Q9SE50 (BGL18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Abscisic acid signaling pathway
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW abscisic acid metabolic process Inferred from direct assay Ref.9. Source: TAIR 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 mediated 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 abscisic acid stimulus 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_component	ER 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_function	abscisic acid glucose ester beta-glucosidase activity Inferred from direct assay 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 528	502	Beta-D-glucopyranosyl abscisate beta-glucosidase		PRO_0000011766
Regions
	Region	480 – 481	2	Substrate binding By similarity
	Motif	525 – 528	4	Prevents secretion from ER Potential
Sites
	Active site	207	1	Proton donor Probable
	Active site	422	1	Nucleophile By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	206	1	Substrate By similarity
	Binding site	351	1	Substrate By similarity
	Binding site	473	1	Substrate By similarity
Amino acid modifications
	Glycosylation	189	1	N-linked (GlcNAc...) Potential
	Glycosylation	466	1	N-linked (GlcNAc...) Potential
	Glycosylation	499	1	N-linked (GlcNAc...) Potential
	Disulfide bond	226 ↔ 237		By similarity
Natural variations
	Alternative sequence	461	1	C → W in isoform 2.		VSP_041996
	Alternative sequence	462 – 528	67	Missing in isoform 2.		VSP_041997
Experimental info
	Mutagenesis	207	1	E → Q: Loss of activity towards ABA-GE. Ref.9
	Sequence conflict	134	1	S → N in AAF22295. Ref.2
	Sequence conflict	210	1	V → G in AAN60329. Ref.6
	Sequence conflict	214	1	A → V in AAN60329. Ref.6
	Sequence conflict	253	1	L → S in AAN31804. Ref.6
	Sequence conflict	266	1	N → K in CAC19786. Ref.1
	Sequence conflict	266	1	N → K in AAN60329. Ref.6
	Sequence conflict	365	1	S → N in CAC19786. Ref.1
	Sequence conflict	431	1	E → G in BAD94819. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: F148D04C0A6F27B8	FASTA	528	60,459
	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
	Isoform 2 [UniParc]. Checksum: A83D86C9F943776D	FASTA	461	52,371
	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 AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ RHLLSMHDAI W

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00521974.
PIR	C96564.
RefSeq	NP_001031175.1. NM_001036098.2. NP_001185204.1. NM_001198275.1. NP_175649.1. NM_104118.2.
UniGene	At.24169.
3D structure databases
ProteinModelPortal	Q9SE50.
SMR	Q9SE50. Positions 40-515.
ModBase	Search...
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
2D gel databases
SWISS-2DPAGE	Q9SE50.
Proteomic databases
PaxDb	Q9SE50.
PRIDE	Q9SE50.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G52400.1; AT1G52400.1; AT1G52400. AT1G52400.3; AT1G52400.3; AT1G52400.
GeneID	841670.
KEGG	ath:AT1G52400.
Organism-specific databases
TAIR	At1g52400.
Phylogenomic databases
eggNOG	COG2723.
HOGENOM	HOG000088630.
InParanoid	Q9SE50.
KO	K15748.
OMA	CENHNAD.
PhylomeDB	Q9SE50.
ProtClustDB	CLSN2679726.
Enzyme and pathway databases
BioCyc	ARA:AT1G52400-MONOMER. MetaCyc:AT1G52400-MONOMER.
Gene expression databases
ArrayExpress	Q9SE50.
Genevestigator	Q9SE50.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10353. PTHR10353. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00572. GLYCOSYL_HYDROL_F1_1. False negative. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGL18_ARATH

Accession

Primary (citable) accession number: Q9SE50
Secondary accession number(s): F4ICX8 , Q56WI9, Q8H169, Q8H7A3, Q93V63, Q9FNZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program