E136_ARATH
ID E136_ARATH Reviewed; 477 AA.
AC Q93Z08; Q9FGT5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 6;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 6;
DE Short=(1->3)-beta-glucanase 6;
DE AltName: Full=Beta-1,3-endoglucanase 6;
DE Short=Beta-1,3-glucanase 6;
DE Flags: Precursor;
GN OrderedLocusNames=At5g58090; ORFNames=K21L19.12, K21L19_70;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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].
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).
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; Lipid-anchor, GPI-anchor.
CC -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; AB024029; BAB11001.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96996.1; -; Genomic_DNA.
DR EMBL; AY058864; AAL24251.1; -; mRNA.
DR EMBL; BT000612; AAN18179.1; -; mRNA.
DR RefSeq; NP_200617.2; NM_125194.4.
DR AlphaFoldDB; Q93Z08; -.
DR SMR; Q93Z08; -.
DR BioGRID; 21165; 1.
DR IntAct; Q93Z08; 1.
DR STRING; 3702.AT5G58090.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q93Z08; -.
DR PRIDE; Q93Z08; -.
DR ProteomicsDB; 221955; -.
DR EnsemblPlants; AT5G58090.1; AT5G58090.1; AT5G58090.
DR GeneID; 835921; -.
DR Gramene; AT5G58090.1; AT5G58090.1; AT5G58090.
DR KEGG; ath:AT5G58090; -.
DR Araport; AT5G58090; -.
DR TAIR; locus:2155841; AT5G58090.
DR eggNOG; ENOG502QPZ6; Eukaryota.
DR HOGENOM; CLU_024953_2_0_1; -.
DR InParanoid; Q93Z08; -.
DR OMA; VACKFPN; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q93Z08; -.
DR BioCyc; ARA:AT5G58090-MON; -.
DR PRO; PR:Q93Z08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Z08; baseline and differential.
DR Genevisible; Q93Z08; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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: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 InterPro; IPR012946; X8.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Plant defense; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..455
FT /note="Glucan endo-1,3-beta-glucosidase 6"
FT /id="PRO_0000011892"
FT PROPEP 456..477
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000011893"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 455
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 363..425
FT /evidence="ECO:0000250"
FT CONFLICT 219
FT /note="F -> L (in Ref. 3; AAL24251/AAN18179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 52211 MW; B8FE6F29218DF57C CRC64;
MGWGSVLLLL AVALLCQRAS SIGANWGTQA SHPLPPDIVV RMLRENGIQK VKLFDAEYDT
LRALGKSGIE VMVGIPNEML ATLASSLKAA EKWVAKNVST HISTDNVNIR YVAVGNEPFL
STYNGSYLST TFPALRNIQI AIIKAGLQNQ VKVTCPLNAD VYDSSTTFPS GGDFRANIRD
LMITIVKFLS ENGGPFTVNI YPYISLYTNP DFPVDYAFFD GNAQPLNDGG TFYYNMFDAN
YDTLVHALEK NGFGNMPIII GEIGWPTDGD SNANLDYAKK FNQGFMAHIS GGKGTPRRPG
PIDAYLFSLI DEDAKSVQPG YFERHWGIFT FDGLPKYALN LGTTNTGALI QAKGVRYLER
KWCVMKPNVR LDDPQVAPAV SYACSLGDCT SLGVGTSCAN LDGKQNISYA FNSYYQIQDQ
LDTACKFPNI SEVTKTDPST GTCRFPIMIE PYYGGAAREH GFFFPLLMVA AIAVSIF