Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucan endo-1,3-beta-D-glucosidase

Gene

OLE9

Organism
Olea europaea (Common olive)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

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)DescriptionActionsGraphical viewLength
Active sitei268NucleophileBy similarity1
Active sitei331Proton donorBy similarity1

GO - Molecular functioni

  • glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • (1->3)-beta-D-glucan catabolic process Source: UniProtKB

Keywordsi

Molecular functionGlycosidase, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000042108127 – 460Glucan endo-1,3-beta-D-glucosidaseAdd BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi355N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi373 ↔ 4352 Publications
Glycosylationi447N-linked (GlcNAc...) asparagineSequence analysis1

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

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1460
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi372 – 375Combined sources4
Helixi381 – 391Combined sources11
Turni392 – 394Combined sources3
Beta strandi395 – 399Combined sources5
Beta strandi405 – 407Combined sources3
Helixi415 – 428Combined sources14
Helixi432 – 434Combined sources3
Beta strandi439 – 446Combined sources8
Beta strandi451 – 453Combined sources3

3D structure databases

ProteinModelPortaliQ94G86
SMRiQ94G86
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

InterProiView protein in InterPro
IPR000490 Glyco_hydro_17
IPR017853 Glycoside_hydrolase_SF
IPR012946 X8
PfamiView protein in Pfam
PF00332 Glyco_hydro_17, 1 hit
PF07983 X8, 1 hit
SMARTiView protein in SMART
SM00768 X8, 1 hit
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

        10         20         30         40         50
MAANVQTSSL LFLVFLLLQN FYSANSQSFL GVNYGQLSDN LPSLQATVNL
60 70 80 90 100
LKSTTIQKVR LFGAEPAVIK AFANTGVEIV IGFDNGDIPT LASNPNVASQ
110 120 130 140 150
FVKSNVMSFY PASNIIAITV GNEVLTSGDQ KLISQLLPAM QNVQNALNAA
160 170 180 190 200
SLGGKVKVST VHAMAVLSQS YPPSSGVFNP GLGDTMKALL QFQSANDAPF
210 220 230 240 250
MISPYPYFAY KNQPTPDTLA FCLFQPNAGQ VDSGNGHKYT NMFDAQVDAV
260 270 280 290 300
HSALNAMGFK DIEIVVAETG WPHGGDSNEV GPSLDNAKAY VGNLINHLKS
310 320 330 340 350
KVGTPLMPGK SIDTYLFSLY DEDKKTGASS EKYFGLFKPD GSTTYDVGLL
360 370 380 390 400
KNTQNPTTPA TPTPTPKAAG SWCVPKPGVS DDQLTGNINY ACGQGIDCGP
410 420 430 440 450
IQPGGACFEP NTVKAHAAYV MNLYYQSAGR NSWNCDFSQT ATLTNTNPSY
460
GACNFPSGSN
Length:460
Mass (Da):48,838
Last modified:December 1, 2001 - v1
Checksum:i46899175F7843DFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249675 mRNA Translation: AAK58515.1

Similar proteinsi

Entry informationi

Entry nameiALL9_OLEEU
AccessioniPrimary (citable) accession number: Q94G86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: December 1, 2001
Last modified: May 10, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health