DGLB_MOUSE
ID DGLB_MOUSE Reviewed; 669 AA.
AC Q91WC9; Q8BU39; Q8BU97; Q8BV05;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Diacylglycerol lipase-beta {ECO:0000303|PubMed:31991095};
DE Short=DAGL-beta {ECO:0000303|PubMed:31991095};
DE Short=DAGLbeta {ECO:0000303|PubMed:20147530, ECO:0000303|PubMed:23103940};
DE Short=DGL-beta {ECO:0000303|PubMed:20159446};
DE EC=3.1.1.116 {ECO:0000269|PubMed:23103940};
DE AltName: Full=PUFA-specific triacylglycerol lipase {ECO:0000303|PubMed:31991095};
DE EC=3.1.1.3 {ECO:0000269|PubMed:31991095};
DE AltName: Full=Sn1-specific diacylglycerol lipase beta {ECO:0000303|PubMed:14610053};
GN Name=Daglb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Lung, and Ovary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=14610053; DOI=10.1083/jcb.200305129;
RA Bisogno T., Howell F., Williams G., Minassi A., Cascio M.G., Ligresti A.,
RA Matias I., Schiano-Moriello A., Paul P., Williams E.-J., Gangadharan U.,
RA Hobbs C., Di Marzo V., Doherty P.;
RT "Cloning of the first sn1-DAG lipases points to the spatial and temporal
RT regulation of endocannabinoid signaling in the brain.";
RL J. Cell Biol. 163:463-468(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=20147530; DOI=10.1523/jneurosci.5693-09.2010;
RA Gao Y., Vasilyev D.V., Goncalves M.B., Howell F.V., Hobbs C.,
RA Reisenberg M., Shen R., Zhang M.Y., Strassle B.W., Lu P., Mark L.,
RA Piesla M.J., Deng K., Kouranova E.V., Ring R.H., Whiteside G.T., Bates B.,
RA Walsh F.S., Williams G., Pangalos M.N., Samad T.A., Doherty P.;
RT "Loss of retrograde endocannabinoid signaling and reduced adult
RT neurogenesis in diacylglycerol lipase knock-out mice.";
RL J. Neurosci. 30:2017-2024(2010).
RN [6]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=20159446; DOI=10.1016/j.neuron.2010.01.021;
RA Tanimura A., Yamazaki M., Hashimotodani Y., Uchigashima M., Kawata S.,
RA Abe M., Kita Y., Hashimoto K., Shimizu T., Watanabe M., Sakimura K.,
RA Kano M.;
RT "The endocannabinoid 2-arachidonoylglycerol produced by diacylglycerol
RT lipase alpha mediates retrograde suppression of synaptic transmission.";
RL Neuron 65:320-327(2010).
RN [7]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE,
RP AND TISSUE SPECIFICITY.
RX PubMed=23103940; DOI=10.1038/nchembio.1105;
RA Hsu K.L., Tsuboi K., Adibekian A., Pugh H., Masuda K., Cravatt B.F.;
RT "DAGLbeta inhibition perturbs a lipid network involved in macrophage
RT inflammatory responses.";
RL Nat. Chem. Biol. 8:999-1007(2012).
RN [8]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=26779719; DOI=10.7554/elife.12345;
RA Viader A., Ogasawara D., Joslyn C.M., Sanchez-Alavez M., Mori S.,
RA Nguyen W., Conti B., Cravatt B.F.;
RT "A chemical proteomic atlas of brain serine hydrolases identifies cell
RT type-specific pathways regulating neuroinflammation.";
RL Elife 5:e12345-e12345(2016).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=31991095; DOI=10.1016/j.chembiol.2020.01.005;
RA Shin M., Ware T.B., Hsu K.L.;
RT "DAGL-Beta Functions as a PUFA-Specific Triacylglycerol Lipase in
RT Macrophages.";
RL Cell Chem. Biol. 0:0-0(2020).
CC -!- FUNCTION: Lipase that catalyzes the hydrolysis of arachidonic acid
CC (AA)-esterified diacylglycerols (DAGs) to produce the principal
CC endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further
CC cleaved by downstream enzymes to release arachidonic acid (AA) for
CC cyclooxygenase (COX)-mediated eicosanoid production (PubMed:20159446,
CC PubMed:20147530, PubMed:23103940). Preferentially hydrolyzes DAGs at
CC the sn-1 position in a calcium-dependent manner and has negligible
CC activity against other lipids including monoacylglycerols and
CC phospholipids (By similarity). Plays a key role in the regulation of 2-
CC AG and AA pools utilized by COX1/2 to generate lipid mediators of
CC macrophage and microglia inflammatory responses (PubMed:23103940,
CC PubMed:26779719). Functions also as a polyunsaturated fatty acids-
CC specific triacylglycerol lipase in macrophages (PubMed:31991095). Plays
CC an important role to support the metabolic and signaling demands of
CC macrophages (PubMed:31991095, PubMed:23103940).
