MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIVSLTLYLTHRRRLDCPGGVLLSTYLIVLLVLLAVIICTVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIIFVFDPLGGKMAPYPPCIPEHLDSNSSNRLLTGLKTAAKSVWETRVQFCCCCVGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDNISHSREPPEVVTHTPGQPQETELDAEVENCHHYMPFAAAAYGWPLYIYRNPFTGLCRIGGDCCRARDIEYDAVEGDQHNCHFASILKTTGLQYRDFIHISFHDKVYELPFIVVLDHRKESVVVAVRGTMSLQDVLTDLSAESETLELGIELQDCVAHKGIAQAARYIHRRLVNDGILSQAFSVAPEYQLVLVGHSLGAGAAALLAIMLRGAYPQVRAYAFSPPRGLLSKSLYEYSKDFVVSLILGMDVIPRLSVTNMEDLKRRILRVIANCNKPKYKILLHGCWYGLFGGSPDNFPTELDEGTQGALTQPLLGEQTLLTRYSPGYCSSDSPLDSPTKYPTLYPPGRIIHLEEEGGSGRFGCCSAAQYRARWAHEAEFSKILIGPKMLIDHMPDVMIRALDRVLADRTACVSCPGQGGSSVP

Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production (PubMed:20159446, PubMed:20147530, PubMed:23103940). Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids (By similarity). Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses (PubMed:23103940, PubMed:26779719). Functions also as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages (PubMed:31991095). Plays an important role to support the metabolic and signaling demands of macrophages (PubMed:31991095, PubMed:23103940).