BG3_ARATH
ID BG3_ARATH Reviewed; 341 AA.
AC F4J270; Q9M2M3; Q9ZRI3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase BG3 {ECO:0000305};
DE EC=3.2.1.39 {ECO:0000305};
DE AltName: Full=Beta-1,3-glucanase 3 {ECO:0000303|PubMed:1824335};
DE Short=AtBG3 {ECO:0000303|PubMed:23656331};
DE Flags: Precursor;
GN Name=BG3 {ECO:0000303|PubMed:1824335};
GN OrderedLocusNames=At3g57240 {ECO:0000312|Araport:AT3G57240};
GN ORFNames=F28O9.90 {ECO:0000312|EMBL:CAB68130.1};
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. 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 [2]
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 [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 INDUCTION.
RX PubMed=16473969; DOI=10.1105/tpc.105.038372;
RA Stein M., Dittgen J., Sanchez-Rodriguez C., Hou B.-H., Molina A.,
RA Schulze-Lefert P., Lipka V., Somerville S.;
RT "Arabidopsis PEN3/PDR8, an ATP binding cassette transporter, contributes to
RT nonhost resistance to inappropriate pathogens that enter by direct
RT penetration.";
RL Plant Cell 18:731-746(2006).
RN [5]
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: May play a role in plant defense against pathogens.
CC {ECO:0000305|PubMed:23656331}.
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; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000305|PubMed:23656331}. Secreted {ECO:0000250|UniProtKB:P33157}.
CC -!- INDUCTION: By infection with a virulent strain of P.syringae pv.
CC maculicola (PubMed:1824335). Induced by infection with the biotrophic
CC powdery mildew pathogens Golovinomyces cichoracearum and Blumeria
CC graminis (PubMed:16473969). Induced by infection with the turnip vein
CC clearing virus (TVCV) and cucumber mosaic virus (CMV)
CC (PubMed:23656331). {ECO:0000269|PubMed:16473969,
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=AAA32756.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB68130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M58464; AAA32756.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL137080; CAB68130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79631.1; -; Genomic_DNA.
DR PIR; T45802; T45802.
DR RefSeq; NP_191283.2; NM_115584.5.
DR AlphaFoldDB; F4J270; -.
DR SMR; F4J270; -.
DR STRING; 3702.AT3G57240.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; F4J270; -.
DR PRIDE; F4J270; -.
DR ProteomicsDB; 240371; -.
DR EnsemblPlants; AT3G57240.1; AT3G57240.1; AT3G57240.
DR GeneID; 824891; -.
DR Gramene; AT3G57240.1; AT3G57240.1; AT3G57240.
DR KEGG; ath:AT3G57240; -.
DR Araport; AT3G57240; -.
DR TAIR; locus:2082518; AT3G57240.
DR eggNOG; ENOG502QQ3M; Eukaryota.
DR HOGENOM; CLU_024953_0_0_1; -.
DR InParanoid; F4J270; -.
DR OMA; QNFFDAN; -.
DR OrthoDB; 966331at2759; -.
DR PRO; PR:F4J270; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J270; baseline and differential.
DR Genevisible; F4J270; 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:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..341
FT /note="Probable glucan endo-1,3-beta-glucosidase BG3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434697"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 219
FT /note="T -> I (in Ref. 1; AAA32756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37632 MW; E37686ADBCCD4FC6 CRC64;
MKMCNGSSFL ASLPLLLLLL SFILASFFDT AVGQIGVCYG RNGNNLRPAS EVVALYQQRN
IRRMRLYDPN QETLNALRGS NIELVLDVPN PDLQRLASSQ AEADTWVRNN VRNYANVTFR
YISVGNEVQP SDQAASFVLP AMQNIERAVS SLGIKVSTAI DTRGISGFPP SSGTFTPEFR
SFIAPVISFL SSKQSPLLVN NYPYFSYTGN MRDIRLDYTL FTAPSTVVND GQNQYRNLFH
AILDTVYASL EKAGGGSLEI VVSESGWPTA GGAATGVDNA RTYVNNLIQT VKNGSPRRPG
RATETYIFAM FDENSKQGPE TEKFWGLFLP NLQPKYVVNF N
