ID   ACES_ANOST              Reviewed;         664 AA.
AC   P56161;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1901515; DOI=10.1007/bf00712805;
RA   Hall L.M.C., Malcolm C.A.;
RT   "The acetylcholinesterase gene of Anopheles stephensi.";
RL   Cell. Mol. Neurobiol. 11:131-141(1991).
CC   -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can
CC       hydrolyze butyrylthiocholine.
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. Cell membrane; Lipid-anchor, GPI-anchor.
CC       Note=Attached to the membrane of the neuronal cholinergic synapses by a
CC       GPI-anchor.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P56161; -.
DR   SMR; P56161; -.
DR   STRING; 30069.P56161; -.
DR   ESTHER; anost-ACHE; AChE.
DR   MEROPS; S09.980; -.
DR   EnsemblMetazoa; ASTE010565-RA; ASTE010565-PA; ASTE010565.
DR   VEuPathDB; VectorBase:ASTE010565; -.
DR   VEuPathDB; VectorBase:ASTEI01008; -.
DR   VEuPathDB; VectorBase:LOC118504721; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Neurotransmitter degradation; Reference proteome;
KW   Serine esterase; Signal; Synapse.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..647
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008600"
FT   PROPEP          648..664
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000008601"
FT   ACT_SITE        261
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        390
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        504
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           647
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..330
FT                   /evidence="ECO:0000250"
FT   DISULFID        466..588
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  74629 MW;  0BFBF9414F8020C7 CRC64;
     MFVNQRTRRP YMSVFVLVLG AAVICPAYGI IDRLVVQTSS GPIRGRSTMV QGREVHVFNG
     VPFAKPPVDS LRFKKPVPAE PWHGVLDATR LPPSCIQERY EYFPGFAGEE MWNPNTNVSE
     DCLYLNIWVP TKTRLRHGRG LNFGSNDYFQ DDDDFQRQHQ SKGGLAMLVW IYGGGFMSGT
     STLDIYNAEI LAAVGNVIVA SMQYRVGAFG FLYLAPYING YEEDAPGNMG MWDQALAIRW
     LKENAKAFGG DPDLITLFGE SAGGSSVSLH LLSPVTRGLS KRGILQSGTL NAPWSHMTAE
     KALQIAEGLI DDCNCNLTML KESPSTVMQC MRNVDAKTIS VQQWNSYSGI LGFPSAPTID
     GVFMTADPMT MLREANLEGI DILVGSNRDE GTYFLLYDFI DYFEKDAATS LPRDKFLEIM
     NTIFNKASEP EREAIIFQYT GWESGNDGYQ NQHQVGRAVG DHFFICPTNE FALGLTERGA
     SVHYYYFTHR TSTSLWGEWM GVLHGDEVEY IFGQPMNASL QYRQRERDLS RRMVLSVSEF
     ARTGNPALEG EHWPLYTREN PIFFIFNAEG EDDLRGEKYG RGPMATSCAF WNDFLPRLRA
     WSVPSKSPCN LLEQMSIASV SSTMPIVVMV VLVLIPLCAW WWAIKKNKTP PHPQVILETR
     AFMH