ID   ACES_ELEEL              Reviewed;         633 AA.
AC   O42275;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ache;
OS   Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC   Gymnotoidei; Gymnotidae; Electrophorus.
OX   NCBI_TaxID=8005;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9407087; DOI=10.1074/jbc.272.52.33045;
RA   Simon S., Massoulie J.;
RT   "Cloning and expression of acetylcholinesterase from Electrophorus.
RT   Splicing pattern of the 3' exons in vivo and in transfected mammalian
RT   cells.";
RL   J. Biol. Chem. 272:33045-33055(1997).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC       by rapid hydrolysis of the acetylcholine released into the synaptic
CC       cleft.
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   -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF030422; AAB86606.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42275; -.
DR   SMR; O42275; -.
DR   STRING; 8005.ENSEEEP00000024330; -.
DR   BindingDB; O42275; -.
DR   ChEMBL; CHEMBL4078; -.
DR   DrugCentral; O42275; -.
DR   ESTHER; eleel-ACHE; ACHE.
DR   GlyCosmos; O42275; 6 sites, No reported glycans.
DR   ABCD; O42275; 3 sequenced antibodies.
DR   BRENDA; 3.1.1.7; 2051.
DR   SABIO-RK; O42275; -.
DR   Proteomes; UP000314983; Unassembled WGS sequence.
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   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR014788; AChE_tetra.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF11; ACETYLCHOLINESTERASE; 1.
DR   Pfam; PF08674; AChE_tetra; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Reference proteome; Secreted;
KW   Serine esterase; Signal; Synapse.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..633
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008594"
FT   ACT_SITE        225
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        352
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        494
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        427..579
FT                   /evidence="ECO:0000250"
FT   DISULFID        630
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   633 AA;  71815 MW;  FC92FE7E4ADB84C3 CRC64;
     MKILDALLFP VIFIMFFIHL SIAQTDPELT IMTRLGQVQG TRLPVPDRSH VIAFLGIPFA
     EPPLGKMRFK PPEPKKPWND VFDARDYPSA CYQYVDTSYP GFSGTEMWNP NRMMSEDCLY
     LNVWVPATPR PHNLTVMVWI YGGGFYSGSS SLDVYDGRYL AHSEKVVVVS MNYRVSAFGF
     LALNGSAEAP GNVGLLDQRL ALQWVQDNIH FFGGNPKQVT IFGESAGAAS VGMHLLSPDS
     RPKFTRAILQ SGVPNGPWRT VSFDEARRRA IKLGRLVGCP DGNDTDLIDC LRSKQPQDLI
     DQEWLVLPFS GLFRFSFVPV IDGVVFPDTP EAMLNSGNFK DTQILLGVNQ NEGSYFLIYG
     APGFSKDNES LITREDFLQG VKMSVPHANE IGLEAVILQY TDWMDEDNPI KNREAMDDIV
     GDHNVVCPLQ HFAKMYAQYS ILQGQTGTAS QGNLGWGNSG SASNSGNSQV SVYLYMFDHR
     ASNLVWPEWM GVIHGYEIEF VFGLPLEKRL NYTLEEEKLS RRMMKYWANF ARTGNPNINV
     DGSIDSRRRW PVFTSTEQKH VGLNTDSLKV HKGLKSQFCA LWNRFLPRLL NVTENIDDAE
     RQWKAEFHRW SSYMMHWKNQ FDHYSKQERC TNL
//