Patatin-like phospholipase domain-containing protein 7 (PNPLA7)

Patatin-like phospholipase domain-containing protein 7 (PNPLA7) is an endoplasmic reticulum-anchored transmembrane enzyme that specifically hydrolyzes lysophosphatidylcholine (LPC) and other lysophospholipids in mammalian cells. It plays an essential role in cellular lipid metabolism, energy balance, and immune modulation, particularly through its impact on macrophage polarization and inflammatory responses. PNPLA7 shares homology with PNPLA6 (neuropathy target esterase) and is expressed in a range of tissues, including skeletal muscle, heart, adipose tissue, and testis. Its enzymatic activity is critical for controlling intracellular LPC levels, and its function is regulated by nutritional and hormonal status such as insulin. Although alterations in PNPLA7 may be implicated in metabolic and neurodegenerative diseases, its precise roles in disease pathophysiology and therapeutic potential remain under investigation.

Other names

C9orf111FLJ43070FLJ31318FLJ44279RP11-48C7.2NTEL1NTE-R1patatin-like phospholipase domain-containing protein 7patatin-like domain 7 lysophospholipasePNPLA7

Hydrolysis of lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine to regulate lipid levels; Modulation of SIRT1/NF-κB- and p38 MAPK-dependent pathways in immune cells