ID   E131_SOLTU              Reviewed;         337 AA.
AC   P52400;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic isoform 1;
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=GLUB1;
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 leaves, in response to infection, elicitor, ethylene, or
CC       wounding.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; U01900; AAA88794.1; -; mRNA.
DR   PIR; S65022; S65022.
DR   AlphaFoldDB; P52400; -.
DR   SMR; P52400; -.
DR   STRING; 4113.PGSC0003DMT400090689; -.
DR   Allergome; 2551; Sola t Glucanase.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   eggNOG; ENOG502QQ3M; Eukaryota.
DR   InParanoid; P52400; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52400; 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..314
FT                   /note="Glucan endo-1,3-beta-glucosidase, basic isoform 1"
FT                   /id="PRO_0000011860"
FT   PROPEP          315..337
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011861"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   337 AA;  37022 MW;  6787E5C69528F996 CRC64;
     LGVCYGMMGN NLPSHSEVIQ LYKSRNIGRL RLYDPNHGAL NALRGSNIEV ILGLPNVDVK
     HIASGMEHAR WWVQKNVKDF WPDVKIKYIA VGNEISPVTG TSSLTSFQVP ALVNIYKAVG
     EAGLGNDIKV STSVDMTLIG NSYPPSQGSF RNDVRWFTDP IVGFLRDTRA PLLVNIYPYF
     SYSGNPGQIS LPYALFTAPN AVVQDGSRQY RNLFDAMLDS VYAAMERTGG GSVGIVVSES
     GWPSAGAFGA TQDNAATYLR NLIQHAKEGS PRKPGPIETY IFAMFDENNK NPELEKHFGL
     FSPNKQPKYN LNFGVSERVW DISAETNSTA SSLISEM