Lanthionine synthetase C-like protein 1 (LANCL1)

Lanthionine synthetase C-like protein 1 (LANCL1) is a mammalian peripheral membrane protein homologous to bacterial lanthionine synthetase components involved in peptide modification. In humans, LANCL1 functions as a putative glutathione transferase, binding glutathione (GSH) at a zinc-dependent site and demonstrating enzymatic activity toward some artificial substrates. It is most abundantly expressed in the brain and testis, with major roles in protecting neurons against oxidative stress, regulating redox homeostasis, and modulating survival pathways, notably through AKT signaling, especially under neurodegenerative conditions such as ALS. LANCL1 also interacts with SH3-domain-containing scaffold proteins like Eps8, influencing neurite outgrowth and differentiation in response to growth factors such as NGF. Although previously annotated as a G protein-coupled receptor (GPR69A), current evidence argues against this classification in humans, and LANCL1 is now more accurately placed within the lanthionine synthetase family. No clinically approved drugs are known to specifically target LANCL1, but it is under investigation as a potential neuroprotective therapeutic target. Loss of LANCL1 function is associated with increased neuronal apoptosis, oxidative damage, and neuroinflammation in animal models.

Other names

GPR69Ap40Glutathione S-transferase LANCL140 kDa erythrocyte membrane proteinLanC-like protein 1G protein-coupled receptor 69ALanC (bacterial lantibiotic synthetase component C)-like 1LanC like 1lanC-like protein 1

Antioxidant response modulation (scavenging reactive oxygen species, ROS); Modulation of AKT signaling pathway activity (in neurologic models); Enhancing neuronal survival via redox and signaling modulation.