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 27-MAR-2024, entry version 96. 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- RT beta-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR000490; Glyco_hydro_17. DR InterPro; IPR044965; Glyco_hydro_17_plant. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1. DR PANTHER; PTHR32227:SF459; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE, ACIDIC ISOFORM; 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 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 //