BGL18_ARATH
ID BGL18_ARATH Reviewed; 528 AA.
AC Q9SE50; F4ICX8; Q56WI9; Q8H169; Q8H7A3; Q93V63; Q9FNZ3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Beta-D-glucopyranosyl abscisate beta-glucosidase;
DE EC=3.2.1.175;
DE AltName: Full=Beta-glucosidase 1;
DE Short=AtBG1;
DE AltName: Full=Beta-glucosidase 18;
DE Short=AtBGLU18;
DE AltName: Full=Beta-glucosidase homolog 1;
DE Flags: Precursor;
GN Name=BGLU18; Synonyms=BG1, BGL1; OrderedLocusNames=At1g52400;
GN ORFNames=F19K6.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=11080278; DOI=10.1104/pp.124.3.1007;
RA Stotz H.U., Pittendrigh B.R., Kroymann J., Weniger K., Fritsche J.,
RA Bauke A., Mitchell-Olds T.;
RT "Induced plant defense responses against chewing insects. Ethylene
RT signaling reduces resistance of Arabidopsis against Egyptian cotton worm
RT but not diamondback moth.";
RL Plant Physiol. 124:1007-1018(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Piao H.L., Hwang I.;
RT "A transgenic Arabidopsis plant overexpressing an ER localized b-
RT glucosidase homolog that is transcriptionally suppressed by NaCl is
RT hypersensitive to NaCl stress.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-308.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-528 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-207.
RX PubMed=16990135; DOI=10.1016/j.cell.2006.07.034;
RA Lee K.H., Piao H.L., Kim H.-Y., Choi S.M., Jiang F., Hartung W., Hwang I.,
RA Kwak J.M., Lee I.-J., Hwang I.;
RT "Activation of glucosidase via stress-induced polymerization rapidly
RT increases active pools of abscisic acid.";
RL Cell 126:1109-1120(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17923167; DOI=10.1016/j.jplph.2007.04.005;
RA Kato-Noguchi H., Tanaka Y.;
RT "Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-
RT glucosidase in Arabidopsis thaliana.";
RL J. Plant Physiol. 165:788-790(2008).
RN [12]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19147648; DOI=10.1093/pcp/pcp007;
RA Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N.,
RA Hara-Nishimura I., Nishimura M.;
RT "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate
RT distinct beta-glucosidases.";
RL Plant Cell Physiol. 50:480-488(2009).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION BY WOUNDING.
RX PubMed=19847124; DOI=10.4161/psb.4.9.9377;
RA Yamada K., Nagano A.J., Ogasawara K., Hara-Nishimura I., Nishimura M.;
RT "The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for
RT its formation and accumulates specific beta-glucosidases.";
RL Plant Signal. Behav. 4:849-852(2009).
CC -!- FUNCTION: Hydrolyzes abscisic acid glucose ester (ABA-GE) which
CC represents the predominant form of conjugated ABA (biologically
CC inactive). No activity with beta-D-glucopyranosyl zeatin. The
CC hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA
CC and contributes to increase its cellular levels under dehydration
CC conditions. ABA-GE hydrolyzing activity is enhanced by dehydration
CC stress-induced polymerization into higher molecular weight forms. The
CC ABA produced by BGLU18 contributes to the initiation of intracellular
CC signaling as well as the increase in the extracellular ABA level.
CC {ECO:0000269|PubMed:16990135, ECO:0000269|PubMed:17923167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-abscisic acid D-glucopyranosyl ester + H2O = 2-cis-(+)-
CC abscisate + beta-D-glucose + H(+); Xref=Rhea:RHEA:31347,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:37569, ChEBI:CHEBI:62436; EC=3.2.1.175;
CC Evidence={ECO:0000269|PubMed:17923167};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for ABA-beta-D-glucopyranosyl ester
CC {ECO:0000269|PubMed:17923167};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:17923167};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:19147648,
CC ECO:0000269|PubMed:19847124}. Note=Located in ER bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SE50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SE50-2; Sequence=VSP_041996, VSP_041997;
CC -!- TISSUE SPECIFICITY: Seeds and hydathodes of rosette and cauline leaves.
CC {ECO:0000269|PubMed:16990135}.
CC -!- INDUCTION: By ABA, dehydration, wounding and salt treatment.
CC {ECO:0000269|PubMed:16990135, ECO:0000269|PubMed:19147648,
CC ECO:0000269|PubMed:19847124}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth, yellow leaf, defective stomatal
CC closure in the dark, increased transpirational water loss, sensitive
CC response to dehydration, lower germination efficiency and decreased ABA
CC levels. {ECO:0000269|PubMed:16990135}.
CC -!- MISCELLANEOUS: Polymerization into higher molecular weight forms
CC displays diurnal fluctuation, similar to the ABA level.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94819.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251301; CAC19786.1; -; mRNA.
