DAGLB
entrez
221955
canonical
uniprot
Q8NCG7
canonical
ensembl
ENSG00000164535
resolver
ensp
ENSP00000297056
resolver
ensp
ENSP00000391171
resolver
genesymbol
DAGLB
resolver
hgnc
HGNC:28923
resolver
uniprot
A4D2P3
resolver
uniprot
B3KV90
resolver
uniprot
B4DQU0
resolver
uniprot
Q6PIX3
resolver
uniprot
Q8N2N2
resolver
uniprot
Q8N9S1
resolver
uniprot
Q8TED3
resolver
uniprot
Q8WXE6
resolver
uniprot_entry
DGLB_HUMAN
resolver
uniprot_sec
A4D2P3
resolver
uniprot_sec
B3KV90
resolver
uniprot_sec
B4DQU0
resolver
uniprot_sec
Q6PIX3
resolver
uniprot_sec
Q8N2N2
resolver
uniprot_sec
Q8N9S1
resolver
uniprot_sec
Q8TED3
resolver
uniprot_sec
Q8WXE6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the 1,2,3-triazole urea covalent inhibitors KT109 and KT172 (By similarity). Inhibited by p-hydroxy-mercuri-benzoate and HgCl(2), but not by PMSF. Also inhibited by RHC80267, a drug that blocks 2-AG formation. {ECO:0000250|UniProtKB:Q91WC9, ECO:0000269|PubMed:14610053}.
uniprot
proteins
amino_acid_sequence
MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA
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:14610053). Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids (PubMed:14610053). 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. Also functions as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages (By similarity). {ECO:0000250|UniProtKB:Q91WC9, ECO:0000269|PubMed:14610053}.
uniprot
proteins
mass_dalton
73732
uniprot
proteins
mutagenesis
MUTAGEN 443; /note="S->A: Loss of activity."; /evidence="ECO:0000269|PubMed:14610053"; MUTAGEN 495; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:14610053
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14610053
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
672
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610053}; 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 133..153; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins