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   24-JAN-2024, entry version 142.
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.Q93Z08; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 3702-AT5G58090-1; -.
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; AT5G58090; -.
DR   eggNOG; ENOG502QPZ6; Eukaryota.
DR   HOGENOM; CLU_024953_2_0_1; -.
DR   InParanoid; Q93Z08; -.
DR   OMA; VACKFPN; -.
DR   OrthoDB; 651017at2759; -.
DR   PhylomeDB; Q93Z08; -.
DR   BioCyc; ARA:AT5G58090-MONOMER; -.
DR   PRO; PR:Q93Z08; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q93Z08; baseline and differential.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   Gene3D; 1.20.58.1040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF20; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE 6; 1.
DR   PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
DR   Genevisible; Q93Z08; AT.
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
//