ABHD3

ABHD3
Identifiers
Aliases	ABHD3, LABH3, abhydrolase domain containing 3
External IDs	MGI: 2147183 HomoloGene: 14055 GeneCards: ABHD3
Gene location (Human)
Chr.	Chromosome 18 (human)[1]
End	21,704,805 bp[1]
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)[2]
End	10,706,771 bp[2]
Gene ontology
Molecular function	• 1-acyl-2-lysophosphatidylserine acylhydrolase activity; • phosphatidylserine 1-acylhydrolase activity; • phospholipase A2 activity; • carboxylic ester hydrolase activity; • hydrolase activity; • phosphatidylcholine 1-acylhydrolase activity; • phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); • phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); • lipase activity; • short-chain carboxylesterase activity; • acylglycerol lipase activity;
Cellular component	• integral component of membrane; • plasma membrane; • membrane; • cellular component;
Biological process	• phosphatidylcholine biosynthetic process; • phosphatidylcholine metabolic process; • lipid metabolic process; • cellular lipid metabolic process; • medium-chain fatty acid biosynthetic process; • medium-chain fatty acid catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	171586
	106861
	ENSG00000158201
	ENSMUSG00000002475
	Q8WU67
	Q91ZH7
	NM_001308256; NM_001308257; NM_138340
	NM_134130
	NP_001295185; NP_001295186; NP_612213
	NP_598891
	Wikidata
View/Edit Human	View/Edit Mouse

Alpha/beta hydrolase domain containing 3 (ABHD3; alternative names: lung alpha/beta hydrolase 3,^[5] phospholipase ABHD3) is a single pass type II membrane member of the serine hydrolase family of enzymes.^[6] The expression of murine ABHD3 is highest in the brain, liver, and kidney. ABHD3 hydrolytic activity is highly specific for medium chain (e.g., dimyristoylphosphatidylcholine) and oxidatively truncated (e.g., azelaoyl PAF) phospholipids. ABHD3-deficient mice are viable, fertile, and possess dramatically elevated medium chain phospholipids in tissues and in blood. Conversely, ectopic expression of ABHD3 prevents the accumulation of oxidized phospholipids in cells.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000158201 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000002475 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Edgar AJ, Polack JM (Apr 2002). "Cloning and tissue distribution of three murine alpha/beta hydrolase fold protein cDNAs". Biochem Biophys Res Commun. 292 (3): 617–25. doi:10.1006/bbrc.2002.6692. PMID 11922611.
↑ Long JZ, Cisar JS, Milliken D, Niessen S, Wang C, Trauger SA, Suizdak G, Cravatt BF (Sep 2011). "Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids". Nature Chemical Biology. 7 (11): 763–5. doi:10.1038/nchembio.659. PMC 3201731. PMID 21926997.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000158201 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000002475 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11922611-5] Edgar AJ, Polack JM (Apr 2002). "Cloning and tissue distribution of three murine alpha/beta hydrolase fold protein cDNAs". Biochem Biophys Res Commun. 292 (3): 617–25. doi:10.1006/bbrc.2002.6692. PMID 11922611.

[pmid21926997-6] Long JZ, Cisar JS, Milliken D, Niessen S, Wang C, Trauger SA, Suizdak G, Cravatt BF (Sep 2011). "Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids". Nature Chemical Biology. 7 (11): 763–5. doi:10.1038/nchembio.659. PMC 3201731. PMID 21926997.