Protein Phosphatase, Mg2+/Mn2+ Dependent 1L (PPM1L)

PPM1L, or PP2CE, belongs to the PP2C group of serine/threonine phosphatases, which are distinguished from other phosphatases by their structure, absolute requirement for Mg(2+) or Mn(2+), and insensitivity to okadaic acid. PP2Cs regulate stress-activated protein kinase signaling cascades that respond to extracellular stimuli . The deduced 360-amino acid protein has a calculated molecular mass of 41 kD. Like other PP2Cs, PP2CE contains a PP2C catalytic domain, unique N- and C-terminal domains, and several highly conserved residues for Mg(2+)/Mn(2+) binding. Human PP2CE shares 99% identity with the mouse and rat Pp2ce proteins, which also contain 360 amino acids. RT-PCR detected highest PP2CE expression in human heart, placenta, lung, liver, kidney, and pancreas, with lower expression in colon, leukocytes, testis, and brain.