ID   E13B_MAIZE              Reviewed;         335 AA.
AC   P49237;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform;
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;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Va26; TISSUE=Seedling;
RX   PubMed=7846180; DOI=10.1104/pp.106.4.1709;
RA   Wu S., Kriz A.L., Widholm J.M.;
RT   "Nucleotide sequence of a maize cDNA for a class II, acidic beta-1,3-
RT   glucanase.";
RL   Plant Physiol. 106:1709-1710(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: Secreted, extracellular space {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Accumulates in aleurone layers. Much lower levels
CC       are found in the embryo, and none in starchy endosperm.
CC   -!- INDUCTION: By pathogen infection.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M95407; AAA74320.1; -; mRNA.
DR   PIR; T02088; T02088.
DR   AlphaFoldDB; P49237; -.
DR   SMR; P49237; -.
DR   STRING; 4577.GRMZM2G065585_P01; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PRIDE; P49237; -.
DR   MaizeGDB; 25482; -.
DR   eggNOG; ENOG502QQ3M; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P49237; baseline and differential.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; 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   Glycosidase; Hydrolase; Plant defense; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..335
FT                   /note="Glucan endo-1,3-beta-glucosidase, acidic isoform"
FT                   /id="PRO_0000011854"
FT   ACT_SITE        122
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   335 AA;  34894 MW;  97F89ADF5C4FBA65 CRC64;
     MARQGVIASM HALALLLGAF AAIPTGVQSI GVCYGVNGDN LPPASDVVQL YQSNGINLLR
     IYFPDANPLN ALSGTSIGLI MDVPNTDLAS LASDPSAAAA WVQSNVQASR RSACRYIAVG
     NEVSGGDTGS ILPAMQNLNA ALANAGLGGS IKVSTAVQSD VTQGFPPSQG TFSQGYMAPS
     RQYLQSTGAP LLSNVYPYFS YVGNPAQIDL KYALFTSPGT VVQDGSNAYQ NLFDALVDTF
     VSALEENAGA GNVPVVVSES GWPSAGGDAA TAANAQTYNQ NLINHVGQGT PKRPGPIETY
     IFAMFNEDQK TGAESERHFG LFNPDKSPVY PINFS