ID   BGL22_ARATH             Reviewed;         524 AA.
AC   Q9C8Y9; C0Z2N5;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Beta-glucosidase 22 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU22 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:19965874};
DE   Flags: Precursor;
GN   Name=BGLU22 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g66280 {ECO:0000312|Araport:AT1G66280};
GN   ORFNames=T27F4.3 {ECO:0000312|EMBL:AAG52159.1};
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
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. No activity with DIMBOA-glucoside, 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=Q9C8Y9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9C8Y9-2; Sequence=VSP_038458, VSP_038459;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in roots.
CC       {ECO:0000269|PubMed:19965874}.
CC   -!- INDUCTION: Up-regulated by salt, 2,4-D and methyl jasmonate. Down-
CC       regulated by cold and mannitol. {ECO:0000269|PubMed:19965874}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AC020665; AAG52159.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34490.1; -; Genomic_DNA.
DR   EMBL; AY074378; AAL67074.1; -; mRNA.
DR   EMBL; AK318849; BAH56964.1; -; mRNA.
DR   PIR; H96687; H96687.
DR   RefSeq; NP_176802.1; NM_105299.3. [Q9C8Y9-1]
DR   AlphaFoldDB; Q9C8Y9; -.
DR   SMR; Q9C8Y9; -.
DR   BioGRID; 28166; 4.
DR   IntAct; Q9C8Y9; 3.
DR   STRING; 3702.Q9C8Y9; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9C8Y9; 2 sites, No reported glycans.
DR   iPTMnet; Q9C8Y9; -.
DR   MetOSite; Q9C8Y9; -.
DR   PaxDb; 3702-AT1G66280-1; -.
DR   ProteomicsDB; 240340; -. [Q9C8Y9-1]
DR   EnsemblPlants; AT1G66280.1; AT1G66280.1; AT1G66280. [Q9C8Y9-1]
DR   GeneID; 842945; -.
DR   Gramene; AT1G66280.1; AT1G66280.1; AT1G66280. [Q9C8Y9-1]
DR   KEGG; ath:AT1G66280; -.
DR   Araport; AT1G66280; -.
DR   TAIR; AT1G66280; BGLU22.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9C8Y9; -.
DR   OMA; ERCSGHN; -.
DR   OrthoDB; 637975at2759; -.
DR   PhylomeDB; Q9C8Y9; -.
DR   BioCyc; ARA:AT1G66280-MONOMER; -.
DR   BRENDA; 3.2.1.21; 399.
DR   PRO; PR:Q9C8Y9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8Y9; 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: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:0071472; P:cellular response to salt 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; Q9C8Y9; 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 22"
FT                   /id="PRO_0000389584"
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         456
FT                   /note="C -> W (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_038458"
FT   VAR_SEQ         457..524
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_038459"
FT   CONFLICT        280
FT                   /note="H -> R (in Ref. 3; BAH56964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  59781 MW;  B05574AECFC56C41 CRC64;
     MALQKFPLLG LLFLITIVVS STIAVDDPVC PTTSKLSRAS FPNGFVFGTA TAAFQVEGAI
     NETCRGPALW DIFCKRNPER CSGHNADVAV DFFHRYKEDI QLMKNLNTDA FRLSIAWSRI
     FPHGRKEKGV SQAGVKFYHD LIDELLKNGI IPFVTVFHWD TPQDLEDEYG GFLSENIVKD
     FREYADYVFT EYGGKVKNWI TFNEPWVFAH AGYDVGKKAP GRCSRYLKGC EDRDGRSGYE
     AYLVSHNLLN AHAEAVEVFR QKVKGGKIGI AHSPAWFEPH DLKDSNDVPT VSRVLDFMLG
     WHLDPTTFGD YPQIMKDLLG HRLPKFTSSQ KAKLKDSTDF VGLNYYTSTF SNHNEKPDPS
     TPSWKQDSLV AWEPKNVDHS AIGSQPLTAA LPVYAKGFRS LLKYIKDKYA NPEIMIMENG
     YGDKLKDKDS VEVGTADYNR KYYLQRHLLA MNEAICIDKV RVTGYFVWSL LDNFEWQDGY
     NNRFGLYYVD FKNNLTRYEK ESAKYYKDFL GQGVRPSALK KDEL
//