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Q9SR37 (BGL23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucosidase 23

Short name=AtBGLU23
EC=3.2.1.21
Alternative name(s):
Protein PHOSPHATE STARVATION-RESPONSE 3.1
Gene names
Name:BGLU23
Synonyms:PSR3.1, PYK10
Ordered Locus Names:At3g09260
ORF Names:F3L24.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May possess beta-D-glucosidase and 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. Ref.9 Ref.11 Ref.12

Catalytic activity

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

Enzyme regulation

Activated by tissue damage. Ref.11

Subunit structure

Homodimers. Binds to the deubiquitinating enzyme AMSH3. The inactive form interacts with PBP1. Ref.11 Ref.15

Subcellular location

Endoplasmic reticulum lumen. Note: Located in ER bodies. Ref.8 Ref.9 Ref.11 Ref.12 Ref.14

Tissue specificity

Highly expressed in roots. Ref.2

Induction

By wounding and methyl jasmonate (MeJA). Ref.11

Post-translational modification

Forms interchain disulfide bonds.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Sequence caution

The sequence AAB38783.1 differs from that shown. Reason: Frameshift at positions 56 and 63.

The sequence BAD94012.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER body organization

Inferred from mutant phenotype PubMed 19906837. Source: TAIR

carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cellular response to cold

Inferred from expression pattern PubMed 19965874. Source: TAIR

negative regulation of defense response

Inferred from mutant phenotype Ref.12. Source: UniProtKB

response to osmotic stress

Inferred from expression pattern PubMed 19965874. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

response to symbiotic fungus

Inferred from mutant phenotype Ref.12. Source: TAIR

   Cellular_componentER body

Inferred from direct assay Ref.8. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066. Source: TAIR

peroxisome

Inferred from direct assay PubMed 17951448. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functionbeta-glucosidase activity

Inferred from direct assay PubMed 18467340PubMed 19965874. Source: TAIR

copper ion binding

Inferred from direct assay PubMed 16526091. Source: TAIR

fucosidase activity

Traceable author statement Ref.11. Source: TAIR

protease binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.8
Chain25 – 524500Beta-glucosidase 23
PRO_0000389585

Regions

Region475 – 4762Substrate binding By similarity
Motif521 – 5244Prevents secretion from ER Potential

Sites

Active site2031Proton donor By similarity
Active site4181Nucleophile By similarity
Binding site541Substrate By similarity
Binding site1571Substrate By similarity
Binding site2021Substrate By similarity
Binding site3461Substrate By similarity
Binding site4681Substrate By similarity

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4941N-linked (GlcNAc...) Potential
Disulfide bond222 ↔ 230 By similarity

Experimental info

Sequence conflict2081S → L in CAB50792. Ref.2
Sequence conflict2081S → L in CAA61592. Ref.2
Sequence conflict2221C → S in AAB38783. Ref.1
Sequence conflict4001S → G in BAD94012. Ref.6
Sequence conflict4591K → E in BAH20034. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9SR37 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4758EA7A9B8336E1

FASTA52459,721
        10         20         30         40         50         60 
MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT AAYQVEGAIN 

        70         80         90        100        110        120 
ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ LMKNLNTDAF RMSIAWPRIF 

       130        140        150        160        170        180 
PHGRKEKGVS QAGVQFYHDL IDELIKNGIT PFVTVFHWDT PQDLEDEYGG FLSERIVKDF 

       190        200        210        220        230        240 
REYADFVFQE YGGKVKHWIT FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY 

       250        260        270        280        290        300 
LVTHNLLISH AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG 

       310        320        330        340        350        360 
WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF SNHLEKPDPS 

       370        380        390        400        410        420 
KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS LLKYIKDKYA NPEIMIMENG 

       430        440        450        460        470        480 
YGEELGASDS VAVGTADHNR KYYLQRHLLS MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY 

       490        500        510        520 
KNRFGLYYVD FKNNLTRYEK ESGKYYKDFL SQGVRPSALK KDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1."
Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R., Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.
Plant Mol. Biol. 55:343-367(2004) [PubMed] [Europe PMC] [Abstract]
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]"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.
[13]"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.
[14]"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.
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS57621.
RefSeqNP_187537.1. NM_111760.3.
UniGeneAt.18035.
At.47576.
At.71001.

3D structure databases

ProteinModelPortalQ9SR37.
SMRQ9SR37. Positions 32-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5416. 4 interactions.
STRING3702.AT3G09260.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ9SR37.
PRIDEQ9SR37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G09260.1; AT3G09260.1; AT3G09260.
GeneID820082.
KEGGath:AT3G09260.

Organism-specific databases

TAIRAT3G09260.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ9SR37.
KOK01188.
OMALITWESK.
PhylomeDBQ9SR37.

Enzyme and pathway databases

BioCycARA:AT3G09260-MONOMER.

Gene expression databases

GenevestigatorQ9SR37.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL23_ARATH
AccessionPrimary (citable) accession number: Q9SR37
Secondary accession number(s): B9DH17 expand/collapse secondary AC list , O24433, Q42585, Q56YN0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names