ACES_CULQU
ID ACES_CULQU Reviewed; 132 AA.
AC Q867X2; Q867X1; Q867X4;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Fragment;
GN Name=ACE-1;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176 {ECO:0000312|EMBL:CAD54761.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BED {ECO:0000312|EMBL:CAD54761.1}, BO {ECO:0000312|EMBL:CAD54763.1},
RC Bouake {ECO:0000312|EMBL:CAD54764.1}, Brazza {ECO:0000312|EMBL:CAD54765.1},
RC Bresil {ECO:0000312|EMBL:CAD54766.1}, BSQ {ECO:0000312|EMBL:CAD54769.1},
RC DJI {ECO:0000312|EMBL:CAD54770.1}, Harare {ECO:0000312|EMBL:CAD54772.1},
RC Ling {ECO:0000312|EMBL:CAD54775.1}, Madurai {ECO:0000312|EMBL:CAD54776.1},
RC Mao {ECO:0000312|EMBL:CAD54777.1},
RC Martinique {ECO:0000312|EMBL:CAD54778.1},
RC Moorea {ECO:0000312|EMBL:CAD54779.1}, ProR {ECO:0000312|EMBL:CAD54782.1},
RC Recife {ECO:0000312|EMBL:CAD54783.1}, Slab {ECO:0000312|EMBL:CAD54784.1},
RC Supercar {ECO:0000312|EMBL:CAD54785.1}, TemR {ECO:0000312|EMBL:CAD54786.1},
RC Thai {ECO:0000312|EMBL:CAD54787.1}, and
RC Trans {ECO:0000312|EMBL:CAD54789.1};
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:0000269|PubMed:12736674};
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; AJ512689; CAD54761.1; -; Genomic_DNA.
DR EMBL; AJ512691; CAD54763.1; -; Genomic_DNA.
DR EMBL; AJ512692; CAD54764.1; -; Genomic_DNA.
DR EMBL; AJ512693; CAD54765.1; -; Genomic_DNA.
DR EMBL; AJ512694; CAD54766.1; -; Genomic_DNA.
DR EMBL; AJ512697; CAD54769.1; -; Genomic_DNA.
DR EMBL; AJ512698; CAD54770.1; -; Genomic_DNA.
DR EMBL; AJ512700; CAD54772.1; -; Genomic_DNA.
DR EMBL; AJ512703; CAD54775.1; -; Genomic_DNA.
DR EMBL; AJ512704; CAD54776.1; -; Genomic_DNA.
DR EMBL; AJ512705; CAD54777.1; -; Genomic_DNA.
DR EMBL; AJ512706; CAD54778.1; -; Genomic_DNA.
DR EMBL; AJ512707; CAD54779.1; -; Genomic_DNA.
DR EMBL; AJ512710; CAD54782.1; -; Genomic_DNA.
DR EMBL; AJ512711; CAD54783.1; -; Genomic_DNA.
DR EMBL; AJ512712; CAD54784.1; -; Genomic_DNA.
DR EMBL; AJ512713; CAD54785.1; -; Genomic_DNA.
DR EMBL; AJ512714; CAD54786.1; -; Genomic_DNA.
DR EMBL; AJ512715; CAD54787.1; -; Genomic_DNA.
DR EMBL; AJ512717; CAD54789.1; -; Genomic_DNA.
DR AlphaFoldDB; Q867X2; -.
DR SMR; Q867X2; -.
DR ESTHER; culpi-ACHE1; AChE.
DR MEROPS; S09.980; -.
DR EnsemblMetazoa; XM_038261576.1; XP_038117504.1; LOC6037551.
DR VEuPathDB; VectorBase:CPIJ006034; -.
DR VEuPathDB; VectorBase:CQUJHB013404; -.
DR Proteomes; UP000002320; Unplaced.
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; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000997; Cholinesterase.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Neurotransmitter degradation; Reference proteome; Secreted;
KW Serine esterase; Synapse.
FT CHAIN <1..>132
FT /note="Acetylcholinesterase"
FT /id="PRO_0000070281"
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: BO, DJI, Harare, Martinique,
FT Recife, Supercar, TemR and Trans; confers resistance to
FT insecticides)"
FT /evidence="ECO:0000269|PubMed:12736674"
FT VARIANT 114
FT /note="A -> T (in strain: TemR and Trans)"
FT /evidence="ECO:0000269|PubMed:12736674"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAD54761.1"
FT NON_TER 132
FT /evidence="ECO:0000312|EMBL:CAD54761.1"
SQ SEQUENCE 132 AA; 14543 MW; 2F40C4B3FC2468E8 CRC64;
SGKKVDAWMG IPYAQPPLGP LRFRHPRPAE RWTGVLNATK PPNSCVQIVD TVFGDFPGAT
MWNPNTPLSE DCLYINVVVP RPRPKNAAVM LWIFGGGFYS GTATLDVYDH RTLASEENVI
VVSLQYRVAS LG
