InterPro domain: IPR002641
General Information
- Identifier IPR002641
- Description Patatin-like phospholipase domain
- Number of genes 2025
- Gene duplication stats Loading...
- Associated GO terms GO:0006629
Abstract
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-likephospholipase (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 [ 1 , 2 , 3 ].
The ~180-amino acid PNPLA domain harbors the evolutionarily conserved consensus serine lipase motif Gly-X-Ser-X-Gly.cIt displays an alpha/beta class protein fold with approximately three layers, basically alpha/beta/alpha in content, in which a central six-stranded beta-sheet is sandwiched essentially between alpha-helices front and back. The central beta-sheet contains five parallel strands and an antiparallel strand at the edge of thesheet. The PNPLA domain has a Ser-Asp catalytic dyad. The catalytic Ser resides in a sharp nucleophile elbow turn loop which follows a beta-strand(beta5) of the central beta-sheet and precedes a helix (helix C) [ 4 , 5 ].
1. Characterization of the human patatin-like phospholipase family. J. Lipid Res. 47, 1940-9
2. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J. Lipid Res. 50 Suppl, S63-8
3. [Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism]. Med Sci (Paris) 26, 177-84
4. The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry 42, 6696-708
5. Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. PLoS ONE 9, e108245