ID   ACES_CULPP              Reviewed;         132 AA.
AC   Q867X3; Q867X5;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Fragment;
GN   Name=ACE-1;
OS   Culex pipiens pipiens (Northern 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=38569 {ECO:0000312|EMBL:CAD54762.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Barriol {ECO:0000312|EMBL:CAD54760.1}, Bleuet
RC   {ECO:0000312|EMBL:CAD54762.1}, BrugesA {ECO:0000312|EMBL:CAD54767.1},
RC   BrugesB {ECO:0000312|EMBL:CAD54768.1}, Espro
RC   {ECO:0000312|EMBL:CAD54771.1}, Heteren {ECO:0000312|EMBL:CAD54773.1},
RC   Killcare {ECO:0000312|EMBL:CAD54774.1}, Padova
RC   {ECO:0000312|EMBL:CAD54780.1}, and Praias
RC   {ECO:0000312|EMBL:CAD54781.1};
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: A number of strains are susceptible to insecticides while
CC       others are resistant. Insensitivity to insecticides results from a loss
CC       of sensitivity of acetylcholinesterase to organophosphates and
CC       carbamates and is due to a variant at position 97.
CC       {ECO:0000269|PubMed:12736674}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ512688; CAD54760.1; -; Genomic_DNA.
DR   EMBL; AJ512690; CAD54762.1; -; Genomic_DNA.
DR   EMBL; AJ512695; CAD54767.1; -; Genomic_DNA.
DR   EMBL; AJ512696; CAD54768.1; -; Genomic_DNA.
DR   EMBL; AJ512699; CAD54771.1; -; Genomic_DNA.
DR   EMBL; AJ512701; CAD54773.1; -; Genomic_DNA.
DR   EMBL; AJ512702; CAD54774.1; -; Genomic_DNA.
DR   EMBL; AJ512708; CAD54780.1; -; Genomic_DNA.
DR   EMBL; AJ512709; CAD54781.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q867X3; -.
DR   SMR; Q867X3; -.
DR   ESTHER; culpi-ACHE1; ACHE.
DR   GlyCosmos; Q867X3; 1 site, No reported glycans.
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   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF12; ACETYLCHOLINESTERASE 1; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Secreted; Serine esterase; Synapse.
FT   CHAIN           <1..>132
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000070280"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..72
FT                   /evidence="ECO:0000250"
FT   VARIANT         97
FT                   /note="G -> S (in strain: Barriol, Espro, Padova and
FT                   Praias)"
FT                   /evidence="ECO:0000269|PubMed:12736674"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAD54762.1"
FT   NON_TER         132
FT                   /evidence="ECO:0000312|EMBL:CAD54762.1"
SQ   SEQUENCE   132 AA;  14543 MW;  2F40C4B3FC2468E8 CRC64;
     SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE RWTGVLNATK PPNSCVQIVD TVFGDFPGAT
     MWNPNTPLSE DCLYINVVVP RPRPKNAAVM LWIFGGGFYS GTATLDVYDH RTLASEENVI
     VVSLQYRVAS LG
//