ID   E13B_HEVBR              Reviewed;         374 AA.
AC   P52407;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform {ECO:0000305};
DE            EC=3.2.1.39 {ECO:0000269|Ref.3};
DE   AltName: Full=(1->3)-beta-glucan endohydrolase {ECO:0000305};
DE            Short=(1->3)-beta-glucanase {ECO:0000305};
DE   AltName: Full=Beta-1,3-endoglucanase {ECO:0000305};
DE   AltName: Allergen=Hev b 2 {ECO:0000303|PubMed:25700348};
DE   Contains:
DE     RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 3 {ECO:0000305|Ref.3};
DE   Contains:
DE     RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 2 {ECO:0000305|Ref.3};
DE   Contains:
DE     RecName: Full=Glucan endo-1,3-beta-glucosidase minor form 1 {ECO:0000305|Ref.3};
DE   Contains:
DE     RecName: Full=Glucan endo-1,3-beta-glucosidase major form {ECO:0000305|Ref.3};
DE   Flags: Precursor;
GN   Name=HGN1 {ECO:0000303|PubMed:7579190};
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. RRIM 600; TISSUE=Latex;
RX   PubMed=7579190; DOI=10.1007/bf00043663;
RA   Chye M.-L., Cheung K.-Y.;
RT   "Beta-1,3-glucanase is highly-expressed in laticifers of Hevea
RT   brasiliensis.";
RL   Plant Mol. Biol. 29:397-402(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 45-64 AND 323-352.
RC   STRAIN=cv. RRIM 600; TISSUE=Latex;
RX   PubMed=8987504; DOI=10.1016/0031-9422(96)00196-3;
RA   Subroto T., van Koningsveld G.A., Schreuder H.A., Soedjanaatmadja U.M.S.,
RA   Beintema J.J.;
RT   "Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea
RT   latex.";
RL   Phytochemistry 43:29-37(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 323-356, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-63 AND ASN-350,
RP   PROTEOLYTIC PROCESSING OF C-TERMINUS, AND VARIANTS ASP-342 AND GLY-352.
RC   STRAIN=cv. GT.1, cv. PR 261, and cv. RRIM 600;
RX   DOI=10.1016/S0981-9428(01)01325-0;
RA   Subroto T., de Vries H., Schuringa J.J., Soedjanaatmadja U.M.S.,
RA   Hofsteenge J., Jekel P.A., Beintema J.J.;
RT   "Enzymic and structural studies on processed proteins from the vacuolar
RT   (lutoid-body) fraction of latex of Hevea brasiliensis.";
RL   Plant Physiol. Biochem. 39:1047-1055(2001).
RN   [4]
RP   SUBUNIT.
RC   STRAIN=cv. RRIM 600;
RA   Churngchow N., Suntaro A., Wititsuwannnakul R.;
RT   "Beta-1,3-glucanase isozymes from the latex of Hevea brasiliensis.";
RL   Phytochemistry 39:505-509(1995).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND ALLERGEN.
RX   PubMed=25700348; DOI=10.1016/j.molimm.2015.01.018;
RA   Galicia C., Mendoza-Hernandez G., Rodriguez-Romero A.;
RT   "Impact of the vulcanization process on the structural characteristics and
RT   IgE recognition of two allergens, Hev b 2 and Hev b 6.02, extracted from
RT   latex surgical gloves.";
RL   Mol. Immunol. 65:250-258(2015).
CC   -!- FUNCTION: Possesses beta-1,3-endoglucanase activity in vitro
CC       (PubMed:25700348). Is thought to be an important plant defense-related
CC       product against fungal pathogens (Probable).
CC       {ECO:0000269|PubMed:25700348, ECO:0000305}.
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; Evidence={ECO:0000269|Ref.3};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5-5.0. The enzyme from cv. GT.1 displays a second
CC         optimum pH at 6.7. {ECO:0000269|Ref.3};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in laticifer cells of
CC       the petiole. {ECO:0000269|PubMed:7579190}.
CC   -!- PTM: Glycosylated in cv. GT.1 and cv. RRIM 600 but not in cv. PR 261.
CC       Asn-350 is glycosylated only in cv. GT.1 due to the presence of Ser-
CC       352. In cv. PR 261 and cv. RRIM 600, Ser-352 is replaced by Gly so Asn-
CC       350 is not glycosylated. {ECO:0000269|Ref.3}.
CC   -!- PTM: In cv. GT.1, four different forms of the enzyme have been detected
CC       with differently processed C-termini. In cv. PR 261 and cv. RRIM 600,
CC       only 2 forms are detected, a major form which is processed at residue
CC       352 and a minor form which is processed at residue 354.
CC       {ECO:0000269|Ref.3}.
CC   -!- POLYMORPHISM: The enzyme from cv. GT.1 displays a 3-5 fold lower
CC       specific activity than the enzyme from cv. PR 261. {ECO:0000269|Ref.3}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:25700348). Binds
CC       to IgE of patients allergic to rubber latex (PubMed:25700348). Binds to
CC       IgE of patients allergic to fruits (PubMed:25700348). Associated to the
CC       latex-fruit syndrome, a hypersensitivity to latex developed by
CC       individuals who are allergic to consumed fruits (Probable).
CC       {ECO:0000269|PubMed:25700348, ECO:0000305|PubMed:25700348}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; U22147; AAA87456.1; -; mRNA.
DR   PIR; S65077; S65077.
DR   AlphaFoldDB; P52407; -.
DR   SMR; P52407; -.
DR   Allergome; 3313; Hev b 2.0101.
DR   Allergome; 386; Hev b 2.
DR   GlyCosmos; P52407; 3 sites, No reported glycans.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   FunFam; 3.20.20.80:FF:000010; glucan endo-1,3-beta-glucosidase, basic; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR061911; GLYCOSYL_HYDROL_F17_CS.
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   Allergen; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Plant defense; Pyrrolidone carboxylic acid; Signal; Vacuole.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..356
FT                   /note="Glucan endo-1,3-beta-glucosidase minor form 3"
FT                   /id="PRO_0000011843"
FT   CHAIN           37..355
FT                   /note="Glucan endo-1,3-beta-glucosidase minor form 2"
FT                   /id="PRO_0000011844"
FT   CHAIN           37..354
FT                   /note="Glucan endo-1,3-beta-glucosidase minor form 1"
FT                   /id="PRO_0000011845"
FT   CHAIN           37..352
FT                   /note="Glucan endo-1,3-beta-glucosidase major form"
FT                   /id="PRO_0000011846"
FT   PROPEP          357..374
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000011847"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        276
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         37
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         342
FT                   /note="N -> D (in strain: cv. PR 261 and cv. RRIM 600)"
FT                   /evidence="ECO:0000269|Ref.3"
FT   VARIANT         352
FT                   /note="S -> G (in strain: cv. PR 261 and cv. RRIM 600)"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CONFLICT        344..345
FT                   /note="WQ -> RP (in Ref. 1; AAA87456)"
FT                   /evidence="ECO:0000305"
SQ   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
//