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Q94G86 (ALL9_OLEEU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-D-glucosidase

EC=3.2.1.39
Alternative name(s):
Major pollen allergen Ole e 9
Allergen=Ole e 9
Gene names
Name:OLE9
OrganismOlea europaea (Common olive)
Taxonomic identifier4146 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesOleaceaeOleeaeOlea

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. Ref.1

Subunit structure

Homodimer. Ref.1

Subcellular location

Secreted Potential.

Tissue specificity

Expressed only in pollen. Ref.1

Domain

The N-terminal region (1-350) contains the enzymatic activity while the C-terminal region (360-460) can bind laminarin. Both regions are allergenic by themselves.

Post-translational modification

Glycosylated. Ref.1 Ref.2

Contains two additional disulfide bonds, but it is unclear if they are between the pairs Cys-392-Cys-398 and Cys-407-Cys-453 (PudMed:18096638) or between the pairs Cys-392-Cys-453 and Cys-398-Cys-407 (PudMed:12392450).

Allergenic properties

Causes an allergic reaction in human. Major allergen from olive pollen. Important in Mediterranean countries. Ref.2 Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Caution

The sequences determined for the two internal peptides of Ole e 4 are identical to internal fragments of Ole e 9. However, the apparent molecular weight of the two proteins is different and they are still classified as two separate allergens (Ref.5), even though we may be facing two different isoforms of the same allergen.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5-6.0. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 460434Glucan endo-1,3-beta-D-glucosidase
PRO_0000421081

Sites

Active site2681Nucleophile By similarity
Active site3311Proton donor By similarity

Amino acid modifications

Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Disulfide bond373 ↔ 435 Ref.2 Ref.6

Secondary structure

................. 460
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q94G86 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 46899175F7843DFC

FASTA46048,838
        10         20         30         40         50         60 
MAANVQTSSL LFLVFLLLQN FYSANSQSFL GVNYGQLSDN LPSLQATVNL LKSTTIQKVR 

        70         80         90        100        110        120 
LFGAEPAVIK AFANTGVEIV IGFDNGDIPT LASNPNVASQ FVKSNVMSFY PASNIIAITV 

       130        140        150        160        170        180 
GNEVLTSGDQ KLISQLLPAM QNVQNALNAA SLGGKVKVST VHAMAVLSQS YPPSSGVFNP 

       190        200        210        220        230        240 
GLGDTMKALL QFQSANDAPF MISPYPYFAY KNQPTPDTLA FCLFQPNAGQ VDSGNGHKYT 

       250        260        270        280        290        300 
NMFDAQVDAV HSALNAMGFK DIEIVVAETG WPHGGDSNEV GPSLDNAKAY VGNLINHLKS 

       310        320        330        340        350        360 
KVGTPLMPGK SIDTYLFSLY DEDKKTGASS EKYFGLFKPD GSTTYDVGLL KNTQNPTTPA 

       370        380        390        400        410        420 
TPTPTPKAAG SWCVPKPGVS DDQLTGNINY ACGQGIDCGP IQPGGACFEP NTVKAHAAYV 

       430        440        450        460 
MNLYYQSAGR NSWNCDFSQT ATLTNTNPSY GACNFPSGSN 

« Hide

References

[1]"Ole e 9, a major olive pollen allergen is a 1,3-beta-glucanase. Isolation, characterization, amino acid sequence, and tissue specificity."
Huecas S., Villalba M., Rodriguez R.
J. Biol. Chem. 276:27959-27966(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 158-177; 261-270; 289-299; 311-320; 333-340; 352-361 AND 368-395, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBUNIT, GLYCOSYLATION.
[2]"The C-terminal segment of the 1,3-beta-glucanase Ole e 9 from olive (Olea europaea) pollen is an independent domain with allergenic activity: expression in Pichia pastoris and characterization."
Palomares O., Villalba M., Rodriguez R.
Biochem. J. 369:593-601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND, GLYCOSYLATION, ALLERGEN.
[3]"1,3-beta-glucanases as candidates in latex-pollen-vegetable food cross-reactivity."
Palomares O., Villalba M., Quiralte J., Polo F., Rodriguez R.
Clin. Exp. Allergy 35:345-351(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALLERGEN.
[4]"Emerging pollen allergens."
Rodriguez R., Villalba M., Batanero E., Palomares O., Salamanca G.
Biomed. Pharmacother. 61:1-7(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: LAMINARIN-BINDING.
[5]"Analysis of olive allergens."
Esteve C., Montealegre C., Marina M.L., Garcia M.C.
Talanta 92:1-14(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
[6]"Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen."
Trevino M.A., Palomares O., Castrillo I., Villalba M., Rodriguez R., Rico M., Santoro J., Bruix M.
Protein Sci. 17:371-376(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 360-460, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF249675 mRNA. Translation: AAK58515.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JONNMR-A360-460[»]
ProteinModelPortalQ94G86.
SMRQ94G86. Positions 360-460.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3391. Ole e 9.0101.
497. Ole e 9.
CAZyCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ94G86.

Entry information

Entry nameALL9_OLEEU
AccessionPrimary (citable) accession number: Q94G86
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries