E1310_ARATH
ID E1310_ARATH Reviewed; 425 AA.
AC Q9FHX5; Q3E8I9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 10;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 10;
DE Short=(1->3)-beta-glucanase 10;
DE AltName: Full=Beta-1,3-endoglucanase 10;
DE Short=Beta-1,3-glucanase 10;
DE AltName: Full=Putative plasmodesmal associated protein {ECO:0000303|PubMed:17270015};
DE Short=AtBG_ppap {ECO:0000303|PubMed:17270015};
DE Flags: Precursor;
GN OrderedLocusNames=At5g42100; ORFNames=MJC20.21;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 1).
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17270015; DOI=10.1111/j.1365-313x.2006.02986.x;
RA Levy A., Erlanger M., Rosenthal M., Epel B.L.;
RT "A plasmodesmata-associated beta-1,3-glucanase in Arabidopsis.";
RL Plant J. 49:669-682(2007).
RN [6]
RP FUNCTION, 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: Plasmodesmal-associated membrane beta-1,3-glucanase involved
CC in plasmodesmal callose degradation and functions in the gating of
CC plasmodesmata. {ECO:0000269|PubMed:17270015,
CC ECO:0000269|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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17270015};
CC Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side
CC {ECO:0000255}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:17270015}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FHX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FHX5-2; Sequence=VSP_020752;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques.
CC {ECO:0000269|PubMed:17270015}.
CC -!- INDUCTION: By infection with the cucumber mosaic virus (CMV).
CC {ECO:0000269|PubMed:23656331}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; AB017067; BAB08443.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94767.1; -; Genomic_DNA.
DR EMBL; BT008863; AAP68302.1; -; mRNA.
DR EMBL; AY054690; AAK96881.1; -; mRNA.
DR EMBL; AY084866; AAM61429.1; -; mRNA.
DR RefSeq; NP_199025.1; NM_123575.4. [Q9FHX5-1]
DR AlphaFoldDB; Q9FHX5; -.
DR SMR; Q9FHX5; -.
DR STRING; 3702.AT5G42100.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9FHX5; -.
DR EnsemblPlants; AT5G42100.1; AT5G42100.1; AT5G42100. [Q9FHX5-1]
DR GeneID; 834215; -.
DR Gramene; AT5G42100.1; AT5G42100.1; AT5G42100. [Q9FHX5-1]
DR KEGG; ath:AT5G42100; -.
DR Araport; AT5G42100; -.
DR TAIR; locus:2165705; AT5G42100.
DR eggNOG; ENOG502SHG9; Eukaryota.
DR HOGENOM; CLU_024953_1_2_1; -.
DR InParanoid; Q9FHX5; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9FHX5; -.
DR BioCyc; ARA:AT5G42100-MON; -.
DR PRO; PR:Q9FHX5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHX5; baseline and differential.
DR Genevisible; Q9FHX5; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 Alternative splicing; Cell junction; Cell membrane;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Plant defense; Reference proteome;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..401
FT /note="Glucan endo-1,3-beta-glucosidase 10"
FT /id="PRO_0000251267"
FT PROPEP 402..425
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251268"
FT REGION 347..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 401
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 404..423
FT /note="GKGRFVECVLFFFLLCIIKL -> VTFSTLHFICCFTLTIFVDI (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020752"
SQ SEQUENCE 425 AA; 45358 MW; 972C1FC722408DA8 CRC64;
MASSSLQSLF SLFCLALFSL PLIVSSIGIN YGQVANNLPP PKNVIPLLKS VGATKVKLYD
ADPQALRAFA GSGFELTVAL GNEYLAQMSD PIKAQGWVKE NVQAYLPNTK IVAIVVGNEV
LTSNQSALTA ALFPAMQSIH GALVDCGLNK QIFVTTAHSL AILDVSYPPS ATSFRRDLLG
SLTPILDFHV KTGSPILINA YPFFAYEENP KHVSLDFVLF QPNQGFTDPG SNFHYDNMLF
AQVDAVYHAL DAVGISYKKV PIVVSETGWP SNGDPQEVGA TCDNARKYNG NLIKMMMSKK
MRTPIRPECD LTIFVFALFN ENMKPGPTSE RNYGLFNPDG TPVYSLGIKT SSTHSSGSGS
SNSTGGSSSG GGGNTGGSSS GGGIYQPVTG NPSPDYMSIS SAGGKGRFVE CVLFFFLLCI
IKLRL
