E13B_HEVBR
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 03-AUG-2022, entry version 102.
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, an 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 CAZy; GH17; Glycoside Hydrolase Family 17.
DR PRIDE; P52407; -.
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 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 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
