSGNKTTLS EIPKSKNIDV RDELLKFHKQ WYSANIMCLA VIGKESLDEL 

       250        260        270        280        290        300 
EGMVLEKFSE IENKNVKVPG WPRHPYAEER YGQKVKIVPI KDIRSLTISF TTDDLTQFYK 

       310        320        330        340        350        360 
SGPDNYLTHL IGHEGKGSIL SELRRLGWCN DLMAGHQNTQ NGFGFFDIVV DLTQEGLEHV 

       370        380        390        400        410        420 
DDIVKIVFQY LEMLRKEGPK KWIFDECVKL NEMRFRFKEK EQPENLVTHA VSSMQIFPLE 

       430        440        450        460        470        480 
EVLIAPYLSN EWRPDLIKGL LDELVPSKSR IVIVSQSFEP DCDLAEPYYK TKYGITRVAK 

       490        500        510        520        530        540 
DTVQSWENCE LNENLKLALP NSFIPTNFDI SDVPADAPKH PTIILDTPIL RVWHKQDNQF 

       550        560        570        580        590        600 
NKPKACMTFD MSNPIAYLDP LNCNLNHMMV MLLKDQLNEY LYDAELASLK LSVMGKSCGI 

       610        620        630        640        650        660 
DFTIRGFSDK QVVLLEKLLD HLFDFSIDEK RFDILKEEYV RSLKNFKAEQ PYQHSIYYLA 

       670        680        690        700        710        720 
LLLTENAWAN MELLDAMELV TYDRVLNFAK EFFQRLHTEC FIFGNVTKQQ ATDIAGRVNT 

       730        740        750        760        770        780 
RLEATNASKL PILARQMLKK REYKLLAGDS YLFEKENEFH KSSCAQLYLQ CGAQTDHTNI 

       790        800        810        820        830        840 
MVNLVSQVLS EPCYDCLRTK EQLGYIVFSG VRKVNGANGI RIIVQSAKHP SYVEDRIENF 

       850        860        870        880        890        900 
LQTYLQVIED MPLDEFERHK EALAVKKLEK PKTIFQQFSQ FYGEIAMQTY HFEREEAEVA 

       910        920        930        940        950        960 
ILRKISKADF VDYFKKFIAK DGEERRVLSV HIVSQQTDEN ATSEAEPVEI TNMERHKPIS 

       970        980        990 
DIVTFKSCKE LYPIALPFLD IKAKGARSKL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme."
Kuo W.L., Gehm B.D., Rosner M.R.
Mol. Endocrinol. 4:1580-1591(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G. expand/collapse author list , Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 663-990.
Strain: Berkeley.
Tissue: Embryo.
[6]"Isolation and characterization of an insulin-degrading enzyme from Drosophila melanogaster."
Garcia J.V., Fenton B.W., Rosner M.R.
Biochemistry 27:4237-4244(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58465 mRNA. Translation: AAA28439.1.
AE014296 Genomic DNA. Translation: AAF51584.3.
BT006006 mRNA. Translation: AAO74689.1. Different initiation.
BT057994 mRNA. Translation: ACM16704.1. Different initiation.
AY061015 mRNA. Translation: AAL28563.1. Different initiation.
PIRSNFFIN. A37254.
RefSeqNP_524182.3. NM_079458.4.
UniGeneDm.36730.

3D structure databases

ProteinModelPortalP22817.
SMRP22817. Positions 25-977.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM16.002.

Proteomic databases

PaxDbP22817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0273273; FBpp0271781; FBgn0001247.
GeneID40248.
KEGGdme:Dmel_CG5517.

Organism-specific databases

CTD3416.
FlyBaseFBgn0001247. Ide.

Phylogenomic databases

eggNOGCOG1025.
GeneTreeENSGT00530000063327.
InParanoidP22817.
KOK01408.
OMANPAHPFS.
OrthoDBEOG7HHWRD.
PhylomeDBP22817.

Enzyme and pathway databases

SignaLinkP22817.

Gene expression databases

BgeeP22817.

Family and domain databases

Gene3D3.30.830.10. 4 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
SUPFAMSSF63411. SSF63411. 4 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIDE. drosophila.
GenomeRNAi40248.
NextBio817784.
PROP22817.

Entry information

Entry nameIDE_DROME
AccessionPrimary (citable) accession number: P22817
Secondary accession number(s): B9EQR9 expand/collapse secondary AC list , Q86MR2, Q95S06, Q9VPG8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase