ID   E132_SOLTU              Reviewed;         363 AA.
AC   P52401;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic isoform 2;
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;
GN   Name=GLUB2;
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   -!- TISSUE SPECIFICITY: High levels in leaves. Appreciable amounts in
CC       stems, roots, and sepals. Tubers, root tips, and all other flower
CC       organs contain very low levels of enzyme.
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; U01901; AAA18928.1; -; mRNA.
DR   PIR; S43318; S43318.
DR   RefSeq; NP_001274869.1; NM_001287940.1.
DR   AlphaFoldDB; P52401; -.
DR   SMR; P52401; -.
DR   Allergome; 2551; Sola t Glucanase.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PRIDE; P52401; -.
DR   GeneID; 102577444; -.
DR   KEGG; sot:102577444; -.
DR   InParanoid; P52401; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P52401; 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;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..340
FT                   /note="Glucan endo-1,3-beta-glucosidase, basic isoform 2"
FT                   /id="PRO_0000011862"
FT   PROPEP          341..363
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011863"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   363 AA;  39759 MW;  201A1A6A50C30DCC CRC64;
     MATSQIAVIV LLGLLVATNI HITEAQLGVC YGMMGNNLPS HSEVIQLYKS RNIGRLRLYD
     PNQGALNALR GSNIEVILGL PNVDVKHIAS GMEHARWWVQ KNVKDFWPDV KIKYIAVGNE
     ISPVTGTSSL TSFQVPALVN IYKAVGEAGL GNDIKVSTSV DMTLIGNSYP PSQGSFRNDV
     RWFTDPIVGF LRDTRAPLLV NIYPYFSYSG NPGQISLPYA LFTAPNVVVQ DGSRQYRNLF
     DAMLDSVYAA MERTGGGSVG IVVSECGWPS AGAFGATQDN AATYLRNLIQ HAKEGSPRKP
     GPIETYIFAM FDENNKNPEL EKHFGLFSPN KQPKYNLNFG VSERVWDISA ETNSTASSLI
     SEM