E13K_TOBAC
ID E13K_TOBAC Reviewed; 331 AA.
AC P52398;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase, acidic isoform GL161;
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 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].
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: 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.
CC -!- TISSUE SPECIFICITY: Is expressed primarily in epidermal cell of healthy
CC plant, and following induction by ethylene, accumulates in mesophyll
CC cells.
CC -!- INDUCTION: By viral infection.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; M60464; AAA34053.1; -; mRNA.
DR PIR; T02343; T02343.
DR RefSeq; NP_001313079.1; NM_001326150.1.
DR AlphaFoldDB; P52398; -.
DR SMR; P52398; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PRIDE; P52398; -.
DR GeneID; 107825406; -.
DR KEGG; nta:107825406; -.
DR Proteomes; UP000084051; Unplaced.
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 Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..9
FT /evidence="ECO:0000255"
FT CHAIN 10..331
FT /note="Glucan endo-1,3-beta-glucosidase, acidic isoform
FT GL161"
FT /id="PRO_0000011879"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT MOD_RES 10
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P15797"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 331 AA; 36891 MW; 5F0171DE53451BBA CRC64;
MCSIQIIGAQ SIGVCYGKAA NNLPSDQDVI NLYNANGIRK LRIYYPDKNI FKALNGSNIE
IILGVPNQDL EALANSSIAN GWVQDNIRSH FPYVKFKYIS IGNKVSPTNN DQYSEFLLQA
MKNVYNALAA AGLQDMIKVS TVTYSGVLAN TYPPERSIFR EEFKSFINPI IQFLARNNLP
LLANVYPYFV HVSNTADVSL SYALFTQQGT NSAGYQNLFD AILDSMYFAV EKAGGPNVEI
IVSESGWPSE GSSAATIENA QTYYRNLINH VKSGAGTPKK PGKTIETYLF AMFDENDKIG
EITEKHFGLF SPDQRAKYQL NFNYLPIYIL R