Coatomer subunit epsilon
Function
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Post-translational modifications
Phosphorylated by PKA.
Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation.
Sequence Similarities
Belongs to the COPE family.
Cellular localization
- Cytoplasm
- Golgi apparatus membrane
- Peripheral membrane protein
- Cytoplasmic side
- Cytoplasmic vesicle
- COPI-coated vesicle membrane
- Peripheral membrane protein
- Cytoplasmic side
- The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.
Alternative names
Coatomer subunit epsilon, Epsilon-coat protein, Epsilon-COP, COPE