ID   E13I_TOBAC              Reviewed;         275 AA.
AC   P52396;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform PR-N;
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: Fragment;
GN   Name=PRN;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Xanthi NC; TISSUE=Leaf;
RX   PubMed=16668198; DOI=10.1104/pp.96.2.390;
RA   Ward E.R., Payne G.B., Moyer M.B., Williams S.C., Dincher S.S.,
RA   Sharkey K.C., Beck J.J., Taylor H.T., Ahl-Goy P., Meins F., Ryals J.A.;
RT   "Differential regulation of beta-1,3-glucanase messenger RNAs in response
RT   to pathogen infection.";
RL   Plant Physiol. 96:390-397(1991).
CC   -!- FUNCTION: Implicated in the defense of plants against 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.
CC   -!- INDUCTION: Not found in healthy tissues, but accumulates to high levels
CC       in the extracellular compartment of leaves in response to pathogen
CC       infection or treatment with salicylic acid.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M60462; AAA34105.1; -; mRNA.
DR   AlphaFoldDB; P52396; -.
DR   SMR; P52396; -.
DR   STRING; 4097.P52396; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 4097-P52396; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32227:SF383; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE A; 1.
DR   PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plant defense;
KW   Reference proteome; Secreted.
FT   CHAIN           <1..275
FT                   /note="Glucan endo-1,3-beta-glucosidase, acidic isoform PR-
FT                   N"
FT                   /id="PRO_0000205277"
FT   ACT_SITE        196
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   NON_TER         1
SQ   SEQUENCE   275 AA;  30386 MW;  EFD9B913A50C8FB5 CRC64;
     NVFNALRGSN IEIILDVPLQ DLQSLTDPSR ANGWVQDNII NHFPDVKFKY IAVGNKVSPG
     NNGQYAPFVA PAMQNVYNAL AAAGLQDQIK VSTATYSGIL ANTYPPKDSI FRGEFNSFIN
     PIIQFLVQHN LPLLANVYPY FGHIFNTADV PLSYALFTQQ EANPAGYQNL FDALLDSMYF
     AVEKAGGQNV EIIVSESGWP SEGNSAATIE NAQTYYENLI NHVKSGAGTP KKPGKAIETY
     LFAMFDENNK EGDITEKHFG LFSPDQRAKY QLNFN
//