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Q7Y1X1 (EST_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 11, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Esterase

EC=3.1.1.-
Alternative name(s):
Early nodule-specific protein homolog
Latex allergen Hev b 13
Allergen=Hev b 13
OrganismHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifier3981 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has lipase and esterase activities. May be involved in plant defense. Ref.1

Post-translational modification

The N-terminus is blocked. Ref.1

Glycosylated. Ref.1

Allergenic properties

Causes an allergic reaction in human. Binds to IgE in 78% of latex allergic patients. IgE binding is abolished by deglycosylation. Ref.1

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family.

Mass spectrometry

Molecular mass is 42975 Da from positions 1 - 391. Determined by MALDI. Ref.1

Ontologies

Keywords
   Biological processPlant defense
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processdefense response

Non-traceable author statement Ref.1. Source: UniProtKB

lipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionIgE binding

Inferred from direct assay Ref.1. Source: UniProtKB

hydrolase activity, acting on ester bonds

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 391365Esterase
PRO_0000017851

Sites

Active site411Nucleophile By similarity
Active site3471 By similarity
Active site3501 By similarity

Amino acid modifications

Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict129 – 1302PF → SR AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7Y1X1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B784257A2FC91428

FASTA39143,329
        10         20         30         40         50         60 
MEFPETNNNP IITLSFLLCM LSLAYASETC DFPAIFNFGD SNSDTGGKAA AFYPLNPPYG 

        70         80         90        100        110        120 
ETFFHRSTGR YSDGRLIIDF IAESFNLPYL SPYLSSLGSN FKHGADFATA GSTIKLPTTI 

       130        140        150        160        170        180 
IPAHGGFSPF YLDVQYSQFR QFIPRSQFIR ETGGIFAELV PEEYYFEKAL YTFDIGQNDL 

       190        200        210        220        230        240 
TEGFLNLTVE EVNATVPDLV NSFSANVKKI YDLGARTFWI HNTGPIGCLS FILTYFPWAE 

       250        260        270        280        290        300 
KDSAGCAKAY NEVAQHFNHK LKEIVAQLRK DLPLATFVHV DIYSVKYSLF SEPEKHGFEF 

       310        320        330        340        350        360 
PLITCCGYGG KYNFSVTAPC GDTVTADDGT KIVVGSCACP SVRVNWDGAH YTEAANEYFF 

       370        380        390 
DQISTGAFSD PPVPLNMACH KTESLRTLAS V 

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References

[1]"Isolation and characterization of the early nodule-specific protein homologue (Hev b 13), an allergenic lipolytic esterase from Hevea brasiliensis latex."
Arif S.A.M., Hamilton R.G., Yusof F., Chew N.-P., Loke Y.-H., Nimkar S., Beintema J.J., Yeang H.-Y.
J. Biol. Chem. 279:23933-23941(2004) [PubMed: 15024009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 116-140 AND 287-295, FUNCTION, MASS SPECTROMETRY, ALLERGEN, POST-TRANSLATIONAL MODIFICATIONS.
Strain: cv. RRIM 600.
Tissue: Latex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY283800 mRNA. Translation: AAP37470.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

Allergome3312. Hev b 13.0101.
702. Hev b 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001087. Lipase_GDSL.
[Graphical view]
PfamPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
PROSITEPS01098. LIPASE_GDSL_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEST_HEVBR
AccessionPrimary (citable) accession number: Q7Y1X1
Secondary accession number(s): P83269
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: January 11, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

SIMILARITY comments

Index of protein domains and families