Adipose triglyceride lipase

PNPLA2
Identifiers
Aliases	PNPLA2, 1110001C14Rik, ATGL, PEDF-R, TTS-2.2, TTS2, iPLA2zeta, FP17548, patatin like phospholipase domain containing 2
External IDs	OMIM: 609059 MGI: 1914103 HomoloGene: 10687 GeneCards: PNPLA2
Gene location (Human)
Chr.	Chromosome 11 (human)[1]
End	825,573 bp[1]
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)[2]
End	141,460,743 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• hydrolase activity; • lipoprotein lipase activity; • acylglycerol O-acyltransferase activity; • triglyceride lipase activity;
Cellular component	• integral component of membrane; • cytosol; • lipid droplet; • cell membrane; • endoplasmic reticulum membrane; • cytoplasm; • membrane; • nucleoplasm; • endoplasmic reticulum lumen;
Biological process	• lipid catabolic process; • lipid storage; • metabolism; • negative regulation of sequestering of triglyceride; • positive regulation of triglyceride catabolic process; • acylglycerol acyl-chain remodeling; • lipid particle organization; • lipid metabolism; • triglyceride catabolic process; • lipid homeostasis; • post-translational modification; • cellular protein metabolic process; • cellular lipid catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	57104
	66853
	ENSG00000177666
	ENSMUSG00000025509
	Q96AD5
	Q8BJ56
	NM_020376
	NM_001163689; NM_025802
	NP_065109
	NP_001157161; NP_080078
	Wikidata
View/Edit Human	View/Edit Mouse

Adipose triglyceride lipase, also known as patatin-like phospholipase domain-containing protein 2 and ATGL, is an enzyme that in humans is encoded by the PNPLA2 gene.[5][6][7][8] ATGL catalyses the first reaction of lipolysis,[9] where triacylglycerols are hydrolysed to diacylglycerols.[10]

Properties

ATGL has very high substrate specificity for triacylglycerols.[11] It contains a catalytic dyad using serine-aspartic acid.[10]

Function

ATGL catalyses the first reaction of lipolysis.[9] It hydrolysis triacylglycerols to diacylglycerols[10] by attacking the fatty acid attached to carbon-3 of glycerol.

ATGL acts as a control mechanism of lipolysis, as variations in diacylglycerol concentration impact enzymes in later stages of lipolysis.[12]

Clinical significance

Defects in ATGL can cause problems in lipolysis, leading to neutral lipid storage disease.[13] As triacylglycerols are not hydrolysed to diacylglycerols, there is a build-up of triacylglycerol droplets in granulocytes.[13]

References

GRCh38: Ensembl release 89: ENSG00000177666 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000025509 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Wilson PA, Gardner SD, Lambie NM, Commans SA, Crowther DJ (September 2006). "Characterization of the human patatin-like phospholipase family". Journal of Lipid Research. 47 (9): 1940–9. doi:10.1194/jlr.M600185-JLR200. PMID 16799181.
Kienesberger PC, Oberer M, Lass A, Zechner R (April 2009). "Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions". Journal of Lipid Research. 50 Suppl (Supplement): S63-8. doi:10.1194/jlr.R800082-JLR200. PMC 2674697. PMID 19029121.
"Entrez Gene: PNPLA2 patatin-like phospholipase domain containing 2".
Ojha S, Budge H, Symonds ME (2014). "Adipocytes in Normal Tissue Biology". In McManus LM, Mitchell RN (eds.). Pathobiology of Human Disease. San Diego: Academic Press. pp. 2003–2013. doi:10.1016/b978-0-12-386456-7.04408-7. ISBN 978-0-12-386457-4.
Lehner R, Quiroga AD (2016). "Chapter 5 - Fatty Acid Handling in Mammalian Cells". In Ridgway ND, McLeod RS (eds.). Biochemistry of Lipids, Lipoproteins and Membranes (Sixth ed.). Boston: Elsevier. pp. 149–184. doi:10.1016/b978-0-444-63438-2.00005-5. ISBN 978-0-444-63438-2.
Tsiloulis T, Watt MJ (2015). "Chapter Eight - Exercise and the Regulation of Adipose Tissue Metabolism". In Bouchard C (ed.). Progress in Molecular Biology and Translational Science. Molecular and Cellular Regulation of Adaptation to Exercise. 135. Academic Press. pp. 175–201. doi:10.1016/bs.pmbts.2015.06.016.
Zhang X, Heckmann BL, Liu J (2013-01-01). Yang P, Li H (eds.). "Studying lipolysis in adipocytes by combining siRNA knockdown and adenovirus-mediated overexpression approaches". Methods in Cell Biology. Lipid Droplets. Academic Press. 116: 83–105. doi:10.1016/b978-0-12-408051-5.00006-1. PMC 4529287. PMID 24099289.
Bongarzone ER, Givogri MI, Darryl C, DiMauro S (January 2012). "Inborn Metabolic Defects of Lysosomes, Peroxisomes, Carbohydrates, Fatty Acids and Mitochondria.". In Brady ST, Siegel GJ, Albers RW, Price DL (eds.). Basic Neurochemistry (Eighth ed.). New York: Academic Press. pp. 755–782. doi:10.1016/b978-0-12-374947-5.00043-2. ISBN 978-0-12-374947-5.

