ALL9_OLEEU
ID ALL9_OLEEU Reviewed; 460 AA.
AC Q94G86;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Glucan endo-1,3-beta-D-glucosidase;
DE EC=3.2.1.39;
DE AltName: Full=Major pollen allergen Ole e 9;
DE AltName: Allergen=Ole e 9;
DE Flags: Precursor;
GN Name=OLE9;
OS Olea europaea (Common olive).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX NCBI_TaxID=4146;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 158-177; 261-270; 289-299;
RP 311-320; 333-340; 352-361 AND 368-395, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBUNIT, AND
RP GLYCOSYLATION.
RX PubMed=11373288; DOI=10.1074/jbc.m103041200;
RA Huecas S., Villalba M., Rodriguez R.;
RT "Ole e 9, a major olive pollen allergen is a 1,3-beta-glucanase. Isolation,
RT characterization, amino acid sequence, and tissue specificity.";
RL J. Biol. Chem. 276:27959-27966(2001).
RN [2]
RP DISULFIDE BOND, GLYCOSYLATION, AND ALLERGEN.
RX PubMed=12392450; DOI=10.1042/bj20020423;
RA Palomares O., Villalba M., Rodriguez R.;
RT "The C-terminal segment of the 1,3-beta-glucanase Ole e 9 from olive (Olea
RT europaea) pollen is an independent domain with allergenic activity:
RT expression in Pichia pastoris and characterization.";
RL Biochem. J. 369:593-601(2003).
RN [3]
RP FUNCTION, AND ALLERGEN.
RX PubMed=15784114; DOI=10.1111/j.1365-2222.2004.02186.x;
RA Palomares O., Villalba M., Quiralte J., Polo F., Rodriguez R.;
RT "1,3-beta-glucanases as candidates in latex-pollen-vegetable food cross-
RT reactivity.";
RL Clin. Exp. Allergy 35:345-351(2005).
RN [4]
RP LAMINARIN-BINDING.
RX PubMed=17188831; DOI=10.1016/j.biopha.2006.09.014;
RA Rodriguez R., Villalba M., Batanero E., Palomares O., Salamanca G.;
RT "Emerging pollen allergens.";
RL Biomed. Pharmacother. 61:1-7(2007).
RN [5]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT "Analysis of olive allergens.";
RL Talanta 92:1-14(2012).
RN [6]
RP STRUCTURE BY NMR OF 360-460, AND DISULFIDE BOND.
RX PubMed=18096638; DOI=10.1110/ps.073230008;
RA Trevino M.A., Palomares O., Castrillo I., Villalba M., Rodriguez R.,
RA Rico M., Santoro J., Bruix M.;
RT "Solution structure of the C-terminal domain of Ole e 9, a major allergen
RT of olive pollen.";
RL Protein Sci. 17:371-376(2008).
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:11373288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-6.0. {ECO:0000269|PubMed:11373288};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11373288}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in pollen.
CC {ECO:0000269|PubMed:11373288}.
CC -!- DOMAIN: The N-terminal region (1-350) contains the enzymatic activity
CC while the C-terminal region (360-460) can bind laminarin. Both regions
CC are allergenic by themselves.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11373288,
CC ECO:0000269|PubMed:12392450}.
CC -!- PTM: Contains two additional disulfide bonds, but it is unclear if they
CC are between the pairs Cys-392-Cys-398 and Cys-407-Cys-453
CC (PudMed:18096638) or between the pairs Cys-392-Cys-453 and Cys-398-Cys-
CC 407 (PudMed:12392450).
CC -!- ALLERGEN: Causes an allergic reaction in human. Major allergen from
CC olive pollen. Important in Mediterranean countries.
CC {ECO:0000269|PubMed:12392450, ECO:0000269|PubMed:15784114}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- CAUTION: The sequences determined for the two internal peptides of Ole
CC e 4 are identical to internal fragments of Ole e 9. However, the
CC apparent molecular weight of the two proteins is different and they are
CC still classified as two separate allergens (PubMed:22385802), even
CC though we may be facing two different isoforms of the same allergen.
CC {ECO:0000305|PubMed:22385802}.
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DR EMBL; AF249675; AAK58515.1; -; mRNA.
DR PDB; 2JON; NMR; -; A=360-460.
DR PDBsum; 2JON; -.
DR AlphaFoldDB; Q94G86; -.
DR BMRB; Q94G86; -.
DR SMR; Q94G86; -.
DR Allergome; 3391; Ole e 9.0101.
DR Allergome; 497; Ole e 9.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EvolutionaryTrace; Q94G86; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006076; P:(1->3)-beta-D-glucan catabolic process; IDA:UniProtKB.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..460
FT /note="Glucan endo-1,3-beta-D-glucosidase"
FT /id="PRO_0000421081"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 373..435
FT /evidence="ECO:0000269|PubMed:12392450,
FT ECO:0000269|PubMed:18096638"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:2JON"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:2JON"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2JON"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:2JON"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2JON"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:2JON"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:2JON"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:2JON"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2JON"
SQ SEQUENCE 460 AA; 48838 MW; 46899175F7843DFC CRC64;
MAANVQTSSL LFLVFLLLQN FYSANSQSFL GVNYGQLSDN LPSLQATVNL LKSTTIQKVR
LFGAEPAVIK AFANTGVEIV IGFDNGDIPT LASNPNVASQ FVKSNVMSFY PASNIIAITV
GNEVLTSGDQ KLISQLLPAM QNVQNALNAA SLGGKVKVST VHAMAVLSQS YPPSSGVFNP
GLGDTMKALL QFQSANDAPF MISPYPYFAY KNQPTPDTLA FCLFQPNAGQ VDSGNGHKYT
NMFDAQVDAV HSALNAMGFK DIEIVVAETG WPHGGDSNEV GPSLDNAKAY VGNLINHLKS
KVGTPLMPGK SIDTYLFSLY DEDKKTGASS EKYFGLFKPD GSTTYDVGLL KNTQNPTTPA
TPTPTPKAAG SWCVPKPGVS DDQLTGNINY ACGQGIDCGP IQPGGACFEP NTVKAHAAYV
MNLYYQSAGR NSWNCDFSQT ATLTNTNPSY GACNFPSGSN
