ID   E133_SOLTU              Reviewed;         328 AA.
AC   P52402;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic isoform 3;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase;
DE            Short=(1->3)-beta-glucanase;
DE   AltName: Full=Beta-1,3-endoglucanase;
DE   Flags: Precursor; Fragment;
GN   Name=GLUB3;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Datura; TISSUE=Leaf;
RX   PubMed=8111037; DOI=10.1007/bf00020173;
RA   Beerhues L., Kombrink E.;
RT   "Primary structure and expression of mRNAs encoding basic chitinase and
RT   1,3-beta-glucanase in potato.";
RL   Plant Mol. Biol. 24:353-367(1994).
CC   -!- FUNCTION: Is thought to be an important plant defense-related product
CC       against fungal pathogens.
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: Vacuole {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels in old segments of leaves, stems
CC       and roots.
CC   -!- INDUCTION: In response to infection, elicitor, ethylene, wounding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; U01902; AAA19111.1; -; mRNA.
DR   PIR; S65023; S65023.
DR   AlphaFoldDB; P52402; -.
DR   SMR; P52402; -.
DR   Allergome; 2551; Sola t Glucanase.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   InParanoid; P52402; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52402; baseline and differential.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   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   Glycoprotein; Glycosidase; Hydrolase; Plant defense; Reference proteome;
KW   Vacuole.
FT   CHAIN           <1..305
FT                   /note="Glucan endo-1,3-beta-glucosidase, basic isoform 3"
FT                   /id="PRO_0000011864"
FT   PROPEP          306..328
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011865"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        230
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   328 AA;  36182 MW;  F2F9266304B89454 CRC64;
     NNLPSHSEVI QLYKSRNIGR LRLYDPNHGA LNALRGSNIE VILGLPNVDV KHIASGMEHA
     RWWVQKNVKD FWPDVKIKYI AVGNEISPVT GTSSLTSFQV PALVNIYKAI GEAGLGNDIK
     VSTSVDMTLI GNSYPPSQGS FRNDVRWFTD PIVGFLRDTR APLLVNIYPY FSYSGNPGQI
     SLPYALFTAP NVVVQDGSRQ YRNLFDAMLD SVYAAMERTG GGSVGIVVSE SGWPSAGAFG
     ATQDNAATYL RNLIQHAKEG SPRKPGPIET YIFAMFDENN KNPELEKHFG LFSPNKQPKY
     NLNFGVSERV WDISAETNST TSSLISEM