ID   EST6_APIME              Reviewed;         557 AA.
AC   B2D0J5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Venom carboxylesterase-6;
DE            EC=3.1.1.1;
DE   AltName: Allergen=Api m 8;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RA   Blank S., Seismann H., Bockisch B., Braren I., Bredehorst R., Grunwald T.,
RA   Ollert M., Spillner E.;
RT   "Identification and recombinant expression of a novel IgE-reactive 70 kDa
RT   carboxylesterase from Apis mellifera venom.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17073008; DOI=10.1038/nature05260;
RG   Honeybee genome sequencing consortium;
RT   "Insights into social insects from the genome of the honeybee Apis
RT   mellifera.";
RL   Nature 443:931-949(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU564833; ACB70231.1; -; mRNA.
DR   RefSeq; NP_001119716.1; NM_001126244.1.
DR   AlphaFoldDB; B2D0J5; -.
DR   SMR; B2D0J5; -.
DR   STRING; 7460.GB53756-PA; -.
DR   Allergome; 5756; Api m 8.
DR   Allergome; 5757; Api m 8.0101.
DR   ESTHER; apime-b2d0j5; Carb_B_Arthropoda.
DR   PaxDb; B2D0J5; -.
DR   EnsemblMetazoa; NM_001126244; NP_001119716; GeneID_410928.
DR   GeneID; 410928; -.
DR   KEGG; ame:410928; -.
DR   CTD; 39392; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; B2D0J5; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   2: Evidence at transcript level;
KW   Allergen; Disulfide bond; Glycoprotein; Hydrolase; Reference proteome;
KW   Secreted; Serine esterase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..557
FT                   /note="Venom carboxylesterase-6"
FT                   /id="PRO_5000336988"
FT   ACT_SITE        212
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        341
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        464
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..275
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  63637 MW;  804E1ED11DA92D25 CRC64;
     MYMLKLSYIL LFLGFVKFSW QDKQVPKVST FTGNIRGYYK KSRSDRLYEA YEGIPYAQSP
     VGKFRFQPPR PIKKWSKDLS ATKKSSVCMQ YLMTFTTHGN RVKGSEDCLY INIYVPVRNN
     RKPLLPVMFW IHGGAFQFAS GNEANETLFM DRNIVFVAIN YRLGPFGFLS TGDIVVPGNM
     GLKDQSMALR WVFNNIKSFG GNPNKITIFG MSAGGASVHY HYLSPMSAGL FKRGISISGV
     AFCPWAQTKH APEKAKKLGA LMKCRTDNTK KMIDCLQSRP ARIIAQAVGD FMFWLYNPFT
     PFGPVVETYG SNPFISNSPI NIINNGQVYD VPWISGVVSK EGLYTAAEFV DNAKLLWHLN
     DHWDEIAPYL LDFNYTIPLD QHRQVAKKIK NYYLRSGPIN YDKVESIIQM MSDRLFNIDF
     EKAVRLQARI NKSPVWTYYY SYRAEHSVSE ILSGGSTTDY GVCHGDDIFL TLNSIISNVT
     KPQDLAMQQL LINFYTSFAI QGIPYIDEAS WPSLNPNDPD FRYLHIVNFT NIKMEVNNNF
     ANKSFWKTIP FNENKLN