ID   E13E_HORVU              Reviewed;         316 AA.
AC   Q02438;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase GV;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase GV;
DE   AltName: Full=(1->3)-beta-glucanase isoenzyme GV;
DE   AltName: Full=Beta-1,3-endoglucanase GV;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Clipper; TISSUE=Leaf, and Root;
RX   PubMed=8034043; DOI=10.1016/0014-5793(94)00610-5;
RA   Xu P., Harvey A.J., Fincher G.B.;
RT   "Heterologous expression of cDNAs encoding barley (Hordeum vulgare)
RT   (1-->3)-beta-glucanase isoenzyme GV.";
RL   FEBS Lett. 348:206-210(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-316.
RC   STRAIN=cv. Clipper; TISSUE=Leaf, and Root;
RX   PubMed=1398132; DOI=10.1016/0378-1119(92)90089-8;
RA   Xu P., Wang J., Fincher G.B.;
RT   "Evolution and differential expression of the (1-->3)-beta-glucan
RT   endohydrolase-encoding gene family in barley, Hordeum vulgare.";
RL   Gene 120:157-165(1992).
CC   -!- FUNCTION: May provide a degree of protection against microbial invasion
CC       of germinated barley grain through its ability to degrade fungal cell
CC       wall polysaccharides.
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: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M96939; AAA21564.1; -; mRNA.
DR   PIR; S46237; S46237.
DR   AlphaFoldDB; Q02438; -.
DR   SMR; Q02438; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   ExpressionAtlas; Q02438; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; 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   Cytoplasm; Glycosidase; Hydrolase; Plant defense.
FT   CHAIN           1..316
FT                   /note="Glucan endo-1,3-beta-glucosidase GV"
FT                   /id="PRO_0000205275"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   316 AA;  34414 MW;  0CC0AA9D48269B4F CRC64;
     MGAVHGVCYG MVGDNLPSRS DVVQLYKSRN IHAMRIYNPD QEALTALRGS GIFLILDVGG
     VDEVRRLGRD PSYAAGWVRS NVQAYYPDVL IRYIAVGNEV PAGDTGIILL AMQNVHNALA
     SANLSSSIKV STAVRFDVIT NSFPPSSGVF RDPSGLVPIA RFLDSTGAPF LANVYPYFAY
     RDDRGQNIRL NYATLQPGTT VRDNGNGLTY TSLFDAMVDS IYAALEKAGT PNVRVVVSES
     GWPSAGGFGA SVENARNYNQ GLIDHIRSGT PKRPGAIETY IFAMFNENRK PGDEVERNFG
     LFFPNKQPVY PTTFPN