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Q94G86

- ALL9_OLEEU

UniProt

Q94G86 - ALL9_OLEEU

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Protein
Glucan endo-1,3-beta-D-glucosidase
Gene
OLE9
Organism
Olea europaea (Common olive)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 4.5-6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei268 – 2681Nucleophile By similarity
Active sitei331 – 3311Proton donor By similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:OLE9
OrganismiOlea europaea (Common olive)
Taxonomic identifieri4146 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesOleaceaeOleeaeOlea

Subcellular locationi

Secreted Reviewed prediction

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

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

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3391. Ole e 9.0101.
497. Ole e 9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed prediction
Add
BLAST
Chaini27 – 460434Glucan endo-1,3-beta-D-glucosidase
PRO_0000421081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi355 – 3551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi373 ↔ 4352 Publications
Glycosylationi447 – 4471N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Glycosylated.2 Publications
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).

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed only in pollen.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi372 – 3754
Helixi381 – 39111
Turni392 – 3943
Beta strandi395 – 3995
Beta strandi405 – 4073
Helixi415 – 42814
Helixi432 – 4343
Beta strandi439 – 4468
Beta strandi451 – 4533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JONNMR-A360-460[»]
ProteinModelPortaliQ94G86.
SMRiQ94G86. Positions 360-460.

Miscellaneous databases

EvolutionaryTraceiQ94G86.

Family & Domainsi

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTiSM00768. X8. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q94G86-1 [UniParc]FASTAAdd to Basket

« Hide

MAANVQTSSL LFLVFLLLQN FYSANSQSFL GVNYGQLSDN LPSLQATVNL    50
LKSTTIQKVR LFGAEPAVIK AFANTGVEIV IGFDNGDIPT LASNPNVASQ 100
FVKSNVMSFY PASNIIAITV GNEVLTSGDQ KLISQLLPAM QNVQNALNAA 150
SLGGKVKVST VHAMAVLSQS YPPSSGVFNP GLGDTMKALL QFQSANDAPF 200
MISPYPYFAY KNQPTPDTLA FCLFQPNAGQ VDSGNGHKYT NMFDAQVDAV 250
HSALNAMGFK DIEIVVAETG WPHGGDSNEV GPSLDNAKAY VGNLINHLKS 300
KVGTPLMPGK SIDTYLFSLY DEDKKTGASS EKYFGLFKPD GSTTYDVGLL 350
KNTQNPTTPA TPTPTPKAAG SWCVPKPGVS DDQLTGNINY ACGQGIDCGP 400
IQPGGACFEP NTVKAHAAYV MNLYYQSAGR NSWNCDFSQT ATLTNTNPSY 450
GACNFPSGSN 460
Length:460
Mass (Da):48,838
Last modified:December 1, 2001 - v1
Checksum:i46899175F7843DFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF249675 mRNA. Translation: AAK58515.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF249675 mRNA. Translation: AAK58515.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JON NMR - A 360-460 [» ]
ProteinModelPortali Q94G86.
SMRi Q94G86. Positions 360-460.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 3391. Ole e 9.0101.
497. Ole e 9.
CAZyi CBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q94G86.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view ]
Pfami PF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view ]
SMARTi SM00768. X8. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  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. Cited for: LAMINARIN-BINDING.
  5. 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.

Entry informationi

Entry nameiALL9_OLEEU
AccessioniPrimary (citable) accession number: Q94G86
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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 (1 Publication), even though we may be facing two different isoforms of the same allergen.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi