Protein phosphatase 2C
IPR015655
Definition
Protein phosphatase 2C (PP2C) is one of the four major classes of mammalian serine/threonine specific protein phosphatases ([ec:3.1.3.16]). PP2C PMID:1312947 is a monomeric enzyme of about 42kDa, that shows broad substrate specificity and is dependent on divalent cations (mainly manganese and magnesium) for its activity. The exact physiological role is still unclear. Three isozymes are currently known in mammals: PP2C-alpha, -beta and -gamma. In yeast, there are at least four PP2C homologues: phosphatase PTC1 PMID:8395005 that have weak tyrosine phosphatase activity in addition to its activity on serines, phosphatases PTC2 and PTC3, and hypothetical protein YBR125c. Isozymes of PP2C are also known from Arabidopsis thaliana (Mouse-ear cress) (ABI1, PPH1), Caenorhabditis elegans (FEM-2, F42G9.1, T23F11.1), Leishmania chagasi and Paramecium tetraurelia. In A. thaliana, the kinase associated protein phosphatase (KAPP) PMID:7973632 is an enzyme that dephosphorylates the Ser/Thr receptor-like kinase RLK5 and contains a C-terminal PP2C domain. This family also includes a broad spectrum phosphatase PP1M PMID:18930133 and Fem-2 which dephosphorylates auto-phosphorylated Ca2+/calmodulin-dependent protein kinase unc-43/CAMKII PMID:11559703. PP2C does not seem to be evolutionary related to the main family of serine/ threonine phosphatases: PP1, PP2A and PP2B. However, it is significantly similar to the catalytic subunit of pyruvate dehydrogenase phosphatase ([ec:3.1.3.43]) (PDPC) PMID:8396421, which catalyses dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. PDPC is a mitochondrial enzyme and, like PP2C, is magnesium-dependent.
17 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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