ID   EST1_CULPI              Reviewed;         540 AA.
AC   P16854;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Esterase B1;
DE            EC=3.1.1.1;
DE   Flags: Precursor;
GN   Name=B1;
OS   Culex pipiens (House mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TEM-R;
RX   PubMed=2320576; DOI=10.1073/pnas.87.7.2574;
RA   Mouches C., Pauplin Y., Agarwal M., Lemieux L., Herzog M., Abadon M.,
RA   Beyssat-Arnaouty V., Hyrien O., de Saint Vincent B.R., Georghiou G.P.,
RA   Pasteur N.;
RT   "Characterization of amplification core and esterase B1 gene responsible
RT   for insecticide resistance in Culex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2574-2578(1990).
CC   -!- FUNCTION: Overproduction of nonspecific esterases is a common mechanism
CC       of resistance to organophosphate insecticides.
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   -!- MISCELLANEOUS: There are two such esterases: A and B. Alleles of both A
CC       and B are known.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M32328; AAA28289.1; -; Genomic_DNA.
DR   PIR; A35986; A35986.
DR   AlphaFoldDB; P16854; -.
DR   SMR; P16854; -.
DR   ESTHER; culpi-1este; Carb_B_Arthropoda.
DR   MEROPS; S09.980; -.
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   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Serine esterase; Signal.
FT   SIGNAL          1..?
FT   CHAIN           ?..540
FT                   /note="Esterase B1"
FT                   /id="PRO_0000008551"
FT   ACT_SITE        191
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        324
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        442
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..81
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  60807 MW;  F73B25B3A7157C95 CRC64;
     MSLESLTVQT KYGPVRGKRN VSLLGQEYVS FQGIPYARAP EGELRFKAPV PPQKWTETLD
     CTQQCEPCYH FDRRLQKIVG CEDSLKINVF AKEINPSTPL PVMLYIYGGG FTEGTSGTEL
     YGPDFLVQKD IVLVSFNYRI GALGFLCCQS EQDGVPGNAG LKDQNLAIRW VLENIAAFGG
     DPKRVTLAGH SAGAASVQYH LISDASKDLF QRRIVMSGST YSSWSLTRQR NWVEKLAKAI
     GWDGQGGESG ALRFLRRAKP EDIVAHQEKL LTDQDMQDDI FTPFGPTVEP YLTEQCIIPK
     APFEMARTAW GDKIDIMIGG TSEEGLLLLQ KIKLHPELLS HPHLFLGNVP PNLKISMEKR
     IEFAAKLKQR YYPDSIPSME NNLGYVHMMS DRVFWHGLHR TILARAARSR ARTFVYRICL
     DSEFYNHYRI MMIDPKLRGT AHADELSYLF SNFTQQVPGK ETFEYRGLQT LVDVFSAFVI
     NGDPNCGMTA KGGVVFEPNA QTKPTFKCLN IANDGVAFVD YPDADRLDMW DAMYVNDELF