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Q23892

- GLUA_DICDI

UniProt

Q23892 - GLUA_DICDI

Protein

Lysosomal beta glucosidase

Gene

gluA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (20 Jan 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei363 – 3631By similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosomal beta glucosidase (EC:3.2.1.21)
    Gene namesi
    Name:gluA
    ORF Names:DDB_G0292810
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 6, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0292810. gluA.

    Subcellular locationi

    Lysosome 1 Publication

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 69451 PublicationPRO_0000361523Add
    BLAST
    Chaini70 – 821752Lysosomal beta glucosidasePRO_0000361524Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi703 – 7031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated. The polyoligosaccharides are of the high-mannose type and are highly substituted with both phosphate and sulfate moieties.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ23892.

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0215373.

    Structurei

    3D structure databases

    ProteinModelPortaliQ23892.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi461 – 4666Poly-Ala
    Compositional biasi571 – 5755Poly-Val

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1472.
    KOiK05349.
    OMAiITINETT.
    PhylomeDBiQ23892.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProiIPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q23892-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTIKSLFLL SLLIVNLLIS STYGSSIRVS IVGGEEAEVI EKPRTFGNKR    50
    ELKLEYSQIY PKKQLNQENI NFMSARDTFV DNLMSKMSIT EKIGQMTQLD 100
    ITTLTSPNTI TINETTLAYY AKTYYIGSYL NSPVSGGLAG DIHHINSSVW 150
    LDMINTIQTI VIEGSPNKIP MIYGLDSVHG ANYVHKATLF PHNTGLAATF 200
    NIEHATTAAQ ITSKDTVAVG IPWVFAPVLG IGVQPLWSRI YETFGEDPYV 250
    ASMMGAAAVR GFQGGNNSFD GPINAPSAVC TAKHYFGYSD PTSGKDRTAA 300
    WIPERMLRRY FLPSFAEAIT GAGAGTIMIN SGEVNGVPMH TSYKYLTEVL 350
    RGELQFEGVA VTDWQDIEKL VYFHHTAGSA EEAILQALDA GIDMSMVPLD 400
    LSFPIILAEM VAAGTVPESR LDLSVRRILN LKYALGLFSN PYPNPNAAIV 450
    DTIGQVQDRE AAAATAEESI TLLQNKNNIL PLNTNTIKNV LLTGPSADSI 500
    RNLNGGWSVH WQGAYEDSEF PFGTSILTGL REITNDTADF NIQYTIGHEI 550
    GVPTNQTSID EAVELAQSSD VVVVVIGELP EAETPGDIYD LSMDPNEVLL 600
    LQQLVDTGKP VVLILVEARP RILPPDLVYS CAAVLMAYLP GSEGGKPIAN 650
    ILMGNVNPSG RLPLTYPGTT GDIGVPYYHK YSENGVTTPL FQFGDGLSYT 700
    TFNYTNLACS NCKPISGQSG NYTGVLGQSY TFTVTVTNNG NVQGKDSVLL 750
    YLSDLWAQVT PEVKMLRGFQ KVDLMPAKSQ QISFTLNAYE FSFIGVDNKI 800
    TLESGQFIIM VGNQQLGLYL Q 821
    Length:821
    Mass (Da):89,344
    Last modified:January 20, 2009 - v2
    Checksum:i297758E5007DD13D
    GO

    Sequence cautioni

    The sequence AAA74233.1 differs from that shown. Reason: Frameshift at positions 393, 397, 399, 402 and 409.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti290 – 2901D → N in AAA74233. (PubMed:8288612)Curated
    Sequence conflicti474 – 4752QN → LF in AAA74233. (PubMed:8288612)Curated
    Sequence conflicti725 – 7251Missing in AAA74233. (PubMed:8288612)Curated
    Sequence conflicti737 – 7371T → TVT in AAA74233. (PubMed:8288612)Curated
    Sequence conflicti806 – 8061Q → P in AAA74233. (PubMed:8288612)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21014 mRNA. Translation: AAA74233.1. Frameshift.
    AAFI02000197 Genomic DNA. Translation: EAL60954.1.
    PIRiA49881.
    RefSeqiXP_629427.1. XM_629425.1.

    Genome annotation databases

    EnsemblProtistsiDDB0215373; DDB0215373; DDB_G0292810.
    GeneIDi8628946.
    KEGGiddi:DDB_G0292810.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21014 mRNA. Translation: AAA74233.1 . Frameshift.
    AAFI02000197 Genomic DNA. Translation: EAL60954.1 .
    PIRi A49881.
    RefSeqi XP_629427.1. XM_629425.1.

    3D structure databases

    ProteinModelPortali Q23892.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0215373.

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Proteomic databases

    PRIDEi Q23892.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0215373 ; DDB0215373 ; DDB_G0292810 .
    GeneIDi 8628946.
    KEGGi ddi:DDB_G0292810.

    Organism-specific databases

    dictyBasei DDB_G0292810. gluA.

    Phylogenomic databases

    eggNOGi COG1472.
    KOi K05349.
    OMAi ITINETT.
    PhylomeDBi Q23892.

    Miscellaneous databases

    PROi Q23892.

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProi IPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the full-length cDNA encoding the developmentally regulated lysosomal enzyme beta-glucosidase in Dictyostelium discoideum."
      Bush J., Richardson J., Cardelli J.
      J. Biol. Chem. 269:1468-1476(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-78; 74-82; 204-213 AND 583-592, DEVELOPMENTAL STAGE.
      Strain: AX3.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Structural analysis of the asparagine-linked oligosaccharides from three lysosomal enzymes of Dictyostelium discoideum. Evidence for an unusual acid-stable phosphodiester."
      Freeze H.H., Yeh R., Miller A.L., Kornfeld S.
      J. Biol. Chem. 258:14874-14879(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    4. "Lysosomal enzymes in Dictyostelium discoideum are transported to lysosomes at distinctly different rates."
      Cardelli J.A., Golumbeski G.S., Dimond R.L.
      J. Cell Biol. 102:1264-1270(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGLUA_DICDI
    AccessioniPrimary (citable) accession number: Q23892
    Secondary accession number(s): Q54CI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: January 20, 2009
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Caution

    PubMed:8288612 reports 2 different N-termini by direct protein sequencing: mature protein either starts at Ile-70 or Ser-74.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    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