ID   ACES_RABIT              Reviewed;         584 AA.
AC   Q29499;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor; Fragment;
GN   Name=ACHE;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=7925428; DOI=10.1111/j.1432-1033.1994.00115.x;
RA   Jbilo O., L'Hermite Y., Talesa V., Toutant J.-P., Chatonnet A.;
RT   "Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit
RT   tissues and during development.";
RL   Eur. J. Biochem. 225:115-124(1994).
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   -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers.
CC       Interacts with PRIMA1. The interaction with PRIMA1 is required to
CC       anchor it to the basal lamina of cells and organize into tetramers (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Synapses usually contain asymmetric molecules of
CC       cholinesterase, with a collagen-like part disulfide-bonded to the
CC       catalytic part. A different, globular type of cholinesterase occurs on
CC       the outer surfaces of cell membranes, including those of erythrocytes.
CC   -!- MISCELLANEOUS: This is the catalytic subunit of an asymmetric or
CC       soluble form of ACHE.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; U05036; AAA53235.1; -; mRNA.
DR   PIR; S48724; S48724.
DR   AlphaFoldDB; Q29499; -.
DR   SMR; Q29499; -.
DR   ESTHER; rabit-ACHE; AChE.
DR   MEROPS; S09.979; -.
DR   InParanoid; Q29499; -.
DR   Proteomes; UP000001811; 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; IPR014788; AChE_tetra.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   Pfam; PF08674; AChE_tetra; 1.
DR   Pfam; PF00135; COesterase; 1.
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; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Reference proteome; Secreted;
KW   Serine esterase; Signal; Synapse.
FT   SIGNAL          <1..1
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..584
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008589"
FT   ACT_SITE        204
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        335
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        448
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        70..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..273
FT                   /evidence="ECO:0000250"
FT   DISULFID        410..530
FT                   /evidence="ECO:0000250"
FT   DISULFID        581
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   584 AA;  64630 MW;  2AE157F3063649FE CRC64;
     AEGREDPELL VTVRGGRLRG LRLKAPGGPV SAFLGIPFEE PPVGPRRFLP PEPKRPWAGV
     LDATAFQSVC YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPT SPTPVLVWIY
     GGGFYSGASS LDVYYGRFLV QAEGTVLVAM NYRVGAFGFT CLPGSREAPG NVGLLDQRLA
     LQWVQENVAA FGGDPASVTL FGESAGAASV GLHLLSPPSR GLFHRAVLQS GAPNGPWATV
     GVGEARRRAT LLARLVVCPP GGAGGNDTEL VACLRTRPAQ DLVDHEWRVL PQESIFRFSF
     VPVVDGDFLS DTPEALINAG DFQGLQVLVG VVKDEGTYFL VYGAPGFSKD NESFISRAQF
     LAGVRVGVPQ ASDLAAEAVV LHYTDWLHPE DPARLRDALS DVVGDHNVVC PVAQLAGRLA
     AQGARVYAYV FEHRASTLSW PLWMGVPHGY EIEFIFGLPL EPSLNYTEEE RIFAQRLMRY
     WANFARTGDP NEPRDAKAPQ WPPYTAGAQQ YVSLNLRPLE VRRGLRAQAC AFWNRFLPKL
     LSATDTLDEA ERQWKAEFHR WSSYMVHWKN QFDHYSKQDR CSDL