ID   ESTE_MYZPE              Reviewed;         552 AA.
AC   P35501;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Esterase E4;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase;
DE   Flags: Precursor;
OS   Myzus persicae (Green peach aphid) (Aphis persicae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Macrosiphini; Myzus.
OX   NCBI_TaxID=13164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-63.
RC   STRAIN=R3 / Isolate 794J;
RX   PubMed=8373371; DOI=10.1042/bj2940569;
RA   Field L.M., Williamson M.S., Moores G.D., Devonshire A.L.;
RT   "Cloning and analysis of the esterase genes conferring insecticide
RT   resistance in the peach-potato aphid, Myzus persicae (Sulzer).";
RL   Biochem. J. 294:569-574(1993).
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: This esterase confers insecticide resistance.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; X74554; CAA52648.1; -; mRNA.
DR   PIR; S36786; S36786.
DR   AlphaFoldDB; P35501; -.
DR   SMR; P35501; -.
DR   ESTHER; myzpe-este4; Carb_B_Arthropoda.
DR   MEROPS; S09.980; -.
DR   PRIDE; P35501; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Serine esterase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:8373371"
FT   CHAIN           24..552
FT                   /note="Esterase E4"
FT                   /id="PRO_0000008566"
FT   ACT_SITE        214
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        339
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        463
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        89..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..277
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  61348 MW;  B97B67272DFF7209 CRC64;
     MKNTCGILLN LFLFIGCFLT CSASNTPKVQ VHSGEIAGGF EYTYNGRKIY SFLGIPYASP
     PVQNNRFKEP QPVQPWLGVW NATVPGSACL GIEFGSGSKI IGQEDCLFLN VYTPKLPQEN
     SAGDLMNVIV HIHGGGYYFG EGILYGPHYL LDNNDFVYVS INYRLGVLGF ASTGDGVLTG
     NNGLKDQVAA LKWIQQNIVA FGGDPNSVTI TGMSAGASSV HNHLISPMSK GLFNRAIIQS
     GSAFCHWSTA ENVAQKTKYI ANLMGCPTNN SVEIVECLRS RPAKAIAKSY LNFMPWRNFP
     FTPFGPTVEV AGYEKFLPDI PEKLVPHDIP VLISIAQDEG LIFSTFLGLE NGFNELNNNW
     NEHLPHILDY NYTISNENLR FKTAQDIKEF YFGDKPISKE TKSNLSKMIS DRSFGYGTSK
     AAQHIAAKNT APVYFYEFGY SGNYSYVAFF DPKSYSRGSS PTHGDETSYV LKMDGFYVYD
     NEEDRKMIKT MVNIWATFIK SGVPDTENSE IWLPVSKNLA DPFRFTKITQ QQTFEAREQS
     TTGIMNFGVA YH