BGL21_ARATH
ID BGL21_ARATH Reviewed; 524 AA.
AC Q9C525; O23656; Q3ECH6;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Beta-glucosidase 21;
DE Short=AtBGLU21;
DE EC=3.2.1.21;
DE AltName: Full=Protein PHOSPHATE STARVATION-RESPONSE 3.2;
DE Flags: Precursor;
GN Name=BGLU21; Synonyms=PSR3.2; OrderedLocusNames=At1g66270;
GN ORFNames=T27F4.2, T6J19.2;
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 [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9177312; DOI=10.1023/a:1005865406382;
RA Malboobi M.A., Lefebvre D.D.;
RT "A phosphate-starvation inducible beta-glucosidase gene (psr3.2) isolated
RT from Arabidopsis thaliana is a member of a distinct subfamily of the BGA
RT family.";
RL Plant Mol. Biol. 34:57-68(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP IDENTIFICATION IN THE PYK10 COMPLEX.
RX PubMed=18467340; DOI=10.1093/pcp/pcn075;
RA Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.;
RT "Antagonistic jacalin-related lectins regulate the size of ER body-type
RT beta-glucosidase complexes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:969-980(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=19965874; DOI=10.1093/pcp/pcp174;
RA Ahn Y.O., Shimizu B., Sakata K., Gantulga D., Zhou C., Zhou Z., Bevan D.R.,
RA Esen A.;
RT "Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis.";
RL Plant Cell Physiol. 51:132-143(2010).
CC -!- FUNCTION: Beta-D-glucosidase active on scopolin >> esculin >> 4-MU-
CC glucoside > DIMBOA-glucoside. No activity with pNP-glucoside, oNP-
CC glucoside and sinigrin as substrates. {ECO:0000269|PubMed:19965874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000269|PubMed:19965874};
CC -!- ACTIVITY REGULATION: Activated upon binding to PBP1 or PBP2.
CC {ECO:0000269|PubMed:19965874}.
CC -!- SUBUNIT: Component of the PYK10 complex, at least composed of
CC PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31,
CC JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.
CC {ECO:0000269|PubMed:18467340}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C525-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C525-2; Sequence=VSP_038457;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in roots.
CC {ECO:0000269|PubMed:19965874}.
CC -!- INDUCTION: Up-regulated by cold, 2,4-D, methyl jasmonate and phosphate
CC starvation. {ECO:0000269|PubMed:19965874, ECO:0000269|PubMed:9177312}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U72155; AAB64244.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC020665; AAG52157.1; -; Genomic_DNA.
DR EMBL; AC066691; AAG51761.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34488.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34489.1; -; Genomic_DNA.
DR EMBL; AY045698; AAK74056.1; -; mRNA.
DR EMBL; BT002684; AAO11600.1; -; mRNA.
DR PIR; G96687; G96687.
DR RefSeq; NP_176801.1; NM_105298.4. [Q9C525-1]
DR RefSeq; NP_849848.1; NM_179517.2. [Q9C525-2]
DR AlphaFoldDB; Q9C525; -.
DR SMR; Q9C525; -.
DR BioGRID; 28165; 2.
DR IntAct; Q9C525; 1.
DR STRING; 3702.AT1G66270.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR MetOSite; Q9C525; -.
DR PaxDb; Q9C525; -.
DR PRIDE; Q9C525; -.
DR ProteomicsDB; 240868; -. [Q9C525-1]
DR EnsemblPlants; AT1G66270.1; AT1G66270.1; AT1G66270. [Q9C525-1]
DR EnsemblPlants; AT1G66270.2; AT1G66270.2; AT1G66270. [Q9C525-2]
DR GeneID; 842944; -.
DR Gramene; AT1G66270.1; AT1G66270.1; AT1G66270. [Q9C525-1]
DR Gramene; AT1G66270.2; AT1G66270.2; AT1G66270. [Q9C525-2]
DR KEGG; ath:AT1G66270; -.
DR Araport; AT1G66270; -.
DR TAIR; locus:2201492; AT1G66270.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9C525; -.
DR OMA; SWEPKNA; -.
DR PhylomeDB; Q9C525; -.
DR BioCyc; ARA:AT1G66270-MON; -.
DR BRENDA; 3.2.1.21; 399.
DR PRO; PR:Q9C525; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C525; baseline and differential.
DR Genevisible; Q9C525; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070417; P:cellular response to cold; IEP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:TAIR.
DR GO; GO:0009804; P:coumarin metabolic process; IDA:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..524
FT /note="Beta-glucosidase 21"
FT /id="PRO_0000389583"
FT MOTIF 521..524
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 223..230
FT /evidence="ECO:0000250"
FT VAR_SEQ 149..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038457"
SQ SEQUENCE 524 AA; 59664 MW; 8848C9751C15DFF9 CRC64;
MALQKFPLMG LLLLLTILVS VTTAVDDPVC PATSKLSRAS FPNGFLFGTA TAAFQVEGAI
NETCRGPALW DIYCRRNPER CSGDHADVAV DFFHRYKEDI QLMKNLNTDA FRLSIAWSRI
FPHGRKEKGV SQAGVQFYHE LIDELLKNGI VPFVTVFHWD TPQDLEDEYG GFLSQNIVKD
FREYADYVFT EYGGKVKNWI TFNEPWVFAH AGYDLGKKAP GRCSRYVPGC EDREGQSGKE
AYLVSHNLLN AHAEAVEVFR QKVKGGKIGI AHSPAWFEPH DLKDSNDAPT VSRVLDFMLG
WHLEPTTSGD YPQIMKDLLG YRLPQFTAAQ KAKLKDSTDF VGLNYYTSTF SNYNEKPDPS
KPSWKQDSLV SWEPKNVDHS AIGSMPLTAA LPVYAKGFRK LLKYIKDKYA NPEIMIMENG
YGDKLGTTDS VDVGTADHNR KYYLQRHLLA MNEAICIDKV RVTGYFVWSL LDNFEWQDGY
KNRFGLYYVD FKNNLTRYEK ESAKYYKDFL AQGVRPSALK RDEL
