UniProt functional annotation for Q9Y215



	UniProt functional annotation for Q9Y215

UniProt code: Q9Y215.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.

Subunit: 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). {ECO:0000269|PubMed:15526038}.

Subcellular location: Cell junction, synapse.

Tissue specificity: Found at the end plate of skeletal muscle.

Domain: The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.

Ptm: The triple-helical tail is stabilized by disulfide bonds at each end.

Disease: Myasthenic syndrome, congenital, 5 (CMS5) [MIM:603034]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS5 inheritance is autosomal recessive. {ECO:0000269|PubMed:10665486, ECO:0000269|PubMed:11865139, ECO:0000269|PubMed:24938146, ECO:0000269|PubMed:9758617}. Note=The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous: [Isoform VII]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.

Similarity: Belongs to the COLQ family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.


Subunit:		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). {ECO:0000269\|PubMed:15526038}.
Subcellular location:		Cell junction, synapse.
Tissue specificity:		Found at the end plate of skeletal muscle.
Domain:		The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.
Ptm:		The triple-helical tail is stabilized by disulfide bonds at each end.
Disease:		Myasthenic syndrome, congenital, 5 (CMS5) [MIM:603034]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS5 inheritance is autosomal recessive. {ECO:0000269\|PubMed:10665486, ECO:0000269\|PubMed:11865139, ECO:0000269\|PubMed:24938146, ECO:0000269\|PubMed:9758617}. Note=The disease is caused by variants affecting the gene represented in this entry.
Miscellaneous:		[Isoform VII]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.
Similarity:		Belongs to the COLQ family. {ECO:0000305}.