COLQ, EAD, CMS5, collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase, collagen like tail subunit of asymmetric acetylcholinesterase
Acetylcholinesterase collagenic tail peptide also known as AChE Q subunit, acetylcholinesterase-associated collagen, or ColQ is the collagen-tail subunit of
acetylcholinesterase found in the
neuromuscular junction. In humans it is encoded by the COLQgene.[5][6]
Function
This gene encodes the subunit of a
collagen-like molecule associated with
acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a
proline-rich attachment domain (PRAD) that binds an acetylcholinesterase
tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Multiple
transcript variants encoding different
isoforms have been found for this gene.[6]
Clinical significance
Mutations in this gene are associated with endplate acetylcholinesterase deficiency[6] and one of the causes of the neuromuscular disease,
congenital myasthenia gravis.[7]
Altamirano CV, Lockridge O (1999). "Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers". Biochemistry. 38 (40): 13414–22.
doi:
10.1021/bi991475+.
PMID10529218.
Shapira YA, Sadeh ME, Bergtraum MP, et al. (2002). "Three novel COLQ mutations and variation of phenotypic expressivity due to G240X". Neurology. 58 (4): 603–9.
doi:
10.1212/wnl.58.4.603.
PMID11865139.
S2CID43142424.
COLQ, EAD, CMS5, collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase, collagen like tail subunit of asymmetric acetylcholinesterase
Acetylcholinesterase collagenic tail peptide also known as AChE Q subunit, acetylcholinesterase-associated collagen, or ColQ is the collagen-tail subunit of
acetylcholinesterase found in the
neuromuscular junction. In humans it is encoded by the COLQgene.[5][6]
Function
This gene encodes the subunit of a
collagen-like molecule associated with
acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a
proline-rich attachment domain (PRAD) that binds an acetylcholinesterase
tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Multiple
transcript variants encoding different
isoforms have been found for this gene.[6]
Clinical significance
Mutations in this gene are associated with endplate acetylcholinesterase deficiency[6] and one of the causes of the neuromuscular disease,
congenital myasthenia gravis.[7]
Altamirano CV, Lockridge O (1999). "Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers". Biochemistry. 38 (40): 13414–22.
doi:
10.1021/bi991475+.
PMID10529218.
Shapira YA, Sadeh ME, Bergtraum MP, et al. (2002). "Three novel COLQ mutations and variation of phenotypic expressivity due to G240X". Neurology. 58 (4): 603–9.
doi:
10.1212/wnl.58.4.603.
PMID11865139.
S2CID43142424.