DR EMBL; AF183827; AAF22295.1; -; mRNA.
DR EMBL; AC037424; AAG51546.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32799.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32800.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32801.1; -; Genomic_DNA.
DR EMBL; AY039855; AAK63959.1; -; mRNA.
DR EMBL; AY056415; AAL08271.1; -; mRNA.
DR EMBL; BT000515; AAN18084.1; -; mRNA.
DR EMBL; BT000657; AAN31804.1; -; mRNA.
DR EMBL; AF083771; AAN60329.1; -; mRNA.
DR EMBL; AK222051; BAD94819.1; ALT_INIT; mRNA.
DR PIR; C96564; C96564.
DR RefSeq; NP_001031175.1; NM_001036098.2. [Q9SE50-2]
DR RefSeq; NP_001185204.1; NM_001198275.1. [Q9SE50-1]
DR RefSeq; NP_175649.1; NM_104118.3. [Q9SE50-1]
DR AlphaFoldDB; Q9SE50; -.
DR SMR; Q9SE50; -.
DR BioGRID; 26895; 3.
DR STRING; 3702.AT1G52400.3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR MetOSite; Q9SE50; -.
DR SWISS-2DPAGE; Q9SE50; -.
DR PaxDb; Q9SE50; -.
DR PRIDE; Q9SE50; -.
DR ProteomicsDB; 240728; -. [Q9SE50-1]
DR EnsemblPlants; AT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
DR EnsemblPlants; AT1G52400.2; AT1G52400.2; AT1G52400. [Q9SE50-2]
DR EnsemblPlants; AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
DR GeneID; 841670; -.
DR Gramene; AT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
DR Gramene; AT1G52400.2; AT1G52400.2; AT1G52400. [Q9SE50-2]
DR Gramene; AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
DR KEGG; ath:AT1G52400; -.
DR Araport; AT1G52400; -.
DR TAIR; locus:2018179; AT1G52400.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9SE50; -.
DR OMA; LVAHMMF; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9SE50; -.
DR BioCyc; ARA:AT1G52400-MON; -.
DR BioCyc; MetaCyc:AT1G52400-MON; -.
DR BRENDA; 3.2.1.175; 399.
DR PRO; PR:Q9SE50; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SE50; baseline and differential.
DR Genevisible; Q9SE50; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0051993; F:abscisic acid glucose ester beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:TAIR.
DR GO; GO:0009687; P:abscisic acid metabolic process; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0080119; P:ER body organization; IMP:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..528
FT /note="Beta-D-glucopyranosyl abscisate beta-glucosidase"
FT /id="PRO_0000011766"
FT MOTIF 525..528
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 480..481
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..237
FT /evidence="ECO:0000250"
FT VAR_SEQ 461
FT /note="C -> W (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041996"
FT VAR_SEQ 462..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041997"
FT MUTAGEN 207
FT /note="E->Q: Loss of activity towards ABA-GE."
FT /evidence="ECO:0000269|PubMed:16990135"
FT CONFLICT 134
FT /note="S -> N (in Ref. 2; AAF22295)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="V -> G (in Ref. 6; AAN60329)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="A -> V (in Ref. 6; AAN60329)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="L -> S (in Ref. 6; AAN31804)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="N -> K (in Ref. 1; CAC19786 and 6; AAN60329)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="S -> N (in Ref. 1; CAC19786)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="E -> G (in Ref. 7; BAD94819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60459 MW; F148D04C0A6F27B8 CRC64;
MVRFEKVHLV LGLALVLTLV GAPTKAQGPV CGAGLPDKFS RLNFPEGFIW GTATAAFQVE
GAVNEGCRGP SMWDTFTKKF PHRCENHNAD VAVDFYHRYK EDIQLMKDLN TDAFRLSIAW
PRIFPHGRMS KGISKVGVQF YHDLIDELLK NNIIPLVTVF HWDTPQDLED EYGGFLSGRI
VQDFTEYANF TFHEYGHKVK HWITFNEPWV FSRAGYDNGK KAPGRCSPYI PGYGQHCQDG
RSGYEAYQVS HNLLLSHAYA VDAFRNCKQC AGGKIGIAHS PAWFEPQDLE HVGGSIERVL
DFILGWHLAP TTYGDYPQSM KDRVGHRLPK FTEAEKKLLK GSTDYVGMNY YTSVFAKEIS
PDPKSPSWTT DSLVDWDSKS VDGYKIGSKP FNGKLDVYSK GLRYLLKYIK DNYGDPEVII
AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ RHLLSMHDAI CKDKVNVTGY FVWSLMDNFE
WQDGYKARFG LYYIDFQNNL TRHQKVSGKW YSEFLKPQFP TSKLREEL
