Short coiled-coil protein (SCOC)

Short coiled-coil protein (SCOC) is a small, widely expressed human protein containing a parallel left-handed coiled-coil domain. SCOC is primarily known for forming a complex with fasciculation and elongation protein zeta 1 (FEZ1); this complex is important for the regulation of autophagy and for axonal outgrowth and presynaptic organization, especially in neuronal tissues. SCOC acts as an effector of the Golgi resident GTPase Arl1 and physiologically is most abundant in brain, heart, and skeletal muscle. The coiled-coil domain is highly conserved, facilitating dimerization and critical protein-protein interactions. In *C. elegans*, loss or mutation of the SCOC homolog (UNC-69) results in severe neurodevelopmental defects, suggesting an essential role in neural circuit formation. There are at least four known human SCOC isoforms with variable N-termini but a conserved coiled-coil region. Current evidence does not indicate direct roles for SCOC as a classical drug target or as a biomarker, and no drugs are reported to interact with this protein. SCOC is not a receptor, enzyme, or transporter, but rather a structural interaction hub involved in essential cell biological processes. No approved drugs or drugs in development are currently reported to modulate SCOC or its direct pathway. Its role in human disease is primarily inferred from model organisms and relates to neural development and autophagy, but there is no strong evidence for a direct association with major clinical diseases in humans. Referenced information is synthesized primarily from crystal structure studies and functional investigations in human cells and model organisms.

Other names

SCOCOHRIHFB2072UNC-69