{PDOC51635}
{PS51635; PNPLA}
{BEGIN}
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* Patatin-like phospholipase (PNPLA) domain profile *
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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 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 (see <PDB:1OXW>). The central beta-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 beta-strand
(beta5) of the central beta-sheet and precedes a helix (helix C) [4,5].

The profile we developed covers the entire PNPLA domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2016 / First entry.

[ 1] Wilson P.A., Gardner S.D., Lambie N.M., Commans S.A., Crowther D.J.
     "Characterization of the human patatin-like phospholipase family."
     J. Lipid Res. 47:1940-1949(2006).
     PubMed=16799181; DOI=10.1194/jlr.M600185-JLR200
[ 2] Kienesberger P.C., Oberer M., Lass A., Zechner R.
     "Mammalian patatin domain containing proteins: a family with diverse
     lipolytic activities involved in multiple biological functions."
     J. Lipid Res. 50:S63-S68(2009).
     PubMed=19029121; DOI=10.1194/jlr.R800082-JLR200
[ 3] Baulande S., Langlois C.
     "Proteins sharing PNPLA domain, a new family of enzymes regulating
     lipid metabolism."
     Medecine/Sciences 26:177-184(2010).
     PubMed=20188050; DOI=10.1051/medsci/2010262177
[ 4] 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.
     "The crystal structure, mutagenesis, and activity studies reveal that
     patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad."
     Biochemistry 42:6696-6708(2003).
     PubMed=12779324; DOI=10.1021/bi027156r
[ 5] Wijeyesakere S.J., Richardson R.J., Stuckey J.A.
     "Crystal structure of patatin-17 in complex with aged and non-aged
     organophosphorus compounds."
     PLoS ONE 9:E108245-E108245(2014).
     PubMed=25248161; DOI=10.1371/journal.pone.0108245

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