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acetylcholinesterase-associated collagen (acetylcholinesterase collagenic tail peptide, AChE Q subunit, COLQ)
Function:
1) component of the asymmetric form of AChE
2) anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina
3) proline-rich attachment domain (PRAD) binds the AChE catalytic subunits
4) triple-helical tail is stabilized by disulfide bonds at each end
5) may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay Homotrimer
Alternative splicing: named isoforms=8
Pathology:
- defects in COLQ result in end-plate acetylcholinesterase deficiency
General
oligomerizing protein
Properties
CONFIGURATION: trimer
SIZE: MW = 48 kD
entity length = 455 aa
MOTIF: signal sequence {1-22}
PRAD {51-67}
MOTIF: cysteine residue {C51}
MODIFICATION: cysteine residue {C-on-T}
cysteine residue {C52}
MODIFICATION: cysteine residue {C-on-T}
cysteine residue {C93}
MODIFICATION: cysteine residue {C93}
COLLAGEN-LIKE {96-269}
MOTIF: binding site
SITE: 130-133
FOR-BINDING-OF: heparan sulfate proteoglycan
binding site
SITE: 235-238
FOR-BINDING-OF: heparan sulfate proteoglycan
COLLAGEN-LIKE {277-291}
MOTIF: cysteine residue {C291}
MODIFICATION: cysteine residue {C291}
cysteine residue {C293}
MODIFICATION: cysteine residue {C293}
Database Correlations
OMIM correlations
MORBIDMAP 603033
UniProt Q9Y215
References
UniProt :accession Q9Y215