Difference between revisions of "Phosphatase Subfamily ACP6"
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Human ACP6 is a lysophosphatidic acid (LPA)-specific acid phosphatase that hydrolyzes LPA to monoacylglycerol (MAG) and phosphate <cite>Li13</cite>. LPA is a phospholipid involved in cell signaling as a secreted ligand for GPCRs. It is also involved in balancing the lipid composition inside the cell, and modulates the function of lipid rafts as an intermediate in phospholipid metabolism. LPA synthesis occurs through a number of pathways; LPA degradation occurs through three known pathways, including one through ACP6 <cite>Li13</cite>. | Human ACP6 is a lysophosphatidic acid (LPA)-specific acid phosphatase that hydrolyzes LPA to monoacylglycerol (MAG) and phosphate <cite>Li13</cite>. LPA is a phospholipid involved in cell signaling as a secreted ligand for GPCRs. It is also involved in balancing the lipid composition inside the cell, and modulates the function of lipid rafts as an intermediate in phospholipid metabolism. LPA synthesis occurs through a number of pathways; LPA degradation occurs through three known pathways, including one through ACP6 <cite>Li13</cite>. | ||
| − | ACP6 is localized in the mitochondria with ubiquitous expression throughout all tissues, and high expression levels in kidney, heart, small intestine, muscle, and liver <cite> Hiroyama99 | + | ACP6 is localized in the mitochondria with ubiquitous expression throughout all tissues, and high expression levels in kidney, heart, small intestine, muscle, and liver <cite> Hiroyama99 </cite>. |
=== References === | === References === | ||
Revision as of 22:49, 25 October 2016
Phosphatase Classification: Fold HP: Superfamily HP: Family HP, branch 2: Subfamily ACP6
Evolution
The ACP6 subfamily is found across holozoa and absent from ecdysozoa. Both Drosophila and C. elegans lack ACP6, but both have expansions in the analogous ACP2 subfamily. The ACP6 subfamily is also absent from S. cerevisiae but present in some other fungi, and detectable in some other basal eukaryotes.
Domain
The ACP6 subfamily has a single structural domain, the phosphatase domain. It also has a signal peptide at N-terminal which may target it to mitochondria [1].
Function
Human ACP6 is a lysophosphatidic acid (LPA)-specific acid phosphatase that hydrolyzes LPA to monoacylglycerol (MAG) and phosphate [2]. LPA is a phospholipid involved in cell signaling as a secreted ligand for GPCRs. It is also involved in balancing the lipid composition inside the cell, and modulates the function of lipid rafts as an intermediate in phospholipid metabolism. LPA synthesis occurs through a number of pathways; LPA degradation occurs through three known pathways, including one through ACP6 [2].
ACP6 is localized in the mitochondria with ubiquitous expression throughout all tissues, and high expression levels in kidney, heart, small intestine, muscle, and liver [1].
References
- Hiroyama M and Takenawa T. Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis. J Biol Chem. 1999 Oct 8;274(41):29172-80. DOI:10.1074/jbc.274.41.29172 |
- Li J, Dong Y, Lü X, Wang L, Peng W, Zhang XC, and Rao Z. Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6. Protein Cell. 2013 Jul;4(7):548-61. DOI:10.1007/s13238-013-3031-z |
