UniProt functional annotation for P21836



	UniProt functional annotation for P21836

UniProt code: P21836.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

Catalytic activity: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;

Subunit: Isoform 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}.

Subcellular location: Cell junction, synapse. Secreted. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.

Subcellular location: [Isoform H]: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side.

Tissue specificity: Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.

Miscellaneous: Synapses 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.

Miscellaneous: This is the catalytic subunit of an asymmetric or soluble form of ACHE.

Similarity: Belongs to the type-B carboxylesterase/lipase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.


Catalytic activity:		Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7;
Subunit:		Isoform 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}.
Subcellular location:		Cell junction, synapse. Secreted. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Subcellular location:		[Isoform H]: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side.
Tissue specificity:		Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.
Miscellaneous:		Synapses 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.
Miscellaneous:		This is the catalytic subunit of an asymmetric or soluble form of ACHE.
Similarity:		Belongs to the type-B carboxylesterase/lipase family. {ECO:0000305}.