ID   E13D_HORVU              Reviewed;         327 AA.
AC   Q02437;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase GIV;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase GIV;
DE   AltName: Full=(1->3)-beta-glucanase isoenzyme GIV;
DE   AltName: Full=Beta-1,3-endoglucanase GIV;
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 [GENOMIC DNA].
RC   STRAIN=cv. Clipper, and cv. NK 1558; TISSUE=Seedling;
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: Vacuole {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Aleurone layer of germinated grain.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M96940; AAA32961.1; -; Genomic_DNA.
DR   PIR; JC1437; JC1437.
DR   AlphaFoldDB; Q02437; -.
DR   SMR; Q02437; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   ExpressionAtlas; Q02437; baseline and differential.
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; Vacuole.
FT   CHAIN           1..327
FT                   /note="Glucan endo-1,3-beta-glucosidase GIV"
FT                   /id="PRO_0000205274"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   327 AA;  35034 MW;  C5002AC7AB830E85 CRC64;
     IGVCYGIIAN NLPPRREVVQ LYRSKGITNM RIYSVQPQAI RALHGSGIRL MLGTTNNDVA
     VLAGSLSAAT SWVHANVKPY HSAGVTIRYI AVGNEITGGA AQSILAAMRN LNKALAAARL
     GGIKVSTAVR FDVITNSFPP SSAVFAQPYM VDIARHLAST NAPLLANVYP YFAYSGNPRD
     IKLNYATFQP GATPVRDAGN GLIYTNLFNA MVDAMYAALE KAGAPSVRVV VSESGWPSAG
     GFAATPENAR AYNQGLIDHV AHGTPKKPGH MEAYVFAMFN ENQKPGLETE RHFGLFYPNK
     RPVYHINFAG GRLAPVNHTN SHGFGGH