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Protein

Beta-glucosidase 23

Gene

BGLU23

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Beta-D-glucosidase active on scopolin > esculin >> 4-MU-glucoside >> DIMBOA-glucoside. No activity with pNP-glucoside, oNP-glucoside and sinigrin as substrates. May possess beta-D-fucosidase activity. Required for the beneficial interaction with the endophytic fungus P.indica. May participate in the control of root colonization by P.indica by repressing defense responses and modulating other responses required for a mutualistic interaction.4 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Enzyme regulationi

Activated by tissue damage and upon binding to PBP1 or PBP2.2 Publications

Kineticsi

  1. KM=0.81 mM for scopolin (with recombinant enzyme)1 Publication
  2. KM=0.73 mM for scopolin (with native enzyme)1 Publication
  3. KM=9.7 mM for esculin (with recombinant enzyme)1 Publication
  4. KM=5.8 mM for esculin (with native enzyme)1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541SubstrateBy similarity
    Binding sitei157 – 1571SubstrateBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Active sitei203 – 2031Proton donorBy similarity
    Binding sitei346 – 3461SubstrateBy similarity
    Active sitei418 – 4181NucleophileBy similarity
    Binding sitei468 – 4681SubstrateBy similarity

    GO - Molecular functioni

    • beta-glucosidase activity Source: TAIR
    • copper ion binding Source: TAIR
    • fucosidase activity Source: TAIR
    • protease binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: InterPro
    • cellular response to cold Source: TAIR
    • ER body organization Source: TAIR
    • negative regulation of defense response Source: UniProtKB
    • response to cytokinin Source: TAIR
    • response to osmotic stress Source: TAIR
    • response to salt stress Source: TAIR
    • response to symbiotic fungus Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G09260-MONOMER.
    BRENDAi3.2.1.21. 399.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 23 (EC:3.2.1.21)
    Short name:
    AtBGLU23
    Alternative name(s):
    Protein PHOSPHATE STARVATION-RESPONSE 3.1
    Gene namesi
    Name:BGLU23
    Synonyms:PSR3.1, PYK10
    Ordered Locus Names:At3g09260
    ORF Names:F3L24.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G09260.

    Subcellular locationi

    GO - Cellular componenti

    • endoplasmic reticulum Source: TAIR
    • endoplasmic reticulum lumen Source: UniProtKB-SubCell
    • ER body Source: TAIR
    • membrane Source: TAIR
    • nucleus Source: TAIR
    • peroxisome Source: TAIR
    • plasmodesma Source: TAIR
    • vacuole Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291C → Y in leb-1; loss of homodimerization resulting in fewer and larger ER bodies. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 524500Beta-glucosidase 23PRO_0000389585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi222 ↔ 230By similarity
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Forms interchain disulfide bonds.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9SR37.
    PRIDEiQ9SR37.

    Expressioni

    Tissue specificityi

    Expressed exclusively in roots.2 Publications

    Inductioni

    Up-regulated by wounding, 2,4-D and methyl jasmonate (MeJA). Down-regulated by salt and manitol.2 Publications

    Interactioni

    Subunit structurei

    Homodimers. Binds to the deubiquitinating enzyme AMSH3. The inactive form interacts with PBP1/JAL30 to form the PYK10 complex, at least composed of PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31, JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.4 Publications

    Protein-protein interaction databases

    BioGridi5416. 4 interactions.
    STRINGi3702.AT3G09260.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SR37.
    SMRiQ9SR37. Positions 35-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni475 – 4762Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi521 – 5244Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SR37.
    KOiK01188.
    OMAiIEIQFAP.
    PhylomeDBiQ9SR37.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9SR37-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT
    60 70 80 90 100
    AAYQVEGAIN ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ
    110 120 130 140 150
    LMKNLNTDAF RMSIAWPRIF PHGRKEKGVS QAGVQFYHDL IDELIKNGIT
    160 170 180 190 200
    PFVTVFHWDT PQDLEDEYGG FLSERIVKDF REYADFVFQE YGGKVKHWIT
    210 220 230 240 250
    FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY LVTHNLLISH
    260 270 280 290 300
    AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG
    310 320 330 340 350
    WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF
    360 370 380 390 400
    SNHLEKPDPS KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS
    410 420 430 440 450
    LLKYIKDKYA NPEIMIMENG YGEELGASDS VAVGTADHNR KYYLQRHLLS
    460 470 480 490 500
    MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY KNRFGLYYVD FKNNLTRYEK
    510 520
    ESGKYYKDFL SQGVRPSALK KDEL
    Length:524
    Mass (Da):59,721
    Last modified:May 1, 2000 - v1
    Checksum:i4758EA7A9B8336E1
    GO

