ID   ACES_LEPDE              Reviewed;         629 AA.
AC   Q27677;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
OS   Leptinotarsa decemlineata (Colorado potato beetle) (Doryphora
OS   decemlineata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Doryphorini; Leptinotarsa.
OX   NCBI_TaxID=7539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SS; TISSUE=Larva, and Pupae;
RX   PubMed=8580913; DOI=10.1016/0965-1748(95)00055-0;
RA   Zhu K.Y., Clark J.M.;
RT   "Cloning and sequencing of a cDNA encoding acetylcholinesterase in Colorado
RT   potato beetle, Leptinotarsa decemlineata (Say).";
RL   Insect Biochem. Mol. Biol. 25:1129-1138(1995).
CC   -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse.
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   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Attached to
CC       the membrane of the neuronal cholinergic synapses by a GPI-anchor.
CC       {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; L41180; AAB00466.1; -; mRNA.
DR   AlphaFoldDB; Q27677; -.
DR   SMR; Q27677; -.
DR   ChEMBL; CHEMBL2366490; -.
DR   ESTHER; lepde-ACHE; AChE.
DR   MEROPS; S09.980; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001445; Acylcholinesterase_insect.
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; PR00880; ACHEINSECT.
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; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Neurotransmitter degradation; Serine esterase;
KW   Signal; Synapse.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..605
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008607"
FT   PROPEP          606..629
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000008608"
FT   ACT_SITE        253
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        496
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           605
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        458..574
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   629 AA;  71142 MW;  06556F833EB16C72 CRC64;
     MGQLSILCLF VTVCASVCGY SWPSDETTTK PSQFKDFHTD PLVVETTSGL VRGYSKTVLG
     REVHVFTGIP FAKPPIEQLR FKKPVPIDPW HGILDATKQP NSCFQERYEY FPGFEGEEMW
     NPNTNISEDC LYLNIWVPQR LRIRHHADKP TIDRPKVPVL IWIYGGGYMS GTATLDVYDA
     DIIAATSDVI VASMQYRLGS FGFLYLNRYF PRGSDETPGN MGLWDQILAI RWIKDNAAAF
     GGDPDLITLF GESAGGGSIS IHLISPVTKG LVRRGIMQSG TMNAPWSYMS GERAEQIGKI
     LIQDCGCNVS LLENSPRKVM DCMRAVDAKT ISLQQWNSYS GILGFPSTPT IEGVLLPKHP
     MDMLAEGDYE DMEILLGSNH DEGTYFLLYD FIDFFEKDGP SFLQREKYHD IIDTIFKNMS
     RLERDAIVFQ YTNWEHVHDG YLNQKMIGDV VGDYFFVCPT NNFAEVAADR GMKVFYYYFT
     HRTSTSLWGE WMGVIHGDEV EYVFGHPLNM SLQFNSRERE LSLKIMQAFA RFATTGKPVT
     DDVNWPLYTK DQPQYFIFNA DKNGIGKGPR ATACAFWNDF LPKLRDNSGS EEAPCVNTYL
     SKIRSSSNEL LPPSTSLVLI WIMTLLNAL