Pnpla2
entrez
66853
canonical
uniprot
Q8BJ56
canonical
ensembl
ENSMUSG00000025509
resolver
ensp
ENSMUSP00000065116
resolver
ensp
ENSMUSP00000127149
resolver
genesymbol
Pnpla2
resolver
genesymbol_syn
Atgl
resolver
uniprot
O89080
resolver
uniprot
Q05BJ0
resolver
uniprot
Q3UD97
resolver
uniprot
Q643S0
resolver
uniprot
Q6P234
resolver
uniprot
Q9D1Q9
resolver
uniprot
Q9DCF6
resolver
uniprot_entry
PLPL2_MOUSE
resolver
uniprot_sec
O89080
resolver
uniprot_sec
Q05BJ0
resolver
uniprot_sec
Q3UD97
resolver
uniprot_sec
Q643S0
resolver
uniprot_sec
Q6P234
resolver
uniprot_sec
Q9D1Q9
resolver
uniprot_sec
Q9DCF6
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by PKA-dependent PLIN phosphorylation. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:17114792}.
uniprot
proteins
amino_acid_sequence
MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHERANGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVVEERAGEEDQLQPYRKDRILEHLPARLNEALLEACVEPKDLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGDHLPSRLSEQVELRRAQSLPSVPLSCATYSEALPNWVRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPDALRMRAPASPTAADPATPQDPPGLPPC
uniprot
proteins
ec_number
3.1.1.3
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15337759, PubMed:15550674, PubMed:16150821, PubMed:16675698, PubMed:16679289, PubMed:17074755, PubMed:17114792, PubMed:23066022). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (PubMed:23066022). Also possesses acylglycerol transacylase and phospholipase A2 activities (By similarity). Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides (By similarity). Regulates adiposome size and may be involved in the degradation of adiposomes (By similarity). Catalyzes the formation of an ester bond between hydroxy fatty acids and fatty acids derived from triglycerides or diglycerides to generate fatty acid esters of hydroxy fatty acids (FAHFAs) in adipocytes (PubMed:35676490). Acts antagonistically with LDAH in regulation of cellular lipid stores (By similarity). Inhibits LDAH-stimulated lipid droplet fusion (By similarity). May play an important role in energy homeostasis (PubMed:16675698). 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 (PubMed:15337759). {ECO:0000250|UniProtKB:Q96AD5, ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:17114792, ECO:0000269|PubMed:23066022, ECO:0000269|PubMed:35676490}.
uniprot
proteins
mass_dalton
53657
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="S->A: Loss of triacylglycerol hydrolysis activity."; /evidence="ECO:0000269|PubMed:16679289"; MUTAGEN 396; /note="S->A: Slightly reduced TG hydrolase activity."; /evidence="ECO:0000269|PubMed:22733971"; MUTAGEN 406; /note="S->A: Reduced TG hydrolase activity."; /evidence="ECO:0000269|PubMed:22733971
uniprot
proteins
pathway_participation
PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-406 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:22733971}.; PTM: Ubiquitinated by PEX2 in response to reactive oxygen species (ROS), leading to its degradation (By similarity). Ubiquitination is stimulated by LDAH (By similarity). {ECO:0000250|UniProtKB:Q96AD5}.
uniprot
proteins
pubmed
15337759
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15550674
uniprot
proteins
pubmed
16009485
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16150821
uniprot
proteins
pubmed
16380488
uniprot
proteins
pubmed
16675698
uniprot
proteins
pubmed
16679289
uniprot
proteins
pubmed
16705060
uniprot
proteins
pubmed
17074755
uniprot
proteins
pubmed
17114792
uniprot
proteins
pubmed
17189257
uniprot
proteins
pubmed
21148142
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21393244
uniprot
proteins
pubmed
22733971
uniprot
proteins
pubmed
23066022
uniprot
proteins
pubmed
35676490
uniprot
proteins
pubmed
9798653
uniprot
proteins
sequence_length
486
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16705060}. Cell membrane {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15337759}.
uniprot
proteins
transmembrane_region
TRANSMEM 9..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 43..63; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 138..158; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 332..352; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins