Sequence Detail

ID/Version

Q99LR1 Q99M06 A2ANB4 (UniProt | EBI)

Last sequence update: 2003-11-28
Last annotation update: 2025-02-05

Sequence description from provider

RecName: Full=Lysophosphatidylserine lipase ABHD12 {ECO:0000305}; EC=3.1.1.- {ECO:0000269|PubMed:23297193};AltName: Full=2-arachidonoylglycerol hydrolase ABHD12 {ECO:0000305};AltName: Full=Abhydrolase domain-containing protein 12 {ECO:0000305};Alt

Provider

SWISS-PROT

Sequence

Polypeptide 398 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Abhd12	abhydrolase domain containing 12	49	96	3	17

Sequence references in MGI

J:163762 Marrs WR, et al., The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors. Nat Neurosci. 2010 Aug;13(8):951-7
J:193716 Blankman JL, et al., ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC. Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1500-5
J:217994 Blankman JL, et al., A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. Chem Biol. 2007 Dec;14(12):1347-56
J:232688 Kamat SS, et al., Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay. Nat Chem Biol. 2015 Feb;11(2):164-71
J:272811 Joshi A, et al., Biochemical characterization of the PHARC-associated serine hydrolase ABHD12 reveals its preference for very-long-chain lipids. J Biol Chem. 2018 Nov 2;293(44):16953-16963
J:273578 Kelkar DS, et al., A chemical-genetic screen identifies ABHD12 as an oxidized-phosphatidylserine lipase. Nat Chem Biol. 2019 Feb;15(2):169-178
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89