PROSITE documentation PDOC51635Patatin-like phospholipase (PNPLA) domain profile
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 [1,2,3].
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 (see <PDB:1OXW>). 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) [4,5].
The profile we developed covers the entire PNPLA domain.
Last update:September 2016 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Wilson P.A. Gardner S.D. Lambie N.M. Commans S.A. Crowther D.J. |
| Title | Characterization of the human patatin-like phospholipase family. | |
| Source | J. Lipid Res. 47:1940-1949(2006). | |
| PubMed ID | 16799181 | |
| DOI | 10.1194/jlr.M600185-JLR200 |
| 2 | Authors | Kienesberger P.C. Oberer M. Lass A. Zechner R. |
| Title | Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. | |
| Source | J. Lipid Res. 50:S63-S68(2009). | |
| PubMed ID | 19029121 | |
| DOI | 10.1194/jlr.R800082-JLR200 |
| 3 | Authors | Baulande S. Langlois C. |
| Title | Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism. | |
| Source | Medecine/Sciences 26:177-184(2010). | |
| PubMed ID | 20188050 | |
| DOI | 10.1051/medsci/2010262177 |
| 4 | Authors | Rydel T.J. Williams J.M. Krieger E. Moshiri F. Stallings W.C. Brown S.M. Pershing J.C. Purcell J.P. Alibhai M.F. |
| Title | The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. | |
| Source | Biochemistry 42:6696-6708(2003). | |
| PubMed ID | 12779324 | |
| DOI | 10.1021/bi027156r |
| 5 | Authors | Wijeyesakere S.J. Richardson R.J. Stuckey J.A. |
| Title | Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. | |
| Source | PLoS ONE 9:E108245-E108245(2014). | |
| PubMed ID | 25248161 | |
| DOI | 10.1371/journal.pone.0108245 |
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