ID   ACES_MYXGL              Reviewed;         338 AA.
AC   Q92081;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Fragment;
GN   Name=ache; Synonyms=ace1;
OS   Myxine glutinosa (Atlantic hagfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC   Myxiniformes; Myxinidae; Myxininae; Myxine.
OX   NCBI_TaxID=7769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8896335; DOI=10.1016/0305-0491(96)00088-0;
RA   Sanders M., Mathews B., Sutherland D., Soong W., Giles H., Pezzementi L.;
RT   "Biochemical and molecular characterization of acetylcholinesterase from
RT   the hagfish Myxine glutinosa.";
RL   Comp. Biochem. Physiol. 115B:97-110(1996).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U55003; AAB17025.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92081; -.
DR   SMR; Q92081; -.
DR   MEROPS; S09.980; -.
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; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR000997; Cholinesterase.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Secreted; Serine esterase; Synapse.
FT   CHAIN           <1..>338
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000070279"
FT   ACT_SITE        99
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        153..164
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         338
SQ   SEQUENCE   338 AA;  37300 MW;  ADDCEA493D582BA2 CRC64;
     VPSPRPQNAT VMVWIFGGGF AYGTSSLNVY DGRYLAQAEG AIVVSMNYRV GALGFLSLPG
     SPVPGNAGLF DQQLALRWVH GNIHRFGGNP QSVTLFGESA GSASVAPHLL SRHSQQFFQR
     AILQSGTLNA PWATVEDTEA RRRAEALAQA LGCPTDDDNE LLNCLYARPP QEIVSKEGDV
     VIEPSIFRFP FVPVVDGHFI IDSPIVLLQQ GIFKKTDLLL GVNRNEGSFF LIYGAPGFSK
     DHESLISRED FLENIPMIVP QGNEVSVDAI VLQYTDWLAQ NDALKNRDAI EDIVGDYNVI
     CPVVEMATRY AEFGNNVYFY FFNQRASNLP WPQWMGVI