| abstract |
UBA-like autoinhibitory domain (AID) found in vertebrate 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPKalpha-2). AMPKalpha-2, also called acetyl-CoA carboxylase kinase (ACACA kinase) or hydroxymethylglutaryl-CoA reductase kinase (HMGCR kinase), is one of the catalytic subunits of adenosine monophosphate (AMP)-activated protein kinase (AMPK). It shows a wide expression pattern and is highly expressed in skeletal muscle, heart, and liver. It may be involved in the regulation of glucose and lipid metabolism and protein synthesis in peripheral tissues, as well as in regulation of energy intake and body weight. AMPKalpha-2 has an N-terminal Ser/Thr kinase domain followed by an ubiquitin-associated (UBA)-like AID, and a C-terminal AMPK regulatory domain. The Ser/Thr kinase domain contains a conserved Thr residue that must be phosphorylated for activity in the activation loop. The AID is responsible for AMPKalpha subunit autoinhibition. The C-terminal regulatory domain is essential for binding the beta- and gamma-subunits. |