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PNPLA2 (human)

Overview PNPLA2 the rate-limiting lipolytic enzyme in mammals, flies, and yeast. Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Upregulated by exercise training in human skeletal muscle. Has acylglycerol transacylase activity. May act coordinately with HSL 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. Interacting with ABHD5 stimulates its triglyceride hydrolase activity. Despite a colocalization in lipid droplets, it probably does not interact with perilipin. Transcriptionally regulated by FOXO1A. Defects cause neutral lipid storage disease (NLSD), an autosomal recessive disorder characterized by the excessive accumulation of neutral lipids in multiple tissues. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Membrane protein, integral; EC 3.1.1.3; Lipase Cellular Component: endoplasmic reticulum membrane; plasma membrane; integral to membrane; lipid particle; cytosol Molecular Function: retinyl-palmitate esterase activity; triacylglycerol lipase activity Biological Process: phospholipid metabolic process; triacylglycerol catabolic process; glycerophospholipid biosynthetic process Reference #:  Q96AD5 (UniProtKB) Alt. Names/Synonyms: 1110001C14Rik; Adipose triglyceride lipase; ATGL; Calcium-independent phospholipase A2; Desnutrin; DKFZp667M109; FP17548; IPLA2-zeta; patatin-like phospholipase domain containing 2; Patatin-like phospholipase domain-containing protein 2; PEDF-R; Pigment epithelium-derived factor; PLPL2; PNPLA2; Transport-secretion protein 2; transport-secretion protein 2.2; triglyceride hydrolase; TTS-2.2; TTS2; TTS2.2 Gene Symbols: PNPLA2 Molecular weight: 55,316 Da Basal Isoelectric point: 6.65  Predict pI for various phosphorylation states

Select Structure to View Below PNPLA2

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  DISEASE 609059 610717  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K74-u	AKFIEVSkEARKRFL
0	1		K100-u	IIRSFLLkVLPADSH
0	12		K224-u	RNLYRLSkALFPPEP
0	8		Y287-p	ESAQAEDySQLPGED
0	1		E293	DySQLPGEDHILEHL
1	51		S404-p	VELRRVQsLPSVPLS
0	1		S407	RRVQsLPSVPLSCAA
0	1		Y415	VPLSCAAYREALPGW
0	17		S428-p	GWMRNNLsLGDALAK

	mouse
K74	ANIIEVSKEARKRFL
K100	TIRGCLLKTLPADCH
K224-u	RNLYRLSkALFPPEP
E287	VEERAGEEDQLQPYR
K295-u	DQLQPYRkDRILEHL
S406-p	VELRRAQsLPsVPLS
S409-p	RRAQsLPsVPLSCAT
Y417-p	VPLSCATySEALPNW
S430-p	NWVRNNLsLGDALAK

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