External links

Human PNPLA2 genome location and PNPLA2 gene details page in the UCSC Genome Browser.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000177666 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025509 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8619474-5] Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.

[pmid16799181-6] Wilson PA, Gardner SD, Lambie NM, Commans SA, Crowther DJ (September 2006). "Characterization of the human patatin-like phospholipase family". Journal of Lipid Research. 47 (9): 1940–9. doi:10.1194/jlr.M600185-JLR200. PMID 16799181.

[pmid19029121-7] Kienesberger PC, Oberer M, Lass A, Zechner R (April 2009). "Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions". Journal of Lipid Research. 50 Suppl (Supplement): S63-8. doi:10.1194/jlr.R800082-JLR200. PMC 2674697. PMID 19029121.

[entrez-8] "Entrez Gene: PNPLA2 patatin-like phospholipase domain containing 2".

[:0-9] Ojha S, Budge H, Symonds ME (2014). "Adipocytes in Normal Tissue Biology". In McManus LM, Mitchell RN (eds.). Pathobiology of Human Disease. San Diego: Academic Press. pp. 2003–2013. doi:10.1016/b978-0-12-386456-7.04408-7. ISBN 978-0-12-386457-4.

[:1-10] Lehner R, Quiroga AD (2016). "Chapter 5 - Fatty Acid Handling in Mammalian Cells". In Ridgway ND, McLeod RS (eds.). Biochemistry of Lipids, Lipoproteins and Membranes (Sixth ed.). Boston: Elsevier. pp. 149–184. doi:10.1016/b978-0-444-63438-2.00005-5. ISBN 978-0-444-63438-2.

[11] Tsiloulis T, Watt MJ (2015). "Chapter Eight - Exercise and the Regulation of Adipose Tissue Metabolism". In Bouchard C (ed.). Progress in Molecular Biology and Translational Science. Molecular and Cellular Regulation of Adaptation to Exercise. 135. Academic Press. pp. 175–201. doi:10.1016/bs.pmbts.2015.06.016.

[12] Zhang X, Heckmann BL, Liu J (2013-01-01). Yang P, Li H (eds.). "Studying lipolysis in adipocytes by combining siRNA knockdown and adenovirus-mediated overexpression approaches". Methods in Cell Biology. Lipid Droplets. Academic Press. 116: 83–105. doi:10.1016/b978-0-12-408051-5.00006-1. PMC 4529287. PMID 24099289.

[:2-13] Bongarzone ER, Givogri MI, Darryl C, DiMauro S (January 2012). "Inborn Metabolic Defects of Lysosomes, Peroxisomes, Carbohydrates, Fatty Acids and Mitochondria.". In Brady ST, Siegel GJ, Albers RW, Price DL (eds.). Basic Neurochemistry (Eighth ed.). New York: Academic Press. pp. 755–782. doi:10.1016/b978-0-12-374947-5.00043-2. ISBN 978-0-12-374947-5.