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

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811ZincPROSITE-ProRule annotation
Active sitei84 – 841Proton acceptorPROSITE-ProRule annotation
Metal bindingi85 – 851ZincPROSITE-ProRule annotation
Metal bindingi162 – 1621ZincPROSITE-ProRule annotation

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

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

        10         20         30         40         50
MTIAESSQKS ATRKPDSMEP ILRLNNIEKS LQDTRDYRGL QLENGLKVLL
60 70 80 90 100
ISDPNTDVSA AALSVQVGHM SDPTNLPGLA HFCEHMLFLG TEKYPHENGY
110 120 130 140 150
TTYLSQSGGS SNAATYPLMT KYHFHVAPDK LDGALDRFAQ FFIAPLFTPS
160 170 180 190 200
ATEREINAVN SEHEKNLPSD LWRIKQVNRH LAKPDHAYSK FGSGNKTTLS
210 220 230 240 250
EIPKSKNIDV RDELLKFHKQ WYSANIMCLA VIGKESLDEL EGMVLEKFSE
260 270 280 290 300
IENKNVKVPG WPRHPYAEER YGQKVKIVPI KDIRSLTISF TTDDLTQFYK
310 320 330 340 350
SGPDNYLTHL IGHEGKGSIL SELRRLGWCN DLMAGHQNTQ NGFGFFDIVV
360 370 380 390 400
DLTQEGLEHV DDIVKIVFQY LEMLRKEGPK KWIFDECVKL NEMRFRFKEK
410 420 430 440 450
EQPENLVTHA VSSMQIFPLE EVLIAPYLSN EWRPDLIKGL LDELVPSKSR
460 470 480 490 500
IVIVSQSFEP DCDLAEPYYK TKYGITRVAK DTVQSWENCE LNENLKLALP
510 520 530 540 550
NSFIPTNFDI SDVPADAPKH PTIILDTPIL RVWHKQDNQF NKPKACMTFD
560 570 580 590 600
MSNPIAYLDP LNCNLNHMMV MLLKDQLNEY LYDAELASLK LSVMGKSCGI
610 620 630 640 650
DFTIRGFSDK QVVLLEKLLD HLFDFSIDEK RFDILKEEYV RSLKNFKAEQ
660 670 680 690 700
PYQHSIYYLA LLLTENAWAN MELLDAMELV TYDRVLNFAK EFFQRLHTEC
710 720 730 740 750
FIFGNVTKQQ ATDIAGRVNT RLEATNASKL PILARQMLKK REYKLLAGDS
760 770 780 790 800
YLFEKENEFH KSSCAQLYLQ CGAQTDHTNI MVNLVSQVLS EPCYDCLRTK
810 820 830 840 850
EQLGYIVFSG VRKVNGANGI RIIVQSAKHP SYVEDRIENF LQTYLQVIED
860 870 880 890 900
MPLDEFERHK EALAVKKLEK PKTIFQQFSQ FYGEIAMQTY HFEREEAEVA
910 920 930 940 950
ILRKISKADF VDYFKKFIAK DGEERRVLSV HIVSQQTDEN ATSEAEPVEI
960 970 980 990
TNMERHKPIS DIVTFKSCKE LYPIALPFLD IKAKGARSKL
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → V in AAA28439. (PubMed:2126597)Curated
Sequence conflicti178 – 1781N → D in AAO74689. 1 PublicationCurated
Sequence conflicti384 – 3841F → L in AAA28439. (PubMed:2126597)Curated
Sequence conflicti402 – 4032QP → ES in AAA28439. (PubMed:2126597)Curated
Sequence conflicti415 – 4151Q → K in AAA28439. (PubMed:2126597)Curated
Sequence conflicti433 – 4331R → S in AAA28439. (PubMed:2126597)Curated

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: October 1, 2014
This is version 113 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