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Q94G86

- ALL9_OLEEU

UniProt

Q94G86 - ALL9_OLEEU

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
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 – 2681NucleophileBy similarity
    Active sitei331 – 3311Proton donorBy 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

    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 Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 460434Glucan endo-1,3-beta-D-glucosidasePRO_0000421081Add
    BLAST

    Amino acid modifications

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

    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

    1
    460
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Belongs to the glycosyl hydrolase 17 family.Curated

    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: October 1, 2014
    This is version 55 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 (PubMed:22385802), even though we may be facing two different isoforms of the same allergen.1 Publication

    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