SACS
Domain
The ubiquitin-like domain mediates interaction with the proteasome.
The J domain is functional and is shown to stimulate E.coli dnaK ATPase activity.
Function
Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins.
Involvement in disease
Spastic ataxia Charlevoix-Saguenay type
SACS
A neurodegenerative disease characterized by early-onset cerebellar ataxia, spasticity, retinal hypermyelination, pyramidal signs, and both axonal and demyelinating neuropathy with loss of sensory nerve conduction and reduced motor conduction velocities. Other features include dysarthria, distal muscle wasting, nystagmus, defect in conjugate pursuit ocular movements, retinal striation (from prominent retinal nerves) obscuring the retinal blood vessels in places, and the frequent presence of mitral valve prolapse.
None
The disease is caused by variants affecting the gene represented in this entry.
Tissue Specificity
Highly expressed in the central nervous system. Also found in skeletal muscle and at low levels in pancreas.
Cellular localization
- Cytoplasm
- Predominantly cytoplasmic, a small portion is present in the nucleus and also shows a partial mitochondrial overlap with the mitochondrial marker Hsp60.
Alternative names
DNAJC29, KIAA0730, SACS, Sacsin, DnaJ homolog subfamily C member 29