In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by;non-clathrin-coated vesicular coat proteins (COPs). Seven coat proteins have been identified, and they represent;subunits of a complex known as coatomer. The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP,;delta-COP, epsilon-COP, and zeta-COP. The alpha-COP, encoded by COPA, shares high sequence similarity with RET1P, the;alpha subunit of the coatomer complex in yeast. Also, the N-terminal 25 amino acids of alpha-COP encode the bioactive;peptide, xenin, which stimulates exocrine pancreatic secretion and may act as a gastrointestinal hormone. Alternative;splicing results in multiple splice forms encoding distinct isoforms.
COPA; coatomer protein complex subunit alpha; Alpha coat protein; Alpha COP; Alpha COPI; AlphaCOP; Coatomer subunit alpha; COP A; COP I alpha; COPI alpha; FLJ26320; HEP COP; HEPCOP; Proxenin; Xenin; Xenopsin-related peptide; coatomer protein complex, subunit alpha; cb281; fb13c12; wu:fb13c12; sneezy