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Q8WSF3

- FDL_DROME

UniProt

Q8WSF3 - FDL_DROME

Protein

Probable beta-hexosaminidase fdl

Gene

fdl

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 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Involved in brain restructurization via hormonal control during metamorphosis. Implicated in N-glycan processing.2 Publications

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.By similarity

    GO - Molecular functioni

    1. beta-N-acetylglucosaminidase activity Source: FlyBase
    2. beta-N-acetylhexosaminidase activity Source: UniProtKB

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. N-glycan processing Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-hexosaminidase fdl (EC:3.2.1.52)
    Alternative name(s):
    Protein fused lobes
    Gene namesi
    Name:fdl
    ORF Names:CG8824
    OrganismiDrosophila melanogaster (Fruit fly)Imported
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0045063. fdl.

    Subcellular locationi

    GO - Cellular componenti

    1. late endosome Source: FlyBase
    2. plasma membrane Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Sequence AnalysisAdd
    BLAST
    Chaini37 – 660624Probable beta-hexosaminidase fdlPRO_0000012017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ8WSF3.
    PRIDEiQ8WSF3.

    Expressioni

    Tissue specificityi

    In third instar larval and early pupal brains, expressed in cells sending projections across the interhemispheric junction. In adult brain, expressed in mushroom body, ellipsoid body and pars intercerebralis.1 Publication

    Gene expression databases

    BgeeiQ8WSF3.

    Interactioni

    Protein-protein interaction databases

    BioGridi75345. 4 interactions.
    DIPiDIP-21467N.
    MINTiMINT-1665363.
    STRINGi7227.FBpp0087058.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WSF3.
    SMRiQ8WSF3. Positions 177-652.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    GeneTreeiENSGT00390000008107.
    InParanoidiQ8WSF3.
    KOiK12373.
    OMAiVYKHRPW.
    OrthoDBiEOG79W94H.
    PhylomeDBiQ8WSF3.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view]
    PfamiPF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSiPR00738. GLHYDRLASE20.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform C (identifier: Q8WSF3-1) [UniParc]FASTAAdd to Basket

    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

    MSLAVSLRRA LLVLLTGAIF ILTVLYWNQG VTKAQAYNEA LERPHSHHDA    50
    SGFPIPVEKS WTYKCENDRC MRVGHHGKSA KRVSFISCSM TCGDVNIWPH 100
    PTQKFLLSSQ THSFSVEDVQ LHVDTAHREV RKQLQLAFDW FLKDLRLIQR 150
    LDYVGSSSEP TVSESSSKSR HHADLEPAAT LFGATFGVKK AGDLTSVQVK 200
    ISVLKSGDLN FSLDNDETYQ LSTQTEGHRL QVEIIANSYF GARHGLSTLQ 250
    QLIWFDDEDH LLHTYANSKV KDAPKFRYRG LMLDTSRHFF SVESIKRTIV 300
    GMGLAKMNRF HWHLTDAQSF PYISRYYPEL AVHGAYSESE TYSEQDVREV 350
    AEFAKIYGVQ VIPEIDAPAH AGNGWDWGPK RGMGELAMCI NQQPWSFYCG 400
    EPPCGQLNPK NNYTYLILQR IYEELLQHTG PTDFFHLGGD EVNLDCWAQY 450
    FNDTDLRGLW CDFMLQAMAR LKLANNGVAP KHVAVWSSAL TNTKCLPNSQ 500
    FTVQVWGGST WQENYDLLDN GYNVIFSHVD AWYLDCGFGS WRATGDAACA 550
    PYRTWQNVYK HRPWERMRLD KKRKKQVLGG EVCMWTEQVD ENQLDNRLWP 600
    RTAALAERLW TDPSDDHDMD IVPPDVFRRI SLFRNRLVEL GIRAEALFPK 650
    YCAQNPGECI 660
    Length:660
    Mass (Da):75,486
    Last modified:March 1, 2002 - v1
    Checksum:i0F14B47C9A55CD74
    GO
    Isoform B (identifier: Q8WSF3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRYVYESLRYLYKM

    Note: No experimental confirmation available.

    Show »
    Length:673
    Mass (Da):77,252
    Checksum:i7A73275BB491AE7D
    GO

    Sequence cautioni

    The sequence AAL28585.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1541V → G in AAM29423. (PubMed:12537569)Curated
    Sequence conflicti495 – 4951C → R in AAM29423. (PubMed:12537569)Curated
    Sequence conflicti551 – 5511P → Q in AAM29423. (PubMed:12537569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRYVYESLRYLYKM in isoform B. CuratedVSP_011911

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323977 mRNA. Translation: AAL55992.1.
    AE013599 Genomic DNA. Translation: AAM68691.2.
    AE013599 Genomic DNA. Translation: AAM68692.1.
    AY113418 mRNA. Translation: AAM29423.1.
    AY061037 mRNA. Translation: AAL28585.1. Different initiation.
    RefSeqiNP_725178.2. NM_165908.1. [Q8WSF3-2]
    NP_725179.1. NM_165909.2. [Q8WSF3-1]
    UniGeneiDm.3735.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087946; FBpp0087057; FBgn0045063. [Q8WSF3-1]
    GeneIDi250735.
    KEGGidme:Dmel_CG8824.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF323977 mRNA. Translation: AAL55992.1 .
    AE013599 Genomic DNA. Translation: AAM68691.2 .
    AE013599 Genomic DNA. Translation: AAM68692.1 .
    AY113418 mRNA. Translation: AAM29423.1 .
    AY061037 mRNA. Translation: AAL28585.1 . Different initiation.
    RefSeqi NP_725178.2. NM_165908.1. [Q8WSF3-2 ]
    NP_725179.1. NM_165909.2. [Q8WSF3-1 ]
    UniGenei Dm.3735.

    3D structure databases

    ProteinModelPortali Q8WSF3.
    SMRi Q8WSF3. Positions 177-652.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 75345. 4 interactions.
    DIPi DIP-21467N.
    MINTi MINT-1665363.
    STRINGi 7227.FBpp0087058.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    Proteomic databases

    PaxDbi Q8WSF3.
    PRIDEi Q8WSF3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087946 ; FBpp0087057 ; FBgn0045063 . [Q8WSF3-1 ]
    GeneIDi 250735.
    KEGGi dme:Dmel_CG8824.

    Organism-specific databases

    CTDi 250735.
    FlyBasei FBgn0045063. fdl.

    Phylogenomic databases

    eggNOGi COG3525.
    GeneTreei ENSGT00390000008107.
    InParanoidi Q8WSF3.
    KOi K12373.
    OMAi VYKHRPW.
    OrthoDBi EOG79W94H.
    PhylomeDBi Q8WSF3.

    Miscellaneous databases

    GenomeRNAii 250735.
    NextBioi 843498.

    Gene expression databases

    Bgeei Q8WSF3.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view ]
    Pfami PF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Central brain postembryonic development in Drosophila: implication of genes expressed at the interhemispheric junction."
      Boquet I., Hitier R., Dumas M., Chaminade M., Preat T.
      J. Neurobiol. 42:33-48(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM C), FUNCTION, TISSUE SPECIFICITY.
    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, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
      Strain: BerkeleyImported.
      Tissue: EmbryoImported and HeadImported.
    5. Leonard R., Altmann F.
      Submitted (APR-2003) to UniProtKB
      Cited for: FUNCTION IN N-GLYCAN PROCESSING.

    Entry informationi

    Entry nameiFDL_DROME
    AccessioniPrimary (citable) accession number: Q8WSF3
    Secondary accession number(s): Q8MZ16, Q95RY8, Q9V6C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 98 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