LACC1
Description
The LACC1 (laccase domain containing 1) is a protein-coding gene located on chromosome 13.
Laccase (multicopper oxidoreductase) domain containing 1 is a protein in humans that is encoded by the LACC1 gene.
LACC1 is a purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine, and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine, and hypoxanthine. It also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. LACC1 has adenosine deaminase activity and acts as a regulator of innate immunity in macrophages by modulating purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages. It enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface. This cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity. LACC1 participates in pattern recognition receptor (PRR)-induced cytokines in macrophages, associating with the NOD2-signaling complex and promoting optimal NOD2-induced signaling, cytokine secretion, and bacterial clearance. Upon PRR stimulation of macrophages, LACC1 localizes to the endoplasmic reticulum, associating with endoplasmic reticulum-stress sensors and promoting the endoplasmic reticulum unfolded protein response (UPR). However, LACC1 does not exhibit laccase activity.
LACC1 is also known as C13orf31, FAMIN, JUVAR.
