Phosphatidate phosphatase PAH1; Magnesium-dependent phosphatidate phosphatase which catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol. Acts redundantly with PAH2 to repress phospholipid biosynthesis at the endoplasmic reticulum (ER). May function indirectly as repressor of multiple enzymes involved in phospholipid biosynthesis. Is involved in the pathway of galactolipid synthesis in the ER, which is required for the membrane lipid remodeling, an essential adaptation mechanism to cope with phosphate starvation; Belongs to the lipin family (904 aa)

Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein; Protein serine/threonine phosphatases;protein kinases;catalytics;cAMP-dependent protein kinase regulators;ATP binding;protein serine/threonine phosphatases; Its function is described as cAMP-dependent protein kinase regulator activity, protein kinase activity, protein serine/threonine phosphatase activity, catalytic activity, ATP binding; Involved in protein amino acid phosphorylation, protein amino acid dephosphorylation, N-terminal protein myristoylation, regulation of protein amino acid phosphoryl [...] (1094 aa)

Lysophospholipid acyltransferase LPEAT2; Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates. Exhibits strong acylation activity of lysophosphatidylethanolamine (LPE) and lower activity on lysophosphatidate (LPA). Has a preference for 18-1-LPE over 16-0- LPE as acceptor and palmitoyl-CoA (16-0-CoA) as acyl donor. Activity is calcium-independent; Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family (539 aa)

Pumilio homolog 24; Encodes a member of the Arabidopsis Pumilio (APUM) proteins containing PUF domain (eight repeats of approximately 36 amino acids each). PUF proteins regulate both mRNA stability and translation through sequence-specific binding to the 3’ UTR of target mRNA transcripts (641 aa)

Serine/threonine-protein phosphatase PP2A-5 catalytic subunit; Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B’ to positively regulates beta- oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins. Involved in the positive regulation of salt stress responses. May function by increasing chloride channel activities on vacuolar membranes; Belongs to the PPP phosphatase family. PP-2A subfamily (307 aa)

Encodes one of the isoforms of the catalytic subunit of protein phosphatase 2A- AT1G59830/PP2A-1, AT1G10430/PP2A-2, At2g42500/PP2A-3, At3g58500/PP2A-4 [Plant Molecular Biology (1993) 21-475-485 and (1994) 26-523-528; Note that in more recent publications, there is mixed use of gene names for PP2A-3 and PP2A-4 - some refer to At2g42500 as PP2A-3 and some as PP2A-4] (306 aa)

Serine/threonine-protein phosphatase PP2A-4 catalytic subunit; Functions redundantly with PP2A3, and is involved in establishing auxin gradients, apical-basal axis of polarity and root and shoot apical meristem during embryogenesis. May dephosphorylate PIN1 and regulate its subcellular distribution for polar auxin transport. The holoenzyme composed of PP2AA1, PP2A4 and B’ZETA or B’ETA acts as negative regulator of plant innate immunity by controlling BAK1 phosphorylation state and activation in surface-localized immune receptor complexes; Belongs to the PPP phosphatase family. PP-2A su [...] (313 aa)

Serine/threonine-protein phosphatase PP2A-3 catalytic subunit; Functions redundantly with PP2A3, and is involved in establishing auxin gradients, apical-basal axis of polarity and root and shoot apical meristem during embryogenesis. May dephosphorylate PIN1 and regulate its subcellular distribution for polar auxin transport. The holoenzyme composed of PP2AA1, PP2A4 and B’ZETA or B’ETA acts as negative regulator of plant innate immunity by controlling BAK1 phosphorylation state and activation in surface-localized immune receptor complexes; Belongs to the PPP phosphatase family. PP-2A su [...] (313 aa)