Dagla
entrez
269060
canonical
uniprot
Q6WQJ1
canonical
ensembl
ENSMUSG00000035735
resolver
ensp
ENSMUSP00000046358
resolver
ensp
ENSMUSP00000200658
resolver
ensp
ENSMUSP00000200661
resolver
enst
ENSMUST00000039327
resolver
genesymbol
Dagla
resolver
genesymbol_syn
Kiaa0659
resolver
genesymbol_syn
Nsddr
resolver
uniprot
A4FU75
resolver
uniprot
A8WFL4
resolver
uniprot
Q6ZQ76
resolver
uniprot_entry
A4FU75_MOUSE
resolver
uniprot_entry
DGLA_MOUSE
resolver
uniprot_sec
A8WFL4
resolver
uniprot_sec
Q6ZQ76
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 1,2,3-triazole urea covalent inhibitor KT172, DH376 and DO34 (PubMed:23103940, PubMed:26668358). Inhibited by p-hydroxy-mercuri-benzoate and HgCl(2), but not to PMSF. Also inhibited by RHC80267. Diacylglycerol lipase activity is inhibited by the phosphorylation of Ser-784 and Ser-810 by CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q9Y4D2, ECO:0000269|PubMed:23103940, ECO:0000269|PubMed:26668358}.
uniprot
proteins
amino_acid_sequence
MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSHEMLRYKEVCYYMLFALAAYGWPMYLMRKPTCGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHRGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEDQVEVTTLASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPLPTGLALELPATEHRNSSVRSKSQSEMSLEGFSEGRLLSPVAAASAARQDPVELLLLSTQERLAAELQSRRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSATIEEEEAAGGSEGGGVAPRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMMVPESPTSDYTEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSAEPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLATDKIRTSTPTGHGASPTKQDDLVISAR
uniprot
proteins
ec_number
3.1.1.116
uniprot
proteins
function
FUNCTION: Serine hydrolase that hydrolyzes arachidonic acid-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid (eCB), 2-arachidonoylglycerol (2-AG) (PubMed:17584991, PubMed:23103940). Preferentially hydrolyzes sn-1 fatty acids from diacylglycerols (DAG) that contain arachidonic acid (AA) esterified at the sn-2 position to biosynthesize 2-AG. Has negligible activity against other lipids including monoacylglycerols and phospholipids (PubMed:17584991). Plays a key role in regulating 2-AG signaling in the central nervous system (CNS) (PubMed:20147530, PubMed:20159446, PubMed:25466252, PubMed:26668358, PubMed:26779719). Controls the activity of 2-AG as a retrograde messenger at neuronal synapses (PubMed:20147530, PubMed:20159446, PubMed:26668358). Supports axonal growth during development and adult neurogenesis (PubMed:20147530). Plays a role for eCB signaling in the physiological regulation of anxiety and depressive behaviors (PubMed:25466252). Also regulates neuroinflammatory responses in the brain, in particular, LPS-induced microglial activation (PubMed:26779719). {ECO:0000269|PubMed:17584991, ECO:0000269|PubMed:20147530, ECO:0000269|PubMed:20159446, ECO:0000269|PubMed:23103940, ECO:0000269|PubMed:25466252, ECO:0000269|PubMed:26668358, ECO:0000269|PubMed:26779719}.
uniprot
proteins
mass_dalton
115375
uniprot
proteins
mutagenesis
MUTAGEN 975; /note="P->C: Abolishes interaction with HOMER1. Does not affect enzymatic activity. Fails to associate with the plasma membrane."; /evidence="ECO:0000269|PubMed:17584991"; MUTAGEN 978; /note="F->R: Abolishes interaction with HOMER1."; /evidence="ECO:0000269|PubMed:17584991
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-784 and Ser-810 by CAMK2A; phosphorylation by CAMK2A inhibits diacylglycerol lipase activity. {ECO:0000250|UniProtKB:Q9Y4D2}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
14610053
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
16723519
uniprot
proteins
pubmed
17584991
uniprot
proteins
pubmed
20147530
uniprot
proteins
pubmed
20159446
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23103940
uniprot
proteins
pubmed
23502535
uniprot
proteins
pubmed
25466252
uniprot
proteins
pubmed
26668358
uniprot
proteins
pubmed
26779719
uniprot
proteins
sequence_length
1044
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17584991}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:16723519}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the cell surface and an intracellular endosomal compartment. Internalized by early endosomes via a clathrin-independent pathway before transport back to the postsynaptic membrane surface in a PKC-dependent manner. {ECO:0000250|UniProtKB:Q9Y4D2}.
uniprot
proteins
transmembrane_region
TRANSMEM 23..43; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 61..81; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 102..122; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 137..157; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins