DAGLA
entrez
747
canonical
uniprot
Q9Y4D2
canonical
ensembl
ENSG00000134780
resolver
ensp
ENSP00000257215
resolver
ensp
ENSP00000545720
resolver
ensp
ENSP00000609772
resolver
enst
ENST00000257215
resolver
enst
ENST00000875661
resolver
enst
ENST00000939713
resolver
genesymbol
DAGLA
resolver
genesymbol_syn
C11orf11
resolver
genesymbol_syn
KIAA0659
resolver
genesymbol_syn
NSDDR
resolver
hgnc
HGNC:1165
resolver
uniprot
A0A024R517
resolver
uniprot
A7E233
resolver
uniprot
Q6WQJ0
resolver
uniprot_entry
DGLA_HUMAN
resolver
uniprot_sec
A0A024R517
resolver
uniprot_sec
A7E233
resolver
uniprot_sec
Q6WQJ0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 1,2,3-triazole urea covalent inhibitors KT172, DH376 and DO34 (PubMed:26668358). Inhibited by p-hydroxy-mercuri-benzoate and HgCl(2), but not to PMSF. Also inhibited by RHC80267 (PubMed:14610053). Diacylglycerol lipase activity is inhibited by the phosphorylation of Ser-782 and Ser-808 by CAMK2A (PubMed:23502535). {ECO:0000269|PubMed:14610053, ECO:0000269|PubMed:23502535, ECO:0000269|PubMed:26668358}.
uniprot
proteins
amino_acid_sequence
MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSQEMLRYKEVCYYMLFALAAYGWPMYLMRKPACGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEEVEVTTLASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPMPTGLALELPTADHRNSSVRSKSQSEMSLEGFSEGRLLSPVVAAAARQDPVELLLLSTQERLAAELQARRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSAAANDEEEEVGGGGGGPASRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMVVPESPTSDYAEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSADPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLAADKIRTSTPTGHGASPAKQDELVISAR
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia 20 (SCA20) [MIM:608687]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA20 is an autosomal dominant, adult-onset form characterized by dysarthria due to spasmodic dysphonia followed by slowly progressive ataxia. {ECO:0000269|PubMed:18801880}. Note=The disease may be caused by variants affecting the gene represented in this entry. A copy number variation consisting of a 260-kb duplication at chromosome 11q12.2-12.3 is responsible for SCA20. The critical gene within the duplicated segment may be DAGLA.; DISEASE: Neuroocular syndrome 2, paroxysmal type (NOC2) [MIM:168885]: A form of neuroocular syndrome, a group of disorders characterized by developmental delay, impaired intellectual development and ocular anomalies as primary findings. NOC2 is an autosomal dominant form characterized by eye deviation or nystagmus with abnormal head posturing apparent from birth or early infancy. Affected individuals also have hypotonia, mild developmental delay, dysarthria, and gait ataxia. Most patients have mildly impaired intellectual development. {ECO:0000269|PubMed:35737950}. Note=The disease is caused by variants affecting the gene represented in this entry.
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) (PubMed:14610053, PubMed:23502535, PubMed:26668358). Preferentially hydrolyzes sn-1 fatty acids from diacylglycerols (DAG) that contain arachidonic acid (AA) esterified at the sn-2 position to biosynthesize 2-AG (PubMed:14610053, PubMed:23502535, PubMed:26668358). Has negligible activity against other lipids including monoacylglycerols and phospholipids (PubMed:14610053). Plays a key role in regulating 2-AG signaling in the central nervous system (CNS). Regulates 2-AG involved in retrograde suppression at central 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 (By similarity). {ECO:0000250|UniProtKB:Q6WQJ1, ECO:0000269|PubMed:14610053, ECO:0000269|PubMed:23502535, ECO:0000269|PubMed:26668358}.
uniprot
proteins
mass_dalton
114952
uniprot
proteins
mutagenesis
MUTAGEN 782; /note="S->A: Slightly reduces phosphorylation by CAMK2A. Abolishes phosphorylation by CAMK2A; when associated with A-808."; /evidence="ECO:0000269|PubMed:23502535"; MUTAGEN 782; /note="S->E: Phosphomimetic mutation; decreased the Vmax of 2-AG production without affecting the KM; when associated with E-808."; /evidence="ECO:0000269|PubMed:23502535"; MUTAGEN 808; /note="S->A: Reduces phosphorylation by CAMK2A. Abolishes phosphorylation by CAMK2A; when associated with A-782."; /evidence="ECO:0000269|PubMed:23502535"; MUTAGEN 808; /note="S->E: Phosphomimetic mutation; decreased the Vmax of 2-AG production without affecting the KM; when associated with E-782."; /evidence="ECO:0000269|PubMed:23502535
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-782 and Ser-808 by CAMK2A; phosphorylation by CAMK2A inhibits diacylglycerol lipase activity. {ECO:0000269|PubMed:23502535}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14610053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16051747
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
18801880
uniprot
proteins
pubmed
23502535
uniprot
proteins
pubmed
26668358
uniprot
proteins
pubmed
27595600
uniprot
proteins
pubmed
35737950
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1042
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27595600}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density membrane {ECO:0000269|PubMed:27595600}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:27595600}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q6WQJ1}; 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:0000269|PubMed:27595600}.
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