SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P22817

- IDE_DROME

UniProt

P22817 - IDE_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Insulin-degrading enzyme

Gene
Ide, CG5517
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Can cleave insulin and TGF-alpha.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

pH dependencei

Optimum pH is 7-8.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Zinc By similarity
Active sitei84 – 841Proton acceptor By similarity
Metal bindingi85 – 851Zinc By similarity
Metal bindingi162 – 1621Zinc By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. defense response to Gram-negative bacterium Source: FlyBase
  2. determination of adult lifespan Source: FlyBase
  3. negative regulation of growth Source: FlyBase
  4. positive regulation of innate immune response Source: FlyBase
  5. regulation of oviposition Source: FlyBase
  6. regulation of trehalose metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiP22817.

Protein family/group databases

MEROPSiM16.002.

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
ORF Names:CG5517
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0001247. Ide.

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 990989Insulin-degrading enzymePRO_0000074407Add
BLAST

Proteomic databases

PaxDbiP22817.

Expressioni

Inductioni

Inhibited by bacitracin and sulfhydryl-specific reagents.1 Publication

Gene expression databases

BgeeiP22817.

Structurei

3D structure databases

ProteinModelPortaliP22817.
SMRiP22817. Positions 25-977.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.

Phylogenomic databases

eggNOGiCOG1025.
GeneTreeiENSGT00530000063327.
InParanoidiP22817.
KOiK01408.
OMAiNPAHPFS.
OrthoDBiEOG7HHWRD.
PhylomeDBiP22817.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22817-1 [UniParc]FASTAAdd to Basket

« Hide

MTIAESSQKS ATRKPDSMEP ILRLNNIEKS LQDTRDYRGL QLENGLKVLL    50
ISDPNTDVSA AALSVQVGHM SDPTNLPGLA HFCEHMLFLG TEKYPHENGY 100
TTYLSQSGGS SNAATYPLMT KYHFHVAPDK LDGALDRFAQ FFIAPLFTPS 150
ATEREINAVN SEHEKNLPSD LWRIKQVNRH LAKPDHAYSK FGSGNKTTLS 200
EIPKSKNIDV RDELLKFHKQ WYSANIMCLA VIGKESLDEL EGMVLEKFSE 250
IENKNVKVPG WPRHPYAEER YGQKVKIVPI KDIRSLTISF TTDDLTQFYK 300
SGPDNYLTHL IGHEGKGSIL SELRRLGWCN DLMAGHQNTQ NGFGFFDIVV 350
DLTQEGLEHV DDIVKIVFQY LEMLRKEGPK KWIFDECVKL NEMRFRFKEK 400
EQPENLVTHA VSSMQIFPLE EVLIAPYLSN EWRPDLIKGL LDELVPSKSR 450
IVIVSQSFEP DCDLAEPYYK TKYGITRVAK DTVQSWENCE LNENLKLALP 500
NSFIPTNFDI SDVPADAPKH PTIILDTPIL RVWHKQDNQF NKPKACMTFD 550
MSNPIAYLDP LNCNLNHMMV MLLKDQLNEY LYDAELASLK LSVMGKSCGI 600
DFTIRGFSDK QVVLLEKLLD HLFDFSIDEK RFDILKEEYV RSLKNFKAEQ 650
PYQHSIYYLA LLLTENAWAN MELLDAMELV TYDRVLNFAK EFFQRLHTEC 700
FIFGNVTKQQ ATDIAGRVNT RLEATNASKL PILARQMLKK REYKLLAGDS 750
YLFEKENEFH KSSCAQLYLQ CGAQTDHTNI MVNLVSQVLS EPCYDCLRTK 800
EQLGYIVFSG VRKVNGANGI RIIVQSAKHP SYVEDRIENF LQTYLQVIED 850
MPLDEFERHK EALAVKKLEK PKTIFQQFSQ FYGEIAMQTY HFEREEAEVA 900
ILRKISKADF VDYFKKFIAK DGEERRVLSV HIVSQQTDEN ATSEAEPVEI 950
TNMERHKPIS DIVTFKSCKE LYPIALPFLD IKAKGARSKL 990
Length:990
Mass (Da):113,684
Last modified:January 23, 2007 - v4
Checksum:i32D19736CB497DCB
GO

Sequence cautioni

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → V in AAA28439. 1 Publication
Sequence conflicti178 – 1781N → D in AAO74689. 1 Publication
Sequence conflicti384 – 3841F → L in AAA28439. 1 Publication
Sequence conflicti402 – 4032QP → ES in AAA28439. 1 Publication
Sequence conflicti415 – 4151Q → K in AAA28439. 1 Publication
Sequence conflicti433 – 4331R → S in AAA28439. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA37254. SNFFIN.
RefSeqiNP_524182.3. NM_079458.4.
UniGeneiDm.36730.

Genome annotation databases

EnsemblMetazoaiFBtr0273273; FBpp0271781; FBgn0001247.
GeneIDi40248.
KEGGidme:Dmel_CG5517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi A37254. SNFFIN.
RefSeqi NP_524182.3. NM_079458.4.
UniGenei Dm.36730.

3D structure databases

ProteinModelPortali P22817.
SMRi P22817. Positions 25-977.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M16.002.

Proteomic databases

PaxDbi P22817.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0273273 ; FBpp0271781 ; FBgn0001247 .
GeneIDi 40248.
KEGGi dme:Dmel_CG5517.

Organism-specific databases

CTDi 3416.
FlyBasei FBgn0001247. Ide.

Phylogenomic databases

eggNOGi COG1025.
GeneTreei ENSGT00530000063327.
InParanoidi P22817.
KOi K01408.
OMAi NPAHPFS.
OrthoDBi EOG7HHWRD.
PhylomeDBi P22817.

Enzyme and pathway databases

SignaLinki P22817.

Miscellaneous databases

ChiTaRSi IDE. drosophila.
GenomeRNAii 40248.
NextBioi 817784.
PROi P22817.

Gene expression databases

Bgeei P22817.

Family and domain databases

Gene3Di 3.30.830.10. 4 hits.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view ]
Pfami PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view ]
SUPFAMi SSF63411. SSF63411. 4 hits.
PROSITEi PS00143. INSULINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. 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.

Entry informationi

Entry nameiIDE_DROME
AccessioniPrimary (citable) accession number: P22817
Secondary accession number(s): B9EQR9
, Q86MR2, Q95S06, Q9VPG8
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi