Difference between revisions of "Phosphatase Subfamily MINPP1"
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| − | 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) <cite>ali93, chi00</cite>. MIPP1 does not display any phosphoglycerate mutase activity. Human MIPP1 has biologically significant 2,3-BPG phosphatase activity <cite>cho08</cite>. However, [[Phosphatase_Subfamily_TIGAR|TIGAR]] of HP2 family also dephosphorylates 2,3-BPG <cite></cite>. | + | 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) <cite>ali93, chi00</cite>. MIPP1 does not display any phosphoglycerate mutase activity. Human MIPP1 has biologically significant 2,3-BPG phosphatase activity <cite>cho08</cite>. However, [[Phosphatase_Subfamily_TIGAR|TIGAR]] of HP2 family also dephosphorylates 2,3-BPG <cite>Gerin14</cite>. |
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. | 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. | ||
Revision as of 21:09, 2 June 2015
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]. However, TIGAR of HP2 family also dephosphorylates 2,3-BPG [4].
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
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