Daglb
entrez
231871
canonical
uniprot
Q91WC9
canonical
ensembl
ENSMUSG00000039206
resolver
ensp
ENSMUSP00000043088
resolver
ensp
ENSMUSP00000225397
resolver
ensp
ENSMUSP00000225416
resolver
enst
ENSMUST00000045593
resolver
genesymbol
Daglb
resolver
uniprot
Q8BU39
resolver
uniprot
Q8BU97
resolver
uniprot
Q8BV05
resolver
uniprot_entry
DGLB_MOUSE
resolver
uniprot_sec
Q8BU39
resolver
uniprot_sec
Q8BU97
resolver
uniprot_sec
Q8BV05
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the 1,2,3-triazole urea covalent inhibitors KT109 and KT172 (PubMed:23103940, PubMed:31991095). Inhibited by p-hydroxy-mercuri-benzoate and HgCl(2), but not by PMSF. Also inhibited by RHC80267, a drug that blocks 2-AG formation (By similarity). {ECO:0000250|UniProtKB:Q8NCG7, ECO:0000269|PubMed:23103940, ECO:0000269|PubMed:31991095}.
uniprot
proteins
amino_acid_sequence
MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIVSLTLYLTHRRRLDCPGGVLLSTYLIVLLVLLAVIICTVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIIFVFDPLGGKMAPYPPCIPEHLDSNSSNRLLTGLKTAAKSVWETRVQFCCCCVGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDNISHSREPPEVVTHTPGQPQETELDAEVENCHHYMPFAAAAYGWPLYIYRNPFTGLCRIGGDCCRARDIEYDAVEGDQHNCHFASILKTTGLQYRDFIHISFHDKVYELPFIVVLDHRKESVVVAVRGTMSLQDVLTDLSAESETLELGIELQDCVAHKGIAQAARYIHRRLVNDGILSQAFSVAPEYQLVLVGHSLGAGAAALLAIMLRGAYPQVRAYAFSPPRGLLSKSLYEYSKDFVVSLILGMDVIPRLSVTNMEDLKRRILRVIANCNKPKYKILLHGCWYGLFGGSPDNFPTELDEGTQGALTQPLLGEQTLLTRYSPGYCSSDSPLDSPTKYPTLYPPGRIIHLEEEGGSGRFGCCSAAQYRARWAHEAEFSKILIGPKMLIDHMPDVMIRALDRVLADRTACVSCPGQGGSSVP
uniprot
proteins
ec_number
3.1.1.116
uniprot
proteins
ec_number
3.1.1.3
uniprot
proteins
function
FUNCTION: 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:20147530, PubMed:20159446, 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). Also functions 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:23103940, PubMed:31991095). {ECO:0000250|UniProtKB:Q8NCG7, ECO:0000269|PubMed:20147530, ECO:0000269|PubMed:20159446, ECO:0000269|PubMed:23103940, ECO:0000269|PubMed:26779719, ECO:0000269|PubMed:31991095}.
uniprot
proteins
mass_dalton
73905
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
14610053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20147530
uniprot
proteins
pubmed
20159446
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23103940
uniprot
proteins
pubmed
26779719
uniprot
proteins
pubmed
31991095
uniprot
proteins
sequence_length
669
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31991095}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 18..38; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 59..79; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 103..123; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 129..149; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins