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Q9SE50 (BGL18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-D-glucopyranosyl abscisate beta-glucosidase

EC=3.2.1.175
Alternative name(s):
Beta-glucosidase 1
Short name=AtBG1
Beta-glucosidase 18
Short name=AtBGLU18
Beta-glucosidase homolog 1
Gene names
Name:BGLU18
Synonyms:BG1, BGL1
Ordered Locus Names:At1g52400
ORF Names:F19K6.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level. Ref.9 Ref.10

Catalytic activity

D-glucopyranosyl abscisate + H2O = D-glucose + abscisate. Ref.10

Subcellular location

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

Tissue specificity

Seeds and hydathodes of rosette and cauline leaves. Ref.9

Induction

By ABA, dehydration, wounding and salt treatment. Ref.9 Ref.11 Ref.12

Disruption phenotype

Reduced growth, yellow leaf, defective stomatal closure in the dark, increased transpirational water loss, sensitive response to dehydration, lower germination efficiency and decreased ABA levels. Ref.9

Miscellaneous

Polymerization into higher molecular weight forms displays diurnal fluctuation, similar to the ABA level.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.41 mM for ABA-beta-D-glucopyranosyl ester Ref.10

pH dependence:

Optimum pH is 6.0.

Sequence caution

The sequence BAD94819.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAbscisic acid signaling pathway
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid metabolic process

Inferred from direct assay Ref.9. Source: TAIR

abscisic acid-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response to fungus

Inferred from expression pattern PubMed 19656045. Source: TAIR

positive regulation of abscisic acid-activated signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein polymerization

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of stomatal movement

Inferred from mutant phenotype Ref.9. Source: UniProtKB

response to abiotic stimulus

Inferred from expression pattern Ref.9. Source: UniProtKB

response to abscisic acid

Inferred from expression pattern Ref.9. Source: UniProtKB

response to insect

Inferred from expression pattern PubMed 23144921. Source: TAIR

response to salt stress

Inferred from expression pattern Ref.9. Source: TAIR

response to water deprivation

Inferred from expression pattern Ref.9. Source: TAIR

water homeostasis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentER body

Inferred from direct assay Ref.11. Source: TAIR

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

endoplasmic reticulum

Inferred from direct assay Ref.9. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

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_functionabscisic acid glucose ester beta-glucosidase activity

Inferred from direct assay Ref.9. Source: TAIR

beta-glucosidase activity

Inferred from genetic interaction Ref.9. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.9. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SE50-1)

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.
Isoform 2 (identifier: Q9SE50-2)

The sequence of this isoform differs from the canonical sequence as follows:
     461-461: C → W
     462-528: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 528502Beta-D-glucopyranosyl abscisate beta-glucosidase
PRO_0000011766

Regions

Region480 – 4812Substrate binding By similarity
Motif525 – 5284Prevents secretion from ER Potential

Sites

Active site2071Proton donor Probable
Active site4221Nucleophile By similarity
Binding site581Substrate By similarity
Binding site1611Substrate By similarity
Binding site2061Substrate By similarity
Binding site3511Substrate By similarity
Binding site4731Substrate By similarity

Amino acid modifications

Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4991N-linked (GlcNAc...) Potential
Disulfide bond226 ↔ 237 By similarity

Natural variations

Alternative sequence4611C → W in isoform 2.
VSP_041996
Alternative sequence462 – 52867Missing in isoform 2.
VSP_041997

Experimental info

Mutagenesis2071E → Q: Loss of activity towards ABA-GE. Ref.9
Sequence conflict1341S → N in AAF22295. Ref.2
Sequence conflict2101V → G in AAN60329. Ref.6
Sequence conflict2141A → V in AAN60329. Ref.6
Sequence conflict2531L → S in AAN31804. Ref.6
Sequence conflict2661N → K in CAC19786. Ref.1
Sequence conflict2661N → K in AAN60329. Ref.6
Sequence conflict3651S → N in CAC19786. Ref.1
Sequence conflict4311E → G in BAD94819. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: F148D04C0A6F27B8

FASTA52860,459
        10         20         30         40         50         60 
MVRFEKVHLV LGLALVLTLV GAPTKAQGPV CGAGLPDKFS RLNFPEGFIW GTATAAFQVE 

        70         80         90        100        110        120 
GAVNEGCRGP SMWDTFTKKF PHRCENHNAD VAVDFYHRYK EDIQLMKDLN TDAFRLSIAW 

       130        140        150        160        170        180 
PRIFPHGRMS KGISKVGVQF YHDLIDELLK NNIIPLVTVF HWDTPQDLED EYGGFLSGRI 

       190        200        210        220        230        240 
VQDFTEYANF TFHEYGHKVK HWITFNEPWV FSRAGYDNGK KAPGRCSPYI PGYGQHCQDG 

       250        260        270        280        290        300 
RSGYEAYQVS HNLLLSHAYA VDAFRNCKQC AGGKIGIAHS PAWFEPQDLE HVGGSIERVL 

       310        320        330        340        350        360 
DFILGWHLAP TTYGDYPQSM KDRVGHRLPK FTEAEKKLLK GSTDYVGMNY YTSVFAKEIS 

       370        380        390        400        410        420 
PDPKSPSWTT DSLVDWDSKS VDGYKIGSKP FNGKLDVYSK GLRYLLKYIK DNYGDPEVII 

       430        440        450        460        470        480 
AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ RHLLSMHDAI CKDKVNVTGY FVWSLMDNFE 

       490        500        510        520 
WQDGYKARFG LYYIDFQNNL TRHQKVSGKW YSEFLKPQFP TSKLREEL 

« Hide

Isoform 2 [UniParc].

Checksum: A83D86C9F943776D
Show »

FASTA46152,371

References

« Hide 'large scale' references
[1]"Induced plant defense responses against chewing insects. Ethylene signaling reduces resistance of Arabidopsis against Egyptian cotton worm but not diamondback moth."
Stotz H.U., Pittendrigh B.R., Kroymann J., Weniger K., Fritsche J., Bauke A., Mitchell-Olds T.
Plant Physiol. 124:1007-1018(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Landsberg erecta.
Tissue: Rosette leaf.
[2]"A transgenic Arabidopsis plant overexpressing an ER localized b-glucosidase homolog that is transcriptionally suppressed by NaCl is hypersensitive to NaCl stress."
Piao H.L., Hwang I.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(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] (ISOFORM 1).
Strain: cv. Columbia.
[6]"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
Stracke R., Palme K.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-308.
[7]"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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-528 (ISOFORM 1).
Strain: cv. Columbia.
[8]"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.
[9]"Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid."
Lee K.H., Piao H.L., Kim H.-Y., Choi S.M., Jiang F., Hartung W., Hwang I., Kwak J.M., Lee I.-J., Hwang I.
Cell 126:1109-1120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-207.
[10]"Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-glucosidase in Arabidopsis thaliana."
Kato-Noguchi H., Tanaka Y.
J. Plant Physiol. 165:788-790(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[11]"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, INDUCTION.
[12]"The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific beta-glucosidases."
Yamada K., Nagano A.J., Ogasawara K., Hara-Nishimura I., Nishimura M.
Plant Signal. Behav. 4:849-852(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251301 mRNA. Translation: CAC19786.1.
AF183827 mRNA. Translation: AAF22295.1.
AC037424 Genomic DNA. Translation: AAG51546.1.
CP002684 Genomic DNA. Translation: AEE32799.1.
CP002684 Genomic DNA. Translation: AEE32800.1.
CP002684 Genomic DNA. Translation: AEE32801.1.
AY039855 mRNA. Translation: AAK63959.1.
AY056415 mRNA. Translation: AAL08271.1.
BT000515 mRNA. Translation: AAN18084.1.
BT000657 mRNA. Translation: AAN31804.1.
AF083771 mRNA. Translation: AAN60329.1.
AK222051 mRNA. Translation: BAD94819.1. Different initiation.
PIRC96564.
RefSeqNP_001031175.1. NM_001036098.2. [Q9SE50-2]
NP_001185204.1. NM_001198275.1. [Q9SE50-1]
NP_175649.1. NM_104118.2. [Q9SE50-1]
UniGeneAt.24169.

3D structure databases

ProteinModelPortalQ9SE50.
SMRQ9SE50. Positions 40-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26895. 1 interaction.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

2D gel databases

SWISS-2DPAGEQ9SE50.

Proteomic databases

PaxDbQ9SE50.
PRIDEQ9SE50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
GeneID841670.
KEGGath:AT1G52400.

Organism-specific databases

TAIRAT1G52400.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ9SE50.
KOK15748.
OMAHEIDAEN.
PhylomeDBQ9SE50.

Enzyme and pathway databases

BioCycARA:AT1G52400-MONOMER.
ARA:GQT-1542-MONOMER.
ARA:GQT-1543-MONOMER.
MetaCyc:AT1G52400-MONOMER.

Gene expression databases

ArrayExpressQ9SE50.
GenevestigatorQ9SE50.

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 nameBGL18_ARATH
AccessionPrimary (citable) accession number: Q9SE50
Secondary accession number(s): F4ICX8 expand/collapse secondary AC list , Q56WI9, Q8H169, Q8H7A3, Q93V63, Q9FNZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 107 of the entry and version 2 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