LMPD Database

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LMP006638

UniProt Annotations

Entry Information
Gene Namepatatin-like phospholipase domain containing 2
Protein EntryPLPL2_HUMAN
UniProt IDQ96AD5
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96AD5-1; Sequence=Displayed; Name=2; IsoId=Q96AD5-2; Sequence=VSP_026421; Note=No experimental confirmation available.;
Biophysicochemical PropertiespH dependence: Optimum pH is 7.5 with (1,2-dilinoleoyl)-phosphatidylcholine as substrate. ;
Catalytic ActivityTriacylglycerol + H(2)O = diacylglycerol + a carboxylate.
Developmental StageInduced during differentiation of primary preadipocytes to adipocytes. Expression increased from fetal to adult in retinal pigment epithelium. {ECO
DiseaseNeutral lipid storage disease with myopathy (NLSDM) [MIM
DiseaseNote=Genetic variations in PNPLA2 may be associated with risk of diabetes mellitus type 2.
Enzyme RegulationInhibited by BEL ((E)-6-(bromomethylene)-3-(1- naphthalenyl)-2H-tetrahydropyran-2-one), a suicide substrate inhibitor. No differences in enzymatic activity that uses (1,2- dilinoleoyl)-phosphatidylcholine as substrate was detected in the presence or absence of ATP. Activated by ABHD5 and SERPINF1.
FunctionCatalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. {ECO
PathwayGlycerolipid metabolism; triacylglycerol degradation.
PolymorphismGenetic variations in PNPLA2 may be associated with plasma free fatty acids, triglycerides levels, and fasting glucose concentrations.
PtmPhosphorylation at Ser-404 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity (By similarity). Phosphorylation at Ser-404 is increased upon beta-adrenergic stimulation. {ECO
Sequence CautionSequence=AAP34448.1; Type=Frameshift; Positions=501; Evidence= ; Sequence=CAC01131.1; Type=Erroneous initiation; Evidence= ; Sequence=CAC01132.1; Type=Erroneous initiation; Evidence= ;
SimilarityContains 1 patatin domain.
Subcellular LocationLipid droplet. Cell membrane; Single-pass type II membrane protein.
SubunitInteracts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity (By similarity). Interacts with SERPINF1; interacts at one site of interaction. Despite a colocalization in lipid droplets, it probably does not interact with PLIN (By similarity). Interacts with PLIN5; prevents interaction with ABHD5 (By similarity).
Tissue SpecificityHighest expression in adipose tissue. Also detected in heart, skeletal muscle, and portions of the gastrointestinal tract. Detected in normal retina and retinoblastoma cells. Detected in retinal pigment epithelium and, at lower intensity, in the inner segments of photoreceptors and in the ganglion cell layer of the neural retina (at protein level). {ECO