D
IPR002641

Patatin-like phospholipase domain

InterPro entry
Short namePNPLA_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

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
[4, 3, 2]
.

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)
[5, 1]
.

References

1.Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. Wijeyesakere SJ, Richardson RJ, Stuckey JA. PLoS ONE 9, e108245, (2014). View articlePMID: 25248161

2.[Proteins sharing PNPLA domain, a new family of enzymes regulating lipid metabolism]. Baulande S, Langlois C. Med Sci (Paris) 26, 177-84, (2010). View articlePMID: 20188050

3.Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. Kienesberger PC, Oberer M, Lass A, Zechner R. J. Lipid Res. 50 Suppl, S63-8, (2009). View articlePMID: 19029121

4.Characterization of the human patatin-like phospholipase family. Wilson PA, Gardner SD, Lambie NM, Commans SA, Crowther DJ. J. Lipid Res. 47, 1940-9, (2006). View articlePMID: 16799181

5.The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF. Biochemistry 42, 6696-708, (2003). View articlePMID: 12779324

GO terms

molecular function

  • None

cellular component

  • None

Cross References

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