PLA2G16, HRAS-like suppressor 3
Enzyme Classification 22.214.171.124
Also Known as
PA216_HUMAN, PLA2G16, HRASLS3, HREV107
Lipid-modifying enzyme that acts as major regulator of adipocyte lipolysis by catalyzing the release of fatty acids from phospholipids in adipose tissue (PubMed:19615464, PubMed:19047760, PubMed:20837014, PubMed:22605381, PubMed:22923616). Shows phospholipase A1 and A2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE) (PubMed:19615464, PubMed:19047760, PubMed:20837014, PubMed:22605381, PubMed:22923616). For most substrates, phospholipase A1 activity is much higher than phospholipase A2 activity (PubMed:19047760). Phospholipase activity causes decreased intracellular levels of ether-type lipids, affecting peroxisome metabolism (By similarity). May also have acyltransferase activity: catalyzes both N-acylation of phosphatidylethanolamine to form N-acyl-phosphatidylethanolamine and O-acylation of lyso-phosphatidylcholines to form phosphatidylcholines (PubMed:22605381, PubMed:25383759). The relevance of acyltransferase activity in vivo is however unclear and would require additional evidences (PubMed:22605381, PubMed:25383759). Also has weak lysophospholipase activity., (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878). Interacts with PPP2R1A; this interaction might decrease PP2A activity.