Reviewed, UniProtKB/Swiss-Prot Q9SE50 (BGL18_ARATH)

Names and origin

Protein names

Recommended name:
    Beta-glucosidase 18
      Short name=AtBGLU18
    EC=3.2.1.21

Gene names

Name:	BGLU18
Synonyms:	BG1, BGL1
Ordered Locus Names:	At1g52400
ORF Names:	F19K6.15

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › 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). 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.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Subcellular location	Endoplasmic reticulum lumen. Note: Located in ER bodies.
Tissue specificity	Seeds and hydathodes of rosette and cauline leaves.
Induction	By ABA, dehydration, wounding and salt treatment.
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.
Miscellaneous	Polymerization into higher molecular weight forms displays diurnal fluctuation, similar to the ABA level.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.

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
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	ER body Ref.9 Inferred from direct assay. Source: TAIR chloroplast Inferred from direct assay. Source: TAIR endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

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.

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-glucosidase 18		PRO_0000011766
Regions
	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	206	1	Substrate By similarity
	Binding site	422	1	Substrate By similarity
	Binding site	480	1	Substrate By similarity
	Binding site	481	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
Experimental info
	Mutagenesis	207	1	E → Q: Loss of activity towards ABA-GE.
	Sequence conflict	134	1	S → N in AAF22295. Ref.2
	Sequence conflict	210	1	V → G in AAN60329. Ref.5
	Sequence conflict	214	1	A → V in AAN60329. Ref.5
	Sequence conflict	253	1	L → S in AAN31804. Ref.5
	Sequence conflict	266	1	N → K in CAC19786. Ref.1
	Sequence conflict	266	1	N → K in AAN60329. Ref.5
	Sequence conflict	365	1	S → N in CAC19786. Ref.1
	Sequence conflict	431	1	E → G in BAD94819. Ref.6

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

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: 11080278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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].
[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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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.
[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 (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-528. Strain: cv. Columbia.
[7]	"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: 15604686] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[8]	"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: 16990135] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-207.
[9]	"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: 19147648] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ251301 mRNA. Translation: CAC19786.1. AF183827 mRNA. Translation: AAF22295.1. AC037424 Genomic DNA. Translation: AAG51546.1. 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_175649.1.
UniGene	At.24169
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
2-D gel databases
SWISS-2DPAGE	Q9SE50.
Proteomic databases
PRIDE	Q9SE50.
ProMEX	Q9SE50.
Genome annotation databases
GeneID	841670.
GenomeReviews	Gene locus AT1G52400 in contig CT485782_GR.
Organism-specific databases
TAIR	At1g52400.
Gene expression databases
Genevestigator	Q9SE50.
Family and domain databases
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10353. Glyco_hydro_1. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
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): Q56WI9 , Q8H169, Q8H7A3, Q93V63, Q9FNZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 5, 2008
Last modified:	November 24, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)