LMPD Database

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LMP002757

UniProt Annotations

Entry Information
Gene Nameacetylcholinesterase
Protein EntryACES_MOUSE
UniProt IDP21836
SpeciesMouse
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=T; IsoId=P21836-1; Sequence=Displayed; Name=H; IsoId=P21836-2; Sequence=Not described; Note=No experimental confirmation available.;
Catalytic ActivityAcetylcholine + H(2)O = choline + acetate.
FunctionTerminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
MiscellaneousSynapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.
MiscellaneousThis is the catalytic subunit of an asymmetric or soluble form of ACHE.
SimilarityBelongs to the type-B carboxylesterase/lipase family. {ECO:0000305}.
Subcellular LocationCell junction, synapse. Secreted. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Subcellular LocationIsoform H: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side.
SubunitIsoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers (By similarity). Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers. {ECO:0000250, ECO:0000269|PubMed:11804574, ECO:0000269|PubMed:12505979}.
Tissue SpecificityPredominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.