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Q9W2M2

- TREA_DROME

UniProt

Q9W2M2 - TREA_DROME

Protein

Trehalase

Gene

Treh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei193 – 1931SubstrateBy similarity
    Binding sitei237 – 2371SubstrateBy similarity
    Binding sitei341 – 3411Substrate; via carbonyl oxygenBy similarity
    Active sitei343 – 3431Proton donor/acceptorBy similarity
    Active sitei541 – 5411Proton donor/acceptorBy similarity
    Binding sitei556 – 5561SubstrateBy similarity

    GO - Molecular functioni

    1. alpha,alpha-trehalase activity Source: FlyBase
    2. trehalase activity Source: FlyBase

    GO - Biological processi

    1. trehalose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH37. Glycoside Hydrolase Family 37.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalase (EC:3.2.1.28)
    Alternative name(s):
    Alpha,alpha-trehalase
    Alpha,alpha-trehalose glucohydrolase
    Gene namesi
    Name:Treh
    ORF Names:CG9364
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0003748. Treh.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 596573TrehalasePRO_0000012058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi451 – 4511N-linked (GlcNAc...)1 Publication
    Glycosylationi516 – 5161N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9W2M2.
    PRIDEiQ9W2M2.

    Expressioni

    Gene expression databases

    BgeeiQ9W2M2.

    Interactioni

    Protein-protein interaction databases

    BioGridi69627. 26 interactions.
    DIPiDIP-23202N.
    IntActiQ9W2M2. 6 interactions.
    MINTiMINT-994217.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9W2M2.
    SMRiQ9W2M2. Positions 59-574.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 2012Substrate bindingBy similarity
    Regioni246 – 2483Substrate bindingBy similarity
    Regioni307 – 3093Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 37 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1626.
    GeneTreeiENSGT00390000006949.
    InParanoidiQ9W2M2.
    KOiK01194.
    OMAiQRSEAMY.
    OrthoDBiEOG7P02H6.
    PhylomeDBiQ9W2M2.

    Family and domain databases

    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR001661. Glyco_hydro_37.
    IPR018232. Glyco_hydro_37_CS.
    [Graphical view]
    PANTHERiPTHR23403. PTHR23403. 1 hit.
    PfamiPF01204. Trehalase. 1 hit.
    [Graphical view]
    PRINTSiPR00744. GLHYDRLASE37.
    SUPFAMiSSF48208. SSF48208. 1 hit.
    PROSITEiPS00927. TREHALASE_1. 1 hit.
    PS00928. TREHALASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform C (identifier: Q9W2M2-1) [UniParc]FASTAAdd to Basket

    Also known as: F

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFKLPTISLL LVSWSCLVAL SQAKTYSLPD LTTDYNNAIP VDEEEAQDPF    50
    ASCKIYCEGN LLHTIQTAVP KLFADSKTFV DMKLNNSPDK TLEDFNAMME 100
    AKNQTPSSED LKQFVDKYFS APGTELEKWT PTDWKENPSF LDLISDPDLK 150
    QWGVELNSIW KDLGRKMKDE VSKNPEYYSI IPVPNPVIVP GGRFIEFYYW 200
    DSYWIIRGLL YSQMFDTARG MIENFFSIVN RFGFIPNGGR VYYHGRSQPP 250
    LLTGMVKSYV DFTNDDKFAI DALDTLEHEF EFFVNNHNVT VKNHSLCVYR 300
    DSSSGPRPES YREDVETGEE FPTDEAKELH YSELKAGAES GMDFSSRWFI 350
    SPTGTNDGNR SALSTTSIVP VDLNAYLYWN AKLIAEFHSK AGNTKKVTEY 400
    ETKAEKLLLG IQEVLWNEEA GVWLDYDMIN QKPRDYYTPT NLSPLWVKAF 450
    NISESEKISA SVMAYIERNK LDSFPGGVPN TLSYTGEQWD APNVWAPMQY 500
    ILVEGLNNLN TPEAKNMSLK WATRWVKTNF AAFSKDRHMY EKYNADEFGV 550
    GGGGGEYEVQ TGFGWSNGVI IEWLSKHGRD ISIGSGCGCL AGEKRQ 596

    Note: No experimental confirmation available.

    Length:596
    Mass (Da):67,689
    Last modified:May 1, 2000 - v1
    Checksum:i600D03B2087929EC
    GO
    Isoform A (identifier: Q9W2M2-2) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MFKLPTISLLLVSWSCLVALSQAKTYSLPDLTTDYNNAIPVDEEEAQDPFASC → MASPANPSSNHKMNGNG

    Note: No experimental confirmation available.

