D
IPR041751

PP2B, metallophosphatase domain

InterPro entry
Short nameMPP_PP2B
Overlapping
homologous
superfamilies
 
domain relationships

Description

PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands
[3]
.

The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes
[1, 2]
. PPPs belong to the metallophosphatase (MPP) superfamily.

References

1.The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Barford D, Das AK, Egloff MP. 27, 133-64, (1998). View articlePMID: 9646865

2.Protein phosphatases: structures and implications. Jia Z. Biochem. Cell Biol. 75, 17-26, (1997). View articlePMID: 9192069

3.A conserved docking surface on calcineurin mediates interaction with substrates and immunosuppressants. Rodriguez A, Roy J, Martinez-Martinez S, Lopez-Maderuelo MD, Nino-Moreno P, Orti L, Pantoja-Uceda D, Pineda-Lucena A, Cyert MS, Redondo JM. Mol. Cell 33, 616-26, (2009). View articlePMID: 19285944

Cross References

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