H-rev107 Phospholipase/Acyltransferase
IPR051496
Definition
The H-rev107 family proteins are multifunctional enzymes with both phospholipase A1/2 and acyltransferase activities. They catalyze the calcium-independent release of fatty acids from glycerophospholipids at the sn-1 or sn-2 position, with a higher activity for PLA1 over PLA2 for most substrates. Additionally, they exhibit O-acyltransferase activity, transferring fatty acyl groups from glycerophospholipids to lysophospholipids. They also show N-acyltransferase activity, transferring fatty acyl groups from phosphatidylcholine and other glycerophospholipids to the primary amine of phosphatidylethanolamine, forming N-acylphosphatidylethanolamine, a precursor for N-acylethanolamines. Some family members are involved in organelle degradation during eye lens terminal differentiation, contributing to lens transparency. Others may act as host factors for picornaviruses, facilitating viral genome release into the cytoplasm. The C-terminal transmembrane domain is essential for targeting to damaged organelles.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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