Phosphatidic acid phosphatases-like
IPR043216
Definition
This entry represents a group of membrane-associated phosphatidic acid phosphatases and their homologues mostly found in metazoa, fungi and plants. In budding yeasts there are two members, Lpp1 and Dpp1. Lpp1 catalyzes the Mg(2+)-independent dephosphorylation of phosphatidate (PA), diacylglycerol pyrophosphate (DGPP), and lysophosphatidate (LPA) PMID:10685032. Dpp1, a zinc-regulated enzyme that catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG) PMID:11139591. In humans, the members are phospholipid phosphatase 1-5 (PLPP1-5) and phospholipid phosphatase-related protein type 1-5 (PLPR1-5). PLPPs are magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters [[cite:PMID:10359651], [cite:PMID:16467304], [cite:PMID:17590538]]. PLPR1-5 may not have 2-lysophosphatidate/LPA phosphatase activity due to the lacking of critical residues supporting the reaction mechanism in active phosphatases of this phosphoesterase family. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity PMID:11278556. Another lipid phosphate phosphatase (LPP) homologue, Wunen, is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors PMID:12856002.
10 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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