PP2Cγ: a human protein phosphatase with a unique acidic domain

We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from Paramecium tetraurelia and Schizosaccharomyces pombe than mammalian PP2...

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Bibliographic Details
Published in:FEBS letters 1997-08, Vol.412 (3), p.415-419
Main Authors: Travis, Sue M, Welsh, Michael J
Format: Article
Language:English
Subjects:
acidic domain
Amino Acid Sequence
Animals
cDNA
Cloning, Molecular
Enzyme Activation
Humans
Mice
Molecular Sequence Data
Organ Specificity
Paramecium - enzymology
Paramecium - genetics
Phosphoprotein Phosphatases - chemistry
Phosphoprotein Phosphatases - genetics
Phosphoprotein Phosphatases - isolation & purification
Phylogeny
Protein Phosphatase 2
Protein Phosphatase 2C
Protein phosphorylation
Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins
Sequence Analysis, DNA
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Summary:We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from Paramecium tetraurelia and Schizosaccharomyces pombe than mammalian PP2Cs. Northern blot analysis shows that PP2Cγ is widely expressed, and is most abundant in testis, skeletal muscle, and heart. Like known PP2Cs, recombinant PP2Cγ requires Mg 2+ or Mn 2+ for activity. Unlike any other known phosphatase, PP2Cγ has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00837-5