The PLAT domain (after polycystin-1, lipoxygenase and α toxin) is an intracellular domain of ~150 residues. The PLAT domain can be found associated with other domains such as LRR, PKD (see <PDOC50093>), C-type lectin (see <PDOC00537>), GPS (see <PDOC50221>), lipase, lipoxygenase (see <PDOC00077>) prokaryotic zinc-dependent phospholipase C (see <PDOC00357>), LCCL (see <PDOC50820>) or SRCR (see <PDOC00348>), It has been proposed that the PLAT domain may be involved in protein-protein and protein-lipid interaction [1,2].

The three-dimensional structure of the PLAT domain is known for several proteins. The domain is a β-sandwich composed of two sheets of four strands each (see <PDB:1LOX>). The most highly conserved regions of the PLAT domain coincide with the β-strands. Most of the highly conserved residues are buried residues. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth β-strand of all eukaryotic PLAT domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site within the PLAT domain [1].

Some proteins known to contain a PLAT domain are listed below:

• Animal polycystin-1 (PKD1). It may be an ion-channel. In human, defects in PKD1 are the cause of autosomal dominant polycystic kidney disease type I (ADPKD) that is characterized by progressive formation and enlargement of cysts in both kidneys, typically leading to end-stage renal disease in adult life. Cysts also occur in the liver and other organs.
• Eukaryotic lipoxygenase.
• Vertebrate lipoprotein lipase.
• Mammalian triacylglycerol lipase.
• Plasmodium falciparum PSLAP protein, a protein with multiple adhesive motifs that is expressed in gametocytes [2].
• Plasmodium berghei multidomain scavenger receptor protein PbSR.
• Bacterial α toxin.

The profile we developed covers the entire PLAT domain.