Phosphatase Subfamily MINPP1

Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2: MINPP1

MINPP1 is a non-protein phosphatase found in a broad of eukaryotes, including most metazoan and amoebazoan.

Evolution

MINPP1 is found broadly in eukaryotes but absent from many genomes, such as C elegans. Human has a single copy, but yeast have as many as five copies.

Domain

MINPP1 has phosphatase domain and N-terminal signal peptide cleavage site.

Functions

Human MINPP1 is the only hitherto known InsP6 phosphatase. It has been shown to be predominantly localized in the lumen of the ER (endoplasmatic reticulum) [1, 2]. MIPP1 does not display any phosphoglycerate mutase activity. Human MIPP1 has biologically significant 2,3-BPG phosphatase activity [3].

Yeast has as many as five MINPP1s, including PHO3, PHO5, PHO11, PHO12 and DIA3. The first four have been known to be involved in phosphate metabolism.

Dictyostelium Mipp1 shows 2,3-BPG phosphatase activity in vitro and in vivo [3].

References

1. Ali N, Craxton A, and Shears SB. Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside endoplasmic reticulum. J Biol Chem. 1993 Mar 25;268(9):6161-7.
2. Chi H, Yang X, Kingsley PD, O'Keefe RJ, Puzas JE, Rosier RN, Shears SB, and Reynolds PR. Targeted deletion of Minpp1 provides new insight into the activity of multiple inositol polyphosphate phosphatase in vivo. Mol Cell Biol. 2000 Sep;20(17):6496-507. DOI:10.1128/MCB.20.17.6496-6507.2000 |
3. Cho J, King JS, Qian X, Harwood AJ, and Shears SB. Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. Proc Natl Acad Sci U S A. 2008 Apr 22;105(16):5998-6003. DOI:10.1073/pnas.0710980105 |