Patatin-like phospholipase domain
IPR002641
Definition
The patatin glycoprotein is a nonspecific lipid acyl hydrolase that is found in high concentrations in mature potato tubers. Patatin is reported to play a role in plant signaling, to cleave fatty acids from membrane lipids, and to act as defense against plant parasites. Proteins encoding a patatin-like phospholipase (PNPLA) domain are ubiquitously distributed across all life forms, including eukaryotes and prokaryotes, and are observed to participate in a miscellany of biological roles, including sepsis induction, host colonization, triglyceride metabolism, and membrane trafficking. PNPLA domain containing proteins display lipase and transacylase properties and appear to have major roles in lipid and energy homeostasis [[cite:PMID:16799181], [cite:PMID:19029121], [cite:PMID:20188050]]. The ~180-amino acid PNPLA domain harbors the evolutionarily conserved consensus serine lipase motif Gly-X-Ser-X-Gly. It displays an α/β class protein fold with approximately three layers, basically α/β/α in content, in which a central six-stranded β-sheet is sandwiched essentially between α-helices front and back. The central β-sheet contains five parallel strands and an antiparallel strand at the edge of the sheet. The PNPLA domain has a Ser-Asp catalytic dyad. The catalytic Ser resides in a sharp nucleophile elbow turn loop which follows a β-strand (β5) of the central β-sheet and precedes a helix (helix C) [[cite:PMID:12779324], [cite:PMID:25248161]].
9 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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