E13A_ARATH
ID E13A_ARATH Reviewed; 339 AA.
AC P33157; Q8LD94; Q9M2M1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase;
DE Short=(1->3)-beta-glucanase;
DE AltName: Full=Beta-1,3-endoglucanase;
DE AltName: Full=Beta-1,3-glucanase 2 {ECO:0000303|PubMed:1824335};
DE Short=AtBG2 {ECO:0000303|PubMed:23656331};
DE AltName: Full=Pathogenesis-related protein 2;
DE Short=PR-2;
DE Flags: Precursor;
GN Name=BG2 {ECO:0000303|PubMed:1824335}; OrderedLocusNames=At3g57260;
GN ORFNames=F28O9.110;
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], PARTIAL PROTEIN SEQUENCE, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=1392589; DOI=10.2307/3869523;
RA Uknes S., Mauch-Mani B., Moyer M., Potter S., Williams S., Dincher S.,
RA Chandler D., Slusarenko A., Ward E., Ryals J.;
RT "Acquired resistance in Arabidopsis.";
RL Plant Cell 4:645-656(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=1824335; DOI=10.2307/3869200;
RA Dong X., Mindrinos M., Davis K., Ausubel F.;
RT "Induction of Arabidopsis defense genes by virulent and avirulent
RT Pseudomonas syringae strains and by a cloned avirulence gene.";
RL Plant Cell 3:61-72(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23656331; DOI=10.1094/mpmi-03-13-0062-r;
RA Zavaliev R., Levy A., Gera A., Epel B.L.;
RT "Subcellular dynamics and role of Arabidopsis beta-1,3-glucanases in cell-
RT to-cell movement of tobamoviruses.";
RL Mol. Plant Microbe Interact. 26:1016-1030(2013).
CC -!- FUNCTION: Implicated in the defense of plants against pathogens
CC (Probable). Not involved in plasmodesmal callose degradation and in the
CC gating of plasmodesmata during tobamovirus infection (PubMed:23656331).
CC {ECO:0000269|PubMed:23656331, ECO:0000305|PubMed:1392589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23656331}. Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:23656331}. Secreted, cell wall
CC {ECO:0000269|PubMed:23656331}. Note=Exported in the apoplast and
CC secreted to the cell wall under treatment with salicylic acid (SA).
CC {ECO:0000269|PubMed:23656331}.
CC -!- INDUCTION: By 2,6-dichloroisonicotinic acid (INA) and salicylic acid
CC (possibly an endogenous signal for acquired resistance). Strongly
CC induced by infection with the bacterial pathogen P.syringae pv. tomato
CC DC3000 (PubMed:1392589). Induced by infection with avirulent and
CC virulent strains of P.syringae pv. maculicola (PubMed:1824335). Induced
CC by infection with the turnip vein clearing virus (TVCV) and cucumber
CC mosaic virus (CMV) (PubMed:23656331). {ECO:0000269|PubMed:1392589,
CC ECO:0000269|PubMed:1824335, ECO:0000269|PubMed:23656331}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32755.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA32864.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M90509; AAA32864.1; ALT_FRAME; mRNA.
DR EMBL; M58462; AAA32755.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL137080; CAB68132.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79633.1; -; Genomic_DNA.
DR EMBL; AY099668; AAM20519.1; -; mRNA.
DR EMBL; AY128847; AAM91247.1; -; mRNA.
DR EMBL; AY086134; AAM63339.1; -; mRNA.
DR PIR; JQ1694; JQ1694.
DR PIR; T45804; T45804.
DR RefSeq; NP_191285.1; NM_115586.2.
DR AlphaFoldDB; P33157; -.
DR SMR; P33157; -.
DR BioGRID; 10209; 1.
DR IntAct; P33157; 1.
DR STRING; 3702.AT3G57260.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; P33157; -.
DR PRIDE; P33157; -.
DR EnsemblPlants; AT3G57260.1; AT3G57260.1; AT3G57260.
DR GeneID; 824893; -.
DR Gramene; AT3G57260.1; AT3G57260.1; AT3G57260.
DR KEGG; ath:AT3G57260; -.
DR Araport; AT3G57260; -.
DR TAIR; locus:2082543; AT3G57260.
DR eggNOG; ENOG502QVKW; Eukaryota.
DR HOGENOM; CLU_024953_0_0_1; -.
DR InParanoid; P33157; -.
DR OMA; QNAMTYV; -.
DR PhylomeDB; P33157; -.
DR BioCyc; ARA:AT3G57260-MON; -.
DR PRO; PR:P33157; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P33157; baseline and differential.
DR Genevisible; P33157; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008810; F:cellulase activity; TAS:TAIR.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; ISS:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Direct protein sequencing; Endoplasmic reticulum;
KW Glycosidase; Hydrolase; Pathogenesis-related protein; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..339
FT /note="Glucan endo-1,3-beta-glucosidase, acidic isoform"
FT /id="PRO_0000011882"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CONFLICT 27
FT /note="H -> P (in Ref. 2; AAA32755 and 6; AAM63339)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> P (in Ref. 6; AAM63339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37339 MW; 3B145DB01733BD22 CRC64;
MSESRSLASP PMLMILLSLV IASFFNHTAG QIGVCYGMLG DTLPSPSDVV ALYKQQNIQR
MRLYGPDPGA LAALRGSDIE LILDVPSSDL ERLASSQTEA DKWVQENVQS YRDGVRFRYI
NVGNEVKPSV GGFLLQAMQN IENAVSGAGL EVKVSTAIAT DTTTDTSPPS QGRFRDEYKS
FLEPVIGFLA SKQSPLLVNL YPYFSYMGDT ANIHLDYALF TAQSTVDNDP GYSYQNLFDA
NLDSVYAALE KSGGGSLEIV VSETGWPTEG AVGTSVENAK TYVNNLIQHV KNGSPRRPGK
AIETYIFAMF DENKKEPTYE KFWGLFHPDR QSKYEVNFN
