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Protein phosphatase 2C (PP2C) is one of the four major classes of mammalian serine/threonine specific protein phosphatases (EC 3.1.3.16). PP2C [1] is a monomeric enzyme of about 42 Kd which shows broad substrate specificity and is dependent on divalent cations (mainly manganese and magnesium) for its activity. Its exact physiological role is still unclear. Three isozymes are currently known in mammals: PP2C-α, -β and -γ. In yeast, there are at least four PP2C homologs: phosphatase PTC1 [2] which has 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 (ABI1, PPH1), Caenorhabditis elegans (FEM-2, F42G9.1, T23F11.1), Leishmania chagasi and Paramecium tetraurelia.

In Arabidopsis thaliana, the kinase associated protein phosphatase (KAPP) [3] is an enzyme that dephosphorylates the Ser/Thr receptor-like kinase RLK5 and which contains a C-terminal PP2C domain.

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 (lipoamide)-phosphatase (EC 3.1.3.43) (PDPC) [4], which catalyzes dephosphorylation and concomitant reactivation of the α subunit of the E1 component of the pyruvate dehydrogenase complex. PDPC is a mitochondrial enzyme and, like PP2C, is magnesium-dependent.

As a signature pattern, we selected the best conserved region which is located in the N-terminal part and contains a perfectly conserved tripeptide. This region includes a conserved aspartate residue involved in divalent cation binding [5].

PP2C belongs [6] to a superfamily which also includes bacterial proteins such as Bacillus spoIIE, rsbU and rsbW, Synechocystis PCC 6803 icfG as well as a domain in fungal adenylate cyclases.

May 2004 / Text revised.

PROSITE method (with tools and information) covered by this documentation:

PP2C, PS01032; Protein phosphatase 2C signature  (PATTERN)

Consensus pattern: [LIVMFY]-[LIVMFYA]-[GSAC]-[LIVM]-[FYC]-D-G-H-[GAV] The D is a manganese ligand Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01032 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01032 • Scan Swiss-Prot/TrEMBL entries against PS01032 • view ligand binding statistics

Matching PDB structures: 1A6Q 2IQ1 2P8E 2PNQ ... [ALL]

1	Authors	Wenk J., Trompeter H.-I., Pettrich K.-G., Cohen P.T.W., Campbell D.G., Mieskes G.
	Title	Molecular cloning and primary structure of a protein phosphatase 2C isoform.
	Source	FEBS Lett. 297:135-138(1992).
	PubMed ID	1312947

2	Authors	Maeda T., Tsai A.Y.M., Saito H.
	Title	Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae.
	Source	Mol. Cell. Biol. 13:5408-5417(1993).
	PubMed ID	8395005

3	Authors	Stone J.M., Collinge M.A., Smith R.D., Horn M.A., Walker J.C.
	Title	Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase.
	Source	Science 266:793-795(1994).
	PubMed ID	7973632

4	Authors	Lawson J.E., Niu X.-D., Browning K.S., Trong H.L., Yan J., Reed L.J.
	Title	Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C.
	Source	Biochemistry 32:8987-8993(1993).
	PubMed ID	8396421

5	Authors	Das A.K., Helps N.R., Cohen P.T.W., Barford D.
	Title	Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
	Source	EMBO J. 15:6798-6809(1996).
	PubMed ID	9003755

6	Authors	Bork P., Brown N.P., Hegyi H., Schultz J.
	Title	The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues.
	Source	Protein Sci. 5:1421-1425(1996).
	PubMed ID	8819174

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