ID   EST_HEVBR               Reviewed;         391 AA.
AC   Q7Y1X1; P83269;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Esterase;
DE            EC=3.1.1.-;
DE   AltName: Full=Early nodule-specific protein homolog;
DE   AltName: Full=Latex allergen Hev b 13;
DE   AltName: Allergen=Hev b 13;
DE   Flags: Precursor;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAP37470.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 116-140 AND 287-295,
RP   FUNCTION, MASS SPECTROMETRY, AND ALLERGEN.
RC   STRAIN=cv. RRIM 600 {ECO:0000269|PubMed:15024009};
RC   TISSUE=Latex {ECO:0000269|PubMed:15024009};
RX   PubMed=15024009; DOI=10.1074/jbc.m309800200;
RA   Arif S.A.M., Hamilton R.G., Yusof F., Chew N.-P., Loke Y.-H., Nimkar S.,
RA   Beintema J.J., Yeang H.-Y.;
RT   "Isolation and characterization of the early nodule-specific protein
RT   homologue (Hev b 13), an allergenic lipolytic esterase from Hevea
RT   brasiliensis latex.";
RL   J. Biol. Chem. 279:23933-23941(2004).
CC   -!- FUNCTION: Has lipase and esterase activities. May be involved in plant
CC       defense. {ECO:0000269|PubMed:15024009, ECO:0000303|PubMed:15024009}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:15024009}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:15024009}.
CC   -!- MASS SPECTROMETRY: Mass=42975; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15024009};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 78% of
CC       latex allergic patients. IgE binding is abolished by deglycosylation.
CC       {ECO:0000269|PubMed:15024009}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AY283800; AAP37470.1; -; mRNA.
DR   AlphaFoldDB; Q7Y1X1; -.
DR   SMR; Q7Y1X1; -.
DR   Allergome; 3312; Hev b 13.0101.
DR   Allergome; 702; Hev b 13.
DR   PRIDE; Q7Y1X1; -.
DR   OrthoDB; 704138at2759; -.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:UniProtKB.
DR   GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; NAS:UniProtKB.
DR   CDD; cd01837; SGNH_plant_lipase_like; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   Pfam; PF00657; Lipase_GDSL; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Plant defense; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..391
FT                   /note="Esterase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000017851"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        129..130
FT                   /note="PF -> SR (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   391 AA;  43329 MW;  B784257A2FC91428 CRC64;
     MEFPETNNNP IITLSFLLCM LSLAYASETC DFPAIFNFGD SNSDTGGKAA AFYPLNPPYG
     ETFFHRSTGR YSDGRLIIDF IAESFNLPYL SPYLSSLGSN FKHGADFATA GSTIKLPTTI
     IPAHGGFSPF YLDVQYSQFR QFIPRSQFIR ETGGIFAELV PEEYYFEKAL YTFDIGQNDL
     TEGFLNLTVE EVNATVPDLV NSFSANVKKI YDLGARTFWI HNTGPIGCLS FILTYFPWAE
     KDSAGCAKAY NEVAQHFNHK LKEIVAQLRK DLPLATFVHV DIYSVKYSLF SEPEKHGFEF
     PLITCCGYGG KYNFSVTAPC GDTVTADDGT KIVVGSCACP SVRVNWDGAH YTEAANEYFF
     DQISTGAFSD PPVPLNMACH KTESLRTLAS V