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Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta-glucanase) (Beta-1,3-endoglucanase) [Cleaved into: Glucan endo-1,3-beta-glucosidase minor form 3; Glucan endo-1,3-beta-glucosidase minor form 2; Glucan endo-1,3-beta-glucosidase minor form 1; Glucan endo-1,3-beta-glucosidase major form]

 E13B_HEVBR              Reviewed;         374 AA.
P52407;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
25-OCT-2017, entry version 89.
RecName: Full=Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform;
EC=3.2.1.39;
AltName: Full=(1->3)-beta-glucan endohydrolase;
Short=(1->3)-beta-glucanase;
AltName: Full=Beta-1,3-endoglucanase;
Contains:
RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 3;
Contains:
RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 2;
Contains:
RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 1;
Contains:
RecName: Full=Glucan endo-1,3-beta-glucosidase major form;
Flags: Precursor;
Name=HGN1;
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae;
Crotonoideae; Micrandreae; Hevea.
NCBI_TaxID=3981;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. RRIM 600; TISSUE=Latex;
PubMed=7579190; DOI=10.1007/BF00043663;
Chye M.-L., Cheung K.-Y.;
"Beta-1,3-glucanase is highly-expressed in laticifers of Hevea
brasiliensis.";
Plant Mol. Biol. 29:397-402(1995).
[2]
PROTEIN SEQUENCE OF 45-64 AND 323-352.
STRAIN=cv. RRIM 600; TISSUE=Latex;
PubMed=8987504; DOI=10.1016/0031-9422(96)00196-3;
Subroto T., van Koningsveld G.A., Schreuder H.A.,
Soedjanaatmadja U.M.S., Beintema J.J.;
"Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea
latex.";
Phytochemistry 43:29-37(1996).
[3]
PROTEIN SEQUENCE OF 323-356, GLYCOSYLATION, PROTEOLYTIC PROCESSING OF
C-TERMINUS, AND VARIANTS ASP-342 AND GLY-352.
STRAIN=cv. GT.1, cv. PR 261, and cv. RRIM 600;
Subroto T., de Vries H., Schuringa J.J., Soedjanaatmadja U.M.S.,
Hofsteenge J., Jekel P.A., Beintema J.J.;
"Enzymic and structural studies on processed proteins from the
vacuolar (lutoid-body) fraction of latex of Hevea brasiliensis.";
Plant Physiol. Biochem. 39:1047-1055(2001).
[4]
SUBUNIT.
STRAIN=cv. RRIM 600;
Churngchow N., Suntaro A., Wititsuwannnakul R.;
"Beta-1,3-glucanase isozymes from the latex of Hevea brasiliensis.";
Phytochemistry 39:505-509(1995).
-!- FUNCTION: Is thought to be an important plant defense-related
product against fungal pathogens.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->3)-beta-D-glucosidic
linkages in (1->3)-beta-D-glucans.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 4.5-5.0. The enzyme from cv. GT.1 displays a
second optimum pH at 6.7.;
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.4}.
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed at highest levels in laticifer cells
of the petiole. {ECO:0000269|PubMed:7579190}.
-!- PTM: Glycosylated in cv. GT.1 and cv. RRIM 600 but not in cv. PR
261. Asn-350 is glycosylated only in cv. GT.1 due to the presence
of Ser-352. In cv. PR 261 and cv. RRIM 600, Ser-352 is replaced by
Gly so Asn-350 is not glycosylated. {ECO:0000269|Ref.3}.
-!- PTM: In cv. GT.1, four different forms of the enzyme have been
detected with differently processed C-termini. In cv. PR 261 and
cv. RRIM 600, only 2 forms are detected, a major form which is
processed at residue 352 and a minor form which is processed at
residue 354. {ECO:0000269|Ref.3}.
-!- POLYMORPHISM: The enzyme from cv. GT.1 displays a 3-5 fold lower
specific activity than the enzyme from cv. PR 261.
{ECO:0000269|Ref.3}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U22147; AAA87456.1; -; mRNA.
PIR; S65077; S65077.
ProteinModelPortal; P52407; -.
SMR; P52407; -.
Allergome; 3313; Hev b 2.0101.
Allergome; 386; Hev b 2.
CAZy; GH17; Glycoside Hydrolase Family 17.
PRIDE; P52407; -.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
InterPro; IPR000490; Glyco_hydro_17.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00332; Glyco_hydro_17; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
1: Evidence at protein level;
Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
Plant defense; Polymorphism; Pyrrolidone carboxylic acid; Signal;
Vacuole.
SIGNAL 1 36 {ECO:0000255}.
CHAIN 37 356 Glucan endo-1,3-beta-glucosidase minor
form 3.
/FTId=PRO_0000011843.
CHAIN 37 355 Glucan endo-1,3-beta-glucosidase minor
form 2.
/FTId=PRO_0000011844.
CHAIN 37 354 Glucan endo-1,3-beta-glucosidase minor
form 1.
/FTId=PRO_0000011845.
CHAIN 37 352 Glucan endo-1,3-beta-glucosidase major
form.
/FTId=PRO_0000011846.
PROPEP 357 374 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000011847.
ACT_SITE 276 276 Nucleophile. {ECO:0000250}.
ACT_SITE 333 333 Proton donor. {ECO:0000250}.
MOD_RES 37 37 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P15797}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.3}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.3}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 342 342 N -> D (in strain: cv. PR 261 and cv.
RRIM 600). {ECO:0000269|Ref.3}.
VARIANT 352 352 S -> G (in strain: cv. PR 261 and cv.
RRIM 600). {ECO:0000269|Ref.3}.
CONFLICT 344 345 WQ -> RP (in Ref. 1). {ECO:0000305}.
SEQUENCE 374 AA; 41396 MW; 7468888769FE3A9D CRC64;
MAISSSTSGT SSSFPSRTTV MLLLFFFAAS VGITDAQVGV CYGMQGNNLP PVSEVIALYK
KSNITRMRIY DPNRAVLEAL RGSNIELILG VPNSDLQSLT NPSNAKSWVQ KNVRGFWSSV
LFRYIAVGNE ISPVNRGTAW LAQFVLPAMR NIHDAIRSAG LQDQIKVSTA IDLTLVGNSY
PPSAGAFRDD VRSYLDPIIG FLSSIRSPLL ANIYPYFTYA YNPRDISLPY ALFTSPSVVV
WDGQRGYKNL FDATLDALYS ALERASGGSL EVVVSESGWP SAGAFAATFD NGRTYLSNLI
QHVKGGTPKR PNRAIETYLF AMFDENKKQP EVEKHFGLFF PNKWQKYNLN FSAEKNWDIS
TEHNATILFL KSDM


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