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

Esterase

Gene
N/A
Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has lipase and esterase activities. May be involved in plant defense.1 Publication1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411NucleophileBy similarity
Active sitei347 – 3471By similarity
Active sitei350 – 3501By similarity

GO - Molecular functioni

  • hydrolase activity, acting on ester bonds Source: UniProtKB
  • IgE binding Source: UniProtKB

GO - Biological processi

  • defense response Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Esterase (EC:3.1.1.-)
Alternative name(s):
Early nodule-specific protein homolog
Latex allergen Hev b 13
Allergen: Hev b 13
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Pathology & Biotechi

Allergenic propertiesi

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

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3312. Hev b 13.0101.
702. Hev b 13.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 391365EsteraseSequence analysisPRO_0000017851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence analysis
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The N-terminus is blocked.1 Publication
Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

GO - Molecular functioni

  • IgE binding Source: UniProtKB

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. GDSL.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7Y1X1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFPETNNNP IITLSFLLCM LSLAYASETC DFPAIFNFGD SNSDTGGKAA
60 70 80 90 100
AFYPLNPPYG ETFFHRSTGR YSDGRLIIDF IAESFNLPYL SPYLSSLGSN
110 120 130 140 150
FKHGADFATA GSTIKLPTTI IPAHGGFSPF YLDVQYSQFR QFIPRSQFIR
160 170 180 190 200
ETGGIFAELV PEEYYFEKAL YTFDIGQNDL TEGFLNLTVE EVNATVPDLV
210 220 230 240 250
NSFSANVKKI YDLGARTFWI HNTGPIGCLS FILTYFPWAE KDSAGCAKAY
260 270 280 290 300
NEVAQHFNHK LKEIVAQLRK DLPLATFVHV DIYSVKYSLF SEPEKHGFEF
310 320 330 340 350
PLITCCGYGG KYNFSVTAPC GDTVTADDGT KIVVGSCACP SVRVNWDGAH
360 370 380 390
YTEAANEYFF DQISTGAFSD PPVPLNMACH KTESLRTLAS V
Length:391
Mass (Da):43,329
Last modified:October 1, 2003 - v1
Checksum:iB784257A2FC91428
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1302PF → SR AA sequence (PubMed:15024009).Curated

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283800 mRNA. Translation: AAP37470.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283800 mRNA. Translation: AAP37470.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3312. Hev b 13.0101.
702. Hev b 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. GDSL.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEST_HEVBR
AccessioniPrimary (citable) accession number: Q7Y1X1
Secondary accession number(s): P83269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: September 16, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.