Dagla
entrez
309207
canonical
uniprot
Q5YLM1
canonical
ensembl
ENSRNOG00000027264
resolver
ensembl
ENSRNOG00055017960
resolver
ensembl
ENSRNOG00060030524
resolver
ensembl
ENSRNOG00065033962
resolver
ensp
ENSRNOP00000033416
resolver
ensp
ENSRNOP00055024475
resolver
ensp
ENSRNOP00060044069
resolver
ensp
ENSRNOP00065048015
resolver
enst
ENSRNOT00000037624
resolver
enst
ENSRNOT00055030421
resolver
enst
ENSRNOT00060053011
resolver
enst
ENSRNOT00065058339
resolver
genesymbol
Dagla
resolver
genesymbol_syn
Nsddr
resolver
uniprot_entry
DGLA_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 1,2,3-triazole urea covalent inhibitors KT172, DH376 and DO34 (By similarity). 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:Q6WQJ1, ECO:0000250|UniProtKB:Q9Y4D2}.
uniprot
proteins
amino_acid_sequence
MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSHEMLRYKEVCYYMLFALAAYGWPMYLMRKPTCGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHRGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEDQVEVTALASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPLPTGLALELPATEHRNSSVRSKSQSEMSLEGFSEGRLLSPVAAASAARQDPVELLLLSTQERLAAELQSRRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSAANDEEEAAGGSEGGGVAPRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMMVPESPTSDYTEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSAEPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLATDKIRTSTPTGHGASPTKQDDLVISAR
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, 2-arachidonoylglycerol (2-AG). 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. Plays a key role in regulating 2-AG signaling in the CNS. Controls the activity of 2-AG as a retrograde messenger at neuronal synapses. Supports axonal growth during development and adult neurogenesis. Plays a role for eCB signaling in the physiological regulation of anxiety and depressive behaviors. Also regulates neuroinflammatory responses in the brain, in particular, LPS-induced microglial activation. {ECO:0000250|UniProtKB:Q6WQJ1}.
uniprot
proteins
mass_dalton
115301
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
22673903
uniprot
proteins
sequence_length
1044
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q6WQJ1}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y4D2}. 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