    Sequence cautioni

    The sequence AAB38783.1 differs from that shown. Reason: Frameshift at positions 56 and 63. Curated
    The sequence BAD94012.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081S → L in CAB50792 (PubMed:11448764).Curated
    Sequence conflicti208 – 2081S → L in CAA61592 (PubMed:11448764).Curated
    Sequence conflicti222 – 2221C → S in AAB38783 (Ref. 1) Curated
    Sequence conflicti400 – 4001S → G in BAD94012 (Ref. 6) Curated
    Sequence conflicti459 – 4591K → E in BAH20034 (PubMed:19423640).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U72153 mRNA. Translation: AAB38783.1. Frameshift.
    X89413 mRNA. Translation: CAA61592.1.
    AJ243490 Genomic DNA. Translation: CAB50792.1.
    AC011436 Genomic DNA. Translation: AAF14024.1.
    CP002686 Genomic DNA. Translation: AEE74744.1.
    AF386967 mRNA. Translation: AAK62412.1.
    AY136440 mRNA. Translation: AAM97105.1.
    AY140060 mRNA. Translation: AAM98201.1.
    BT000230 mRNA. Translation: AAN15549.1.
    AK221291 mRNA. Translation: BAD94012.1. Different initiation.
    AK226844 mRNA. Translation: BAE98937.1.
    AK230345 mRNA. Translation: BAF02144.1.
    AK317362 mRNA. Translation: BAH20034.1.
    AK317443 mRNA. Translation: BAH20110.1.
    PIRiS57621.
    RefSeqiNP_187537.1. NM_111760.3.
    UniGeneiAt.18035.
    At.47576.
    At.71001.

    Genome annotation databases

    EnsemblPlantsiAT3G09260.1; AT3G09260.1; AT3G09260.
    GeneIDi820082.
    KEGGiath:AT3G09260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U72153 mRNA. Translation: AAB38783.1. Frameshift.
    X89413 mRNA. Translation: CAA61592.1.
    AJ243490 Genomic DNA. Translation: CAB50792.1.
    AC011436 Genomic DNA. Translation: AAF14024.1.
    CP002686 Genomic DNA. Translation: AEE74744.1.
    AF386967 mRNA. Translation: AAK62412.1.
    AY136440 mRNA. Translation: AAM97105.1.
    AY140060 mRNA. Translation: AAM98201.1.
    BT000230 mRNA. Translation: AAN15549.1.
    AK221291 mRNA. Translation: BAD94012.1. Different initiation.
    AK226844 mRNA. Translation: BAE98937.1.
    AK230345 mRNA. Translation: BAF02144.1.
    AK317362 mRNA. Translation: BAH20034.1.
    AK317443 mRNA. Translation: BAH20110.1.
    PIRiS57621.
    RefSeqiNP_187537.1. NM_111760.3.
    UniGeneiAt.18035.
    At.47576.
    At.71001.

    3D structure databases

    ProteinModelPortaliQ9SR37.
    SMRiQ9SR37. Positions 35-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi5416. 4 interactions.
    STRINGi3702.AT3G09260.1.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbiQ9SR37.
    PRIDEiQ9SR37.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G09260.1; AT3G09260.1; AT3G09260.
    GeneIDi820082.
    KEGGiath:AT3G09260.

    Organism-specific databases

    TAIRiAT3G09260.

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9SR37.
    KOiK01188.
    OMAiIEIQFAP.
    PhylomeDBiQ9SR37.

    Enzyme and pathway databases

    BioCyciARA:AT3G09260-MONOMER.
    BRENDAi3.2.1.21. 399.

    Miscellaneous databases

    PROiQ9SR37.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and nucleotide sequences of cDNA clones of phosphate-starvation inducible beta-glucosidase genes of Brassicaceae."
      Malboobi M.A., Tremblay L., Lefebvre D.D.
      Plant Gene Register PGR96-114
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Root.
    2. "Pyk10, a seedling and root specific gene and promoter from Arabidopsis thaliana."
      Nitz I., Berkefeld H., Puzio P.S., Grundler F.M.
      Plant Sci. 161:337-346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Strain: cv. C24.
    3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    8. "A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis."
      Matsushima R., Kondo M., Nishimura M., Hara-Nishimura I.
      Plant J. 33:493-502(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-41, SUBCELLULAR LOCATION.
    9. "NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body."
      Matsushima R., Fukao Y., Nishimura M., Hara-Nishimura I.
      Plant Cell 16:1536-1549(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: GENE FAMILY, NOMENCLATURE.
    11. "Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana."
      Nagano A.J., Matsushima R., Hara-Nishimura I.
      Plant Cell Physiol. 46:1140-1148(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, ENZYME REGULATION, SUBUNIT, DISULFIDE BOND, SUBCELLULAR LOCATION, INTERACTION WITH PBP1.
      Strain: cv. Columbia.
    12. "Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana."
      Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.
      Plant Cell Physiol. 49:969-980(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PYK10 COMPLEX.
    13. "PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and the endophytic fungus Piriformospora indica."
      Sherameti I., Venus Y., Drzewiecki C., Tripathi S., Dan V.M., Nitz I., Varma A., Grundler F.M., Oelmueller R.
      Plant J. 54:428-439(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    15. "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases."
      Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N., Hara-Nishimura I., Nishimura M.
      Plant Cell Physiol. 50:480-488(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. Cited for: MUTAGENESIS OF CYS-29, SUBUNIT.
      Strain: cv. Columbia.
    17. "The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana."
      Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.
      Plant Cell 22:1826-1837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMSH3.
    18. "Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis."
      Ahn Y.O., Shimizu B., Sakata K., Gantulga D., Zhou C., Zhou Z., Bevan D.R., Esen A.
      Plant Cell Physiol. 51:132-143(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, ENZYME REGULATION.

    Entry informationi

    Entry nameiBGL23_ARATH
    AccessioniPrimary (citable) accession number: Q9SR37
    Secondary accession number(s): B9DH17
    , O24433, Q42585, Q56YN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: May 1, 2000
    Last modified: July 22, 2015
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.