Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina. Homotrimer. Component of the asymmetric form of AChE, a disulfide-bonded oligomer composed of the collagenic subunits (Q) and a variable number of asymmetric catalytic subunits (T). The N-terminal of a collagenic subunit (Q) associates with the C-terminal of a catalytic subunit (T). Found at the end plate of skeletal muscle. The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits. The triple-helical tail is stabilized by disulfide bonds at each end. The disease is caused by variants affecting the gene represented in this entry. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the COLQ family.