BGL22_ARATH
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 03-AUG-2022, entry version 132.
DE RecName: Full=Beta-glucosidase 22;
DE Short=AtBGLU22;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU22; OrderedLocusNames=At1g66280; ORFNames=T27F4.3;
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}.
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; 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.AT1G66280.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; Q9C8Y9; -.
DR MetOSite; Q9C8Y9; -.
DR PaxDb; Q9C8Y9; -.
DR PRIDE; Q9C8Y9; -.
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; locus:2201502; AT1G66280.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9C8Y9; -.
DR OMA; ERCSGHN; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9C8Y9; -.
DR BioCyc; ARA:AT1G66280-MON; -.
DR BRENDA; 3.2.1.21; 399.
DR PRO; PR:Q9C8Y9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8Y9; baseline and differential.
DR Genevisible; Q9C8Y9; 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: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 GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
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 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"
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 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
