BGNEM_ARATH
ID BGNEM_ARATH Reviewed; 344 AA.
AC Q8VZJ2; O23473;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase At4g16260 {ECO:0000305};
DE EC=3.2.1.39 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At4g16260 {ECO:0000312|Araport:AT4G16260};
GN ORFNames=dl4170c {ECO:0000312|EMBL:CAB10405.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [6]
RP FUNCTION, INTERACTION WITH THE 30C02 EFFECTOR PROTEIN OF THE BEET CYST
RP NEMATODE HETERODERA SCHACHTII (MICROBIAL INFECTION), AND INDUCTION.
RX PubMed=22442414; DOI=10.1093/jxb/ers058;
RA Hamamouch N., Li C., Hewezi T., Baum T.J., Mitchum M.G., Hussey R.S.,
RA Vodkin L.O., Davis E.L.;
RT "The interaction of the novel 30C02 cyst nematode effector protein with a
RT plant beta-1,3-endoglucanase may suppress host defence to promote
RT parasitism.";
RL J. Exp. Bot. 63:3683-3695(2012).
RN [7]
RP 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 be involved in plant defense against cyst nematode
CC pathogens. {ECO:0000269|PubMed:22442414}.
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 -!- SUBUNIT: (Microbial infection) Interacts with the 30C02 effector
CC protein (AC G3GD54) of the beet cyst nematode Heterodera schachtii.
CC Interaction with the 30C02 effector protein may potentially suppress
CC beta-1,3-glucanase activity and plant defense.
CC {ECO:0000269|PubMed:22442414}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Induced by infection with the Cucumber mosaic virus (CMV).
CC {ECO:0000269|PubMed:23656331}.
CC -!- INDUCTION: (Microbial infection) Specifically down-regulated by
CC Heterodera schachtii (cyst nematodes) in nematode-induced syncytia.
CC {ECO:0000269|PubMed:22442414}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64664.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB10405.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78668.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z97340; CAB10405.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL161543; CAB78668.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002687; AEE83722.1; -; Genomic_DNA.
DR EMBL; AY064130; AAL36038.1; -; mRNA.
DR EMBL; AY143867; AAN28806.1; -; mRNA.
DR EMBL; AY087106; AAM64664.1; ALT_FRAME; mRNA.
DR PIR; C71429; C71429.
DR RefSeq; NP_193361.4; NM_117722.7.
DR AlphaFoldDB; Q8VZJ2; -.
DR SMR; Q8VZJ2; -.
DR STRING; 3702.AT4G16260.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q8VZJ2; -.
DR PRIDE; Q8VZJ2; -.
DR ProteomicsDB; 241217; -.
DR EnsemblPlants; AT4G16260.1; AT4G16260.1; AT4G16260.
DR GeneID; 827320; -.
DR Gramene; AT4G16260.1; AT4G16260.1; AT4G16260.
DR KEGG; ath:AT4G16260; -.
DR Araport; AT4G16260; -.
DR TAIR; locus:2130329; AT4G16260.
DR eggNOG; ENOG502QQ3M; Eukaryota.
DR HOGENOM; CLU_024953_0_0_1; -.
DR InParanoid; Q8VZJ2; -.
DR OMA; WEVIELY; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q8VZJ2; -.
DR BioCyc; ARA:AT4G16260-MON; -.
DR PRO; PR:Q8VZJ2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZJ2; baseline and differential.
DR Genevisible; Q8VZJ2; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; 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: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:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0002215; P:defense response to nematode; IMP: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 Glycosidase; Hydrolase; Plant defense; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..344
FT /note="Probable glucan endo-1,3-beta-glucosidase At4g16260"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434700"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
SQ SEQUENCE 344 AA; 37712 MW; B96F8FD95C9DC670 CRC64;
MTTLFLLIAL FITTILNPTS GESVGVCYGM MGNNLPSQSD TIALFRQNNI RRVRLYDPNQ
AALNALRNTG IEVIIGVPNT DLRSLTNPSS ARSWLQNNVL NYYPAVSFKY IAVGNEVSPS
NGGDVVLPAM RNVYDALRGA NLQDRIKVST AIDMTLIGNS FPPSSGEFRG DVRWYIDPVI
GFLTSTNSAL LANIYPYFSY VDNPRDISLS YALFTSPSVV VWDGSRGYQN LFDALLDVVY
SAVERSGGGS LPVVVSESGW PSNGGNAASF DNARAFYTNL ASRVRENRGT PKRPGRGVET
YLFAMFDENQ KSPEIEKNFG LFFPNKQPKF PITFSAARDG TAVE
