ID   ACES_CULPI              Reviewed;         702 AA.
AC   Q86GC8; Q86GD0;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ACHE1;
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 {ECO:0000312|EMBL:CAD56155.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SLAB {ECO:0000312|EMBL:CAD33707.2}, and
RC   SR {ECO:0000312|EMBL:CAD56155.1};
RX   PubMed=12736674; DOI=10.1038/423136b;
RA   Weill M., Lutfalla G., Mogensen K., Chandre F., Berthomieu A., Berticat C.,
RA   Pasteur N., Philips A., Fort P., Raymond M.;
RT   "Insecticide resistance in mosquito vectors.";
RL   Nature 423:136-137(2003).
CC   -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse.
CC       {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetylcholine + H2O = acetate + choline + H(+);
CC         Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
CC         Evidence={ECO:0000250|UniProtKB:P22303};
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}. Secreted {ECO:0000250}.
CC       Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- POLYMORPHISM: Strain SLAB is susceptible to insecticides while strain
CC       SR is resistant. Insensitivity to insecticides results from a loss of
CC       sensitivity of acetylcholinesterase to organophosphates and carbamates
CC       and is due to a variant at position 247. {ECO:0000269|PubMed:12736674}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ515147; CAD56155.1; -; mRNA.
DR   EMBL; AJ489456; CAD33707.2; -; mRNA.
DR   AlphaFoldDB; Q86GC8; -.
DR   SMR; Q86GC8; -.
DR   ESTHER; culpi-ACHE1; AChE.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
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   InterPro; IPR000997; Cholinesterase.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
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   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Secreted; Serine esterase; Signal; Synapse.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..702
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008602"
FT   REGION          107..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        453
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        567
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        529..650
FT                   /evidence="ECO:0000250"
FT   VARIANT         247
FT                   /note="G -> S (in strain: SR; confers resistance to
FT                   insecticides)"
FT                   /evidence="ECO:0000269|PubMed:12736674"
SQ   SEQUENCE   702 AA;  78179 MW;  4B11ABF5EA824A07 CRC64;
     MEIRGLITRL LGPCHLRHLI LCSLGLYSIL VQSVHCRHHD IGSSVAHQLG SKYSQSSSLS
     SSSQSSSSLA EEATLNKDSD AFFTPYIGHG DSVRIVDAEL GTLEREHIHS TTTRRRGLTR
     RESSSDATDS DPLVITTDKG KIRGTTLEAP SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE
     RWTGVLNATK PPNSCVQIVD TVFGDFPGAT MWNPNTPLSE DCLYINVVVP RPRPKNAAVM
     LWIFGGGFYS GTATLDVYDH RTLASEENVI VVSLQYRVAS LGFLFLGTPE APGNAGLFDQ
     NLALRWVRDN IHRFGGDPSR VTLFGESAGA VSVSLHLLSA LSRDLFQRAI LQSGSPTAPW
     ALVSREEATL RALRLAEAVN CPHDATKLSD AVECLRTKDP NELVDNEWGT LGICEFPFVP
     VVDGAFLDET PQRSLASGRF KKTDILTGSN TEEGYYFIIY YLTELLRKEE GVTVTREEFL
     QAVRELNPYV NGAARQAIVF EYTDWIEPDN PNSNRDALDK MVGDYHFTCN VNEFAQRYAE
     EGNNVFMYLY THRSKGNPWP RWTGVMHGDE INYVFGEPLN SALGYQDDEK DFSRKIMRYW
     SNFAKTGNPN PSTPSVDLPE WPKHTAHGRH YLELGLNTTF VGRGPRLRQC AFWKKYLPQL
     VAATSNLQVT PAPSVPCESS STSYRSTLLL IVTLLLVTRF KI