    Show »
    Length:560
    Mass (Da):63,552
    Checksum:iAB9992F3BB522733
    GO
    Isoform B (identifier: Q9W2M2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:515
    Mass (Da):58,722
    Checksum:i1580AADE103A1E25
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform B. CuratedVSP_021831Add
    BLAST
    Alternative sequencei1 – 5353MFKLP…PFASC → MASPANPSSNHKMNGNG in isoform A. 1 PublicationVSP_007735Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF46668.1.
    AE013599 Genomic DNA. Translation: AAF46669.1.
    AE013599 Genomic DNA. Translation: AAM68192.1.
    AY051466 mRNA. Translation: AAK92890.1.
    RefSeqiNP_001261115.1. NM_001274186.1. [Q9W2M2-2]
    NP_524821.1. NM_080082.3. [Q9W2M2-2]
    NP_726023.1. NM_166421.2. [Q9W2M2-2]
    NP_726024.1. NM_166422.2. [Q9W2M2-2]
    NP_726025.1. NM_166423.3. [Q9W2M2-1]
    NP_726026.1. NM_166424.2. [Q9W2M2-1]
    NP_726027.1. NM_166425.2. [Q9W2M2-3]
    UniGeneiDm.6686.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071539; FBpp0071468; FBgn0003748. [Q9W2M2-1]
    FBtr0071540; FBpp0071469; FBgn0003748. [Q9W2M2-1]
    GeneIDi45368.
    KEGGidme:Dmel_CG9364.
    UCSCiCG9364-RA. d. melanogaster. [Q9W2M2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF46668.1 .
    AE013599 Genomic DNA. Translation: AAF46669.1 .
    AE013599 Genomic DNA. Translation: AAM68192.1 .
    AY051466 mRNA. Translation: AAK92890.1 .
    RefSeqi NP_001261115.1. NM_001274186.1. [Q9W2M2-2 ]
    NP_524821.1. NM_080082.3. [Q9W2M2-2 ]
    NP_726023.1. NM_166421.2. [Q9W2M2-2 ]
    NP_726024.1. NM_166422.2. [Q9W2M2-2 ]
    NP_726025.1. NM_166423.3. [Q9W2M2-1 ]
    NP_726026.1. NM_166424.2. [Q9W2M2-1 ]
    NP_726027.1. NM_166425.2. [Q9W2M2-3 ]
    UniGenei Dm.6686.

    3D structure databases

    ProteinModelPortali Q9W2M2.
    SMRi Q9W2M2. Positions 59-574.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69627. 26 interactions.
    DIPi DIP-23202N.
    IntActi Q9W2M2. 6 interactions.
    MINTi MINT-994217.

    Protein family/group databases

    CAZyi GH37. Glycoside Hydrolase Family 37.

    Proteomic databases

    PaxDbi Q9W2M2.
    PRIDEi Q9W2M2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071539 ; FBpp0071468 ; FBgn0003748 . [Q9W2M2-1 ]
    FBtr0071540 ; FBpp0071469 ; FBgn0003748 . [Q9W2M2-1 ]
    GeneIDi 45368.
    KEGGi dme:Dmel_CG9364.
    UCSCi CG9364-RA. d. melanogaster. [Q9W2M2-1 ]

    Organism-specific databases

    CTDi 11181.
    FlyBasei FBgn0003748. Treh.

    Phylogenomic databases

    eggNOGi COG1626.
    GeneTreei ENSGT00390000006949.
    InParanoidi Q9W2M2.
    KOi K01194.
    OMAi QRSEAMY.
    OrthoDBi EOG7P02H6.
    PhylomeDBi Q9W2M2.

    Miscellaneous databases

    GenomeRNAii 45368.
    NextBioi 838071.
    PROi Q9W2M2.

    Gene expression databases

    Bgeei Q9W2M2.

    Family and domain databases

    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR001661. Glyco_hydro_37.
    IPR018232. Glyco_hydro_37_CS.
    [Graphical view ]
    PANTHERi PTHR23403. PTHR23403. 1 hit.
    Pfami PF01204. Trehalase. 1 hit.
    [Graphical view ]
    PRINTSi PR00744. GLHYDRLASE37.
    SUPFAMi SSF48208. SSF48208. 1 hit.
    PROSITEi PS00927. TREHALASE_1. 1 hit.
    PS00928. TREHALASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Head.
    4. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
      Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
      Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-451, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Oregon-R.
      Tissue: Head.

    Entry informationi

    Entry nameiTREA_DROME
    AccessioniPrimary (citable) accession number: Q9W2M2
    Secondary accession number(s): Q0E903
    , Q0E904, Q7YWL2, Q961P0, Q9W2M1, Q9W2M3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 3, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3