BGL20_ARATH
ID BGL20_ARATH Reviewed; 535 AA.
AC Q84WV2; O49117; Q8VXW3; Q9LQS3;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Beta-glucosidase 20;
DE Short=AtBGLU20;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU20; OrderedLocusNames=At1g75940; ORFNames=T4O12.15;
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].
RX PubMed=9687065; DOI=10.1023/a:1005964431302;
RA Rubinelli P., Hu Y., Ma H.;
RT "Identification, sequence analysis and expression studies of novel anther-
RT specific genes of Arabidopsis thaliana.";
RL Plant Mol. Biol. 37:607-619(1998).
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].
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).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26759.2; Type=Erroneous gene model prediction; Note=The predicted gene At1g75930 has been split into 2 genes: At1g75930 and At1g75940.; Evidence={ECO:0000305};
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DR EMBL; AF037590; AAC39504.1; -; mRNA.
DR EMBL; AC007396; AAF26759.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35779.1; -; Genomic_DNA.
DR EMBL; AY074517; AAL67131.1; -; mRNA.
DR EMBL; BT002735; AAO22564.1; -; mRNA.
DR PIR; T52048; T52048.
DR RefSeq; NP_177722.1; NM_106244.3.
DR AlphaFoldDB; Q84WV2; -.
DR SMR; Q84WV2; -.
DR BioGRID; 29146; 1.
DR STRING; 3702.AT1G75940.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q84WV2; -.
DR PRIDE; Q84WV2; -.
DR ProteomicsDB; 240396; -.
DR EnsemblPlants; AT1G75940.1; AT1G75940.1; AT1G75940.
DR GeneID; 843927; -.
DR Gramene; AT1G75940.1; AT1G75940.1; AT1G75940.
DR KEGG; ath:AT1G75940; -.
DR Araport; AT1G75940; -.
DR TAIR; locus:2204345; AT1G75940.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q84WV2; -.
DR OMA; RAGHNSE; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q84WV2; -.
DR BioCyc; ARA:AT1G75940-MON; -.
DR PRO; PR:Q84WV2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84WV2; baseline and differential.
DR Genevisible; Q84WV2; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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: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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..535
FT /note="Beta-glucosidase 20"
FT /id="PRO_0000389582"
FT MOTIF 532..535
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..235
FT /evidence="ECO:0000250"
FT CONFLICT 362
FT /note="P -> T (in Ref. 1; AAC39504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61675 MW; C717D02DA37F1C81 CRC64;
MGRFHKFPLL GLVLFLGLTG SLIAANEYAC SSTDIHFTRA NFPKGFIFGT ATAAFQVEGA
VNEGCRGPSM WDVYTKKFPH KCNYHNADVA VDFYHRYKED IKLMKNLNTD GFRFSIAWPR
IFPHGRMEKG ISKAGVQYYH DLIDELLANG ITPLVTVFHW DTPQDLEDEY GGFLSDRIIK
DFTEYANFTF QEYGDKVKHW ITFNEPWVFS RAGYDIGNKA PGRCSKYIKE HGEMCHDGRS
GHEAYIVSHN MLLAHADAVD AFRKCDKCKG GKIGIAHSPA WFEAHELSDE EHETPVTGLI
DFILGWHLHP TTYGDYPQSM KDHIGHRLPK FTEAQKEKLK NSADFVGINY YTSVFALHDE
EPDPSQPSWQ SDSLVDWEPR YVDKFNAFAN KPDVAKVEVY AKGLRSLLKY IKDKYGNPEI
MITENGYGED LGEQDTSLVV ALSDQHRTYY IQKHLLSLHE AICDDKVNVT GYFHWSLMDN
FEWQDGYKAR FGLYYVDYKN NLTRHEKLSA QWYSSFLHDG SKEFEIEHEF EHDEL
