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P22817

- IDE_DROME

UniProt

P22817 - IDE_DROME

Protein

Insulin-degrading enzyme

Gene

Ide

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    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.

    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

    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