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   27-MAR-2024, entry version 142.
DE   RecName: Full=Beta-glucosidase 21 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU21 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:19965874};
DE   AltName: Full=Protein PHOSPHATE STARVATION-RESPONSE 3.2 {ECO:0000303|PubMed:9177312};
DE   Flags: Precursor;
GN   Name=BGLU21 {ECO:0000303|PubMed:15604686};
GN   Synonyms=PSR3.2 {ECO:0000303|PubMed:9177312};
GN   OrderedLocusNames=At1g66270 {ECO:0000312|Araport:AT1G66270};
GN   ORFNames=T27F4.2 {ECO:0000312|EMBL:AAG52157.1}, T6J19.2
GN   {ECO:0000312|EMBL:AAG51761.1};
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.Q9C525; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9C525; 2 sites, No reported glycans.
DR   MetOSite; Q9C525; -.
DR   PaxDb; 3702-AT1G66270-1; -.
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; AT1G66270; BGLU21.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9C525; -.
DR   OMA; IDAYHTV; -.
DR   OrthoDB; 637975at2759; -.
DR   PhylomeDB; Q9C525; -.
DR   BioCyc; ARA:AT1G66270-MONOMER; -.
DR   BRENDA; 3.2.1.21; 399.
DR   PRO; PR:Q9C525; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C525; baseline and differential.
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:0006970; P:response to osmotic stress; IEP:TAIR.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF235; BETA-GLUCOSIDASE 21-RELATED; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q9C525; AT.
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|UniProtKB:Q7XSK0"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         55
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         158
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         203..204
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         346
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         418
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         468
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         475..476
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         484
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        223..230
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//