E13C_MUSAC
ID E13C_MUSAC Reviewed; 340 AA.
AC O22317; A7U7Q7; D8UYM8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase {ECO:0000305};
DE EC=3.2.1.39 {ECO:0000269|PubMed:10672030};
DE AltName: Full=Beta-1,3-glucanase {ECO:0000303|PubMed:10672030};
DE AltName: Allergen=Mus a 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=BANGLUC {ECO:0000305};
OS Musa acuminata (Banana) (Musa cavendishii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=4641;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Grand nain; TISSUE=Fruit flesh;
RX PubMed=9342866; DOI=10.1104/pp.115.2.463;
RA Clendennen S.K., May G.D.;
RT "Differential gene expression in ripening banana fruit.";
RL Plant Physiol. 115:463-469(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Fruit flesh;
RX PubMed=20467747; DOI=10.1007/s00299-010-0866-0;
RA Roy Choudhury S., Roy S., Singh S.K., Sengupta D.N.;
RT "Molecular characterization and differential expression of beta-1,3-
RT glucanase during ripening in banana fruit in response to ethylene, auxin,
RT ABA, wounding, cold and light-dark cycles.";
RL Plant Cell Rep. 29:813-828(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-340, PROTEIN SEQUENCE OF 29-40,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND ALLERGEN.
RX PubMed=22162266; DOI=10.1002/mnfr.201100541;
RA Aleksic I., Popovic M., Dimitrijevic R., Andjelkovic U., Vassilopoulou E.,
RA Sinaniotis A., Atanaskovic-Markovic M., Lindner B., Petersen A.,
RA Papadopoulos N.G., Gavrovic-Jankulovic M.;
RT "Molecular and immunological characterization of Mus a 5 allergen from
RT banana fruit.";
RL Mol. Nutr. Food Res. 56:446-453(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10672030; DOI=10.1046/j.1432-1327.2000.01117.x;
RA Peumans W.J., Barre A., Derycke V., Rouge P., Zhang W., May G.D.,
RA Delcour J.A., Van Leuven F., Van Damme E.J.;
RT "Purification, characterization and structural analysis of an abundant
RT beta-1,3-glucanase from banana fruit.";
RL Eur. J. Biochem. 267:1188-1195(2000).
RN [5]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24198217; DOI=10.1007/s12033-013-9719-8;
RA Mrkic I., Abughren M., Nikolic J., Andjelkovic U., Vassilopoulou E.,
RA Sinaniotis A., Petersen A., Papadopoulos N.G., Gavrovic-Jankulovic M.;
RT "Molecular characterization of recombinant mus a 5 allergen from banana
RT fruit.";
RL Mol. Biotechnol. 56:498-506(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 29-340, FUNCTION, AND ACTIVE
RP SITE.
RX PubMed=16421930; DOI=10.1002/prot.20876;
RA Receveur-Brechot V., Czjzek M., Barre A., Roussel A., Peumans W.J.,
RA Van Damme E.J., Rouge P.;
RT "Crystal structure at 1.45-A resolution of the major allergen endo-beta-
RT 1,3-glucanase of banana as a molecular basis for the latex-fruit
RT syndrome.";
RL Proteins 63:235-242(2006).
CC -!- FUNCTION: Possesses beta-1,3-endoglucanase activity in vitro
CC (PubMed:10672030). May play a role in fruit pulp softening process
CC (Probable). Can cleave beta-1,6-branched glucans in vitro
CC (PubMed:16421930). {ECO:0000269|PubMed:10672030,
CC ECO:0000269|PubMed:16421930, ECO:0000305|PubMed:10672030,
CC ECO:0000305|PubMed:20467747}.
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|PubMed:10672030};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:10672030};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22162266}.
CC -!- TISSUE SPECIFICITY: Expressed in fruit peel and pulp.
CC {ECO:0000269|PubMed:9342866}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in fruit pulp at early stages
CC of fruit ripening and then decreases in late stages (PubMed:9342866).
CC Expression increases in fruit peel and pulp during ripening (at protein
CC level) (PubMed:20467747). {ECO:0000269|PubMed:20467747,
CC ECO:0000269|PubMed:9342866}.
CC -!- INDUCTION: Induced by ethylene (PubMed:20467747). Down-regulated by
CC exposure to constant white light (PubMed:20467747).
CC {ECO:0000269|PubMed:20467747}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:22162266,
CC PubMed:24198217). Binds to IgE of patients allergic to banana fruit
CC (PubMed:22162266, PubMed:24198217). Induces basophil activation in
CC blood sample of patient allergic to banana fruit (PubMed:22162266).
CC Binds to IgE of patients allergic to rubber latex (PubMed:22162266).
CC Associated to the latex-fruit syndrome, a hypersensitivity to some
CC freshly consumed fruits developed by individuals who are allergic to
CC natural rubber latex (Probable). {ECO:0000269|PubMed:22162266,
CC ECO:0000269|PubMed:24198217, ECO:0000305|PubMed:22162266}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; AF001523; AAB82772.2; -; mRNA.
DR EMBL; EU014210; ABU40624.1; -; mRNA.
DR EMBL; GQ268963; ADG36438.1; -; mRNA.
DR PDB; 2CYG; X-ray; 1.45 A; A=29-340.
DR PDBsum; 2CYG; -.
DR AlphaFoldDB; O22317; -.
DR SMR; O22317; -.
DR Allergome; 2550; Mus a 5.
DR Allergome; 9859; Mus a 5.0101.
DR Allergome; 9860; Mus a 5.0102.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EvolutionaryTrace; O22317; -.
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 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 3D-structure; Allergen; Direct protein sequencing; Glycosidase; Hydrolase;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:22162266"
FT CHAIN 29..340
FT /note="Glucan endo-1,3-beta-glucosidase"
FT /id="PRO_5004157706"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16421930"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16421930"
FT CONFLICT 54
FT /note="N -> D (in Ref. 3; ADG36438)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..154
FT /note="LSSAGLQNQIK -> FVLGWPAKTRFR (in Ref. 2; ABU40624)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="G -> N (in Ref. 2; ABU40624)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="R -> Q (in Ref. 2; ABU40624 and 3; ADG36438)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="I -> M (in Ref. 3; ADG36438)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2CYG"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:2CYG"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:2CYG"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2CYG"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:2CYG"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2CYG"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2CYG"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2CYG"
SQ SEQUENCE 340 AA; 36321 MW; 523A047BA1A02DC2 CRC64;
MATKASLSIK GFALLVSVLV AVPTRVQSIG VCYGMLGNNL PPPSEVVSLY KSNNIARMRL
YDPNQAALQA LRNSNIQVLL DVPRSDVQSL ASNPSAAGDW IRRNVVAYWP SVSFRYIAVG
NELIPGSDLA QYILPAMRNI YNALSSAGLQ NQIKVSTAVD TGVLGTSYPP SAGAFSSAAQ
AYLSPIVQFL ASNGAPLLVN VYPYFSYTGN PGQISLPYAL FTASGVVVQD GRFSYQNLFD
AIVDAVFAAL ERVGGANVAV VVSESGWPSA GGGAEASTSN ARTYNQNLIR HVGGGTPRRP
GKEIEAYIFE MFNENQKAGG IEQNFGLFYP NKQPVYQISF
