Reviewed, UniProtKB/Swiss-Prot Q7Y1X1 (EST_HEVBR)

Names and origin

Protein names	Recommended name:     Esterase     EC=3.1.1.- Alternative name(s):     Early nodule-specific protein homolog     Latex allergen Hev b 13     Allergen=Hev b 13
Organism	Hevea brasiliensis (Para rubber tree)
Taxonomic identifier	3981 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Crotonoideae › Micrandreae › Hevea

Protein attributes

Sequence length	391 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)

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 process	Plant defense
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Ref.1 Non-traceable author statement. Source: UniProtKB lipid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	IgE binding Ref.1 Inferred from direct assay. Source: UniProtKB hydrolase activity, acting on ester bonds Ref.1 Inferred from direct assay. Source: UniProtKB
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 – 391	365	Esterase		PRO_0000017851
Sites
	Active site	41	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	186	1	N-linked (GlcNAc...) Potential
	Glycosylation	193	1	N-linked (GlcNAc...) Potential
	Glycosylation	313	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	129 – 130	2	PF → SR AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7Y1X1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: B784257A2FC91428	FASTA	391	43,329
	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

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, ALLERGENICITY, POST-TRANSLATIONAL MODIFICATIONS. Strain: cv. RRIM 600. Tissue: Latex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY283800 mRNA. Translation: AAP37470.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001087. Lipase_GDSL. [Graphical view]
Pfam	PF00657. Lipase_GDSL. 1 hit. [Graphical view]
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EST_HEVBR

Accession

Primary (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:	February 9, 2010
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)