Q94G86 (ALL9_OLEEU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

OLE9

Organism

Olea europaea (Common olive)

Taxonomic identifier

4146 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Oleaceae › Oleeae › Olea

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Disease	Allergen
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 460

434

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

PRO_0000421081

Sites

Active site

268

1

Nucleophile By similarity

Active site

331

1

Proton donor By similarity

Amino acid modifications

Glycosylation

355

1

N-linked (GlcNAc...) Potential

Glycosylation

447

1

N-linked (GlcNAc...) Potential

Disulfide bond

373 ↔ 435

Ref.2 Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

460

Helix Strand Turn

Details...

Beta strand

372 – 375

4

Helix

381 – 391

11

Turn

392 – 394

3

Beta strand

395 – 399

5

Beta strand

405 – 407

3

Helix

415 – 428

14

Helix

432 – 434

3

Beta strand

439 – 446

8

Beta strand

451 – 453

3

Sequences

	Sequence		Length	Mass (Da)
	Q94G86 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 46899175F7843DFC	FASTA	460	48,838
	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

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: BIINDING TO LAMINARIN.
[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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JON	NMR	-	A	360-460	[»]

ProteinModelPortal

Q94G86.

SMR

Q94G86. Positions 360-460.

ModBase

Search...

Protein family/group databases

Allergome

3391. Ole e 9.0101.
497. Ole e 9.

CAZy

CBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]

Pfam

PF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]

SMART

SM00768. X8. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00587. GLYCOSYL_HYDROL_F17. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q94G86.

Entry information

Entry name

ALL9_OLEEU

Accession

Primary (citable) accession number: Q94G86

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2013
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program