UBA-like autoinhibitory domain (AID) found in vertebrate 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPKalpha-1)
AMPKalpha-1, also called acetyl-CoA carboxylase kinase (ACACA kinase), hydroxymethylglutaryl-CoA reductase kinase (HMGCR kinase), or Tau-protein kinase PRKAA1, is one of the catalytic subunits of adenosine monophosphate (AMP)-activated protein kinase (AMPK). It has been implicated in a number of important cellular processes. For instance, it functions as a glucose sensor controlling CD8 T-cell memory, as well as a new kinase for RhoA and a new mediator of the vasoprotective effects of estrogen. It also plays a significant role in cervical malignant growth, in regulating oxidative stress and life span in erythrocytes, in modulating the antioxidant status of vascular endothelial cells, in limiting skeletal muscle overgrowth during hypertrophy through inhibition of the mammalian target of rapamycin (mTOR)-signaling pathway. AMPKalpha-1 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 of the alpha1-subunit is essential for binding the beta1- and gamma1-subunits.
Jiyao W et al.(2023). "The conserved domain database in 2023.",