Phosphatase Subfamily MINPP1
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2: MINPP1
Contents
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
- 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.
- 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 |
