| Type: | Conserved_site | Name: | Lysophospholipase patatin, conserved site |
| Description: | Lysophospholipase NTE1 was identified in yeast as an endoplasmic reticulum integral membrane protein that acts as a phospholipase B, catalysing the double deacylation of phosphatidylcholine to glycerophosphocholine []. Phosphatidylcholine is the major phospholipid component of eukaryotic membranes. NTE1 plays an important role in membrane lipid homeostasis, and is responsible for the rapid phosphatidylcholine turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium. NTE1-mediated phosphatidylcholine deacylation is strongly affected by Sec14p, a component of the yeast secretory machinery involved in lipid metabolism and vesicular trafficking.The mammalian and Drosophila homologues of NTE1, neuropathy target esterase and swiss cheese, respectively, have been implicated in normal brain development []. The absence of these proteins is associated with increased cytoplasmic vesicularisation and multi-layered membrane stacks.NTE1 contains two cyclic nucleotide-binding domains and a patatin domain. This entry represents the patatin domain. | Short Name: | LysoPLipase_patatin_CS |
