ACHE (P22303) - Overview - Molecular Target Synopsis
Enzyme Classification 188.8.131.52
Also Known as ACES_HUMAN, ACHE
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). 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. Isoform R may be monomeric.
|Protein Length||Ensembl Gene||Ensembl Transcript||Ensembl Protein||Uniprot Isoform|
|617||ENSG00000087085||ENST00000411582, ENST00000302913||ENSP00000404865, ENSP00000303211||P22303-2|
|614||ENSG00000087085||ENST00000428317, ENST00000412389, ENST00000241069||ENSP00000414858, ENSP00000394976, ENSP00000241069||P22303-1|
UniProt: ACHE is active in the following subcellular-locations: cell junction, cell membrane, nucleus, secreted, synapse.
GO terms: ACHE is active in the following subcellular-locations: anchored component of membrane, basement membrane, cell junction, cell surface, extracellular region, extracellular space, Golgi apparatus, membrane, neuromuscular junction, nucleus, perinuclear region of cytoplasm, plasma membrane, synapse, synaptic cleft.