P0C1S9
uniprot
P0C1S9
canonical
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 (By similarity). {ECO:0000250|UniProtKB:Q8NCG7, ECO:0000250|UniProtKB:Q91WC9}.
uniprot
proteins
amino_acid_sequence
MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIASLTLYLMHRRKLDCPGGVLLSTYLIVLLVLLAVIIGIVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIVFVFDPLGGKMAPYPPCIPEHLDSNSSNHLLTGLRTAAKSVWETRVQCCCCCIGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDKISHSREPSEVVTHTPGQPQETELDAEVENCHHYMPFSPVCSPWPVCVLNSSRVELCRTGNNFCRGRDIEYDAVEGDEHHCHFASILKTTGLQYRDFIHVSFHDKVYELPFIVVLDHRKESVVVAVRGTMSLQDVLTDLSAESENLELDIELQDCVAHKGIAQAARYIYRRLVNDGILSQAFSVAPEYRLVVVGHSLGAGAAALLAIMLRGAYPQVRAYAFSPPRGLLSKSLFEYSKDFVVSLILGMDVIPRLSVANMEDLKRRILRVIANCNKPKYKILLHGCWYSVFGGSPDNFPTELDEGNQGALTQPLLGEQTLLTRCSPGYCSGDSPLDSPKYPTLYPPGRIIHLEEEGGSGRFGCCSAAQYRARWAHETEFSKILIGPKMLIDHMPDVMIRALDRVVADRTACVSCPGQGGSNVP
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. 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. 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:Q8NCG7, ECO:0000250|UniProtKB:Q91WC9}.
uniprot
proteins
mass_dalton
73771
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16051747
uniprot
proteins
sequence_length
668
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NCG7}; 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