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.
September 2016 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Wilson P.A. Gardner S.D. Lambie N.M. Commans S.A. Crowther D.J.
Characterization of the human patatin-like phospholipase family.
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(CC BY-NC-ND 4.0) License, see prosite_license.html.