CC {ECO:0000250|UniProtKB:Q8NCG7, ECO:0000269|PubMed:20147530,
CC ECO:0000269|PubMed:20159446, ECO:0000269|PubMed:23103940,
CC ECO:0000269|PubMed:26779719, ECO:0000269|PubMed:31991095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:28868; EC=3.1.1.116;
CC Evidence={ECO:0000269|PubMed:23103940};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC Evidence={ECO:0000305|PubMed:23103940};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:52392,
CC ChEBI:CHEBI:75728; Evidence={ECO:0000269|PubMed:23103940};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycerol + H2O = (9Z)-octadecenoate + 2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38515,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52392, ChEBI:CHEBI:75449;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-octadecanoylglycerol + H(+); Xref=Rhea:RHEA:38519,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75448, ChEBI:CHEBI:75456;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-(9Z,12Z-octadecadienoyl)-sn-glycerol +
CC H2O = (9Z)-octadecenoate + 2-(9Z,12Z-octadecadienoyl)-glycerol +
CC H(+); Xref=Rhea:RHEA:38523, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75450, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-O-(5Z,8Z,11Z,14Z-eicosatetraenyl)-sn-
CC glycerol + H2O = (9Z)-octadecenoate + 2-O-(5Z,8Z,11Z,14Z)-
CC eicosatetraenylglycerol + H(+); Xref=Rhea:RHEA:38527,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75913, ChEBI:CHEBI:75914;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:31991095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:31991095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + a di-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-glycerol + H(+); Xref=Rhea:RHEA:63432,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:147308, ChEBI:CHEBI:147309;
CC Evidence={ECO:0000269|PubMed:31991095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63433;
CC Evidence={ECO:0000305|PubMed:31991095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H2O =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + a di-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:63436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:77016, ChEBI:CHEBI:147310, ChEBI:CHEBI:147311;
CC Evidence={ECO:0000269|PubMed:31991095};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- ACTIVITY REGULATION: Inhibited by the 1,2,3-triazole urea covalent
CC inhibitors KT109 and KT172 (PubMed:23103940, PubMed:31991095).
CC Inhibited by p-hydroxy-mercuri-benzoate and HgCl(2), but not by PMSF.
CC Also inhibited by RHC80267, a drug that blocks 2-AG formation (By
CC similarity). {ECO:0000250|UniProtKB:Q8NCG7,
CC ECO:0000269|PubMed:23103940, ECO:0000269|PubMed:31991095}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31991095};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and immune cells such as
CC macrophages and microglias (PubMed:23103940, PubMed:31991095,
CC PubMed:26779719, PubMed:20147530). In embryonic brains present in
CC axonal tracts, while in adults localizes to dendritic fields,
CC correlating with the developmental change in requirement for 2-AG
CC synthesis from the pre- to the postsynaptic compartment (at protein
CC level) (PubMed:14610053). {ECO:0000269|PubMed:14610053,
CC ECO:0000269|PubMed:20147530, ECO:0000269|PubMed:23103940,
CC ECO:0000269|PubMed:26779719, ECO:0000269|PubMed:31991095}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable, fertile and display
CC normal physiological behaviors (PubMed:20159446, PubMed:20147530).
CC Levels of 2-AG are reduced by up to 90% in liver (PubMed:20147530). In
CC contrast, brain 2-AG and arachidonic acid (AA) content are unaltered in
CC deficient mice (PubMed:20159446, PubMed:23103940, PubMed:26779719).
CC However one report describes a decreased by up to 50% of 2-AG in the
CC brain (PubMed:20147530). Disruption of Daglb results in depletion of 2-
CC AG, AA, and prostaglandins (PGE2 and PGD2) in microglia and
CC macrophages, and also attenuated pro-inflammatorycytokine (TNF-alpha)
CC signaling in response to lipopolysaccharide stimulation
CC (PubMed:26779719, PubMed:23103940). In contrast, lipid profiles of
CC neurons are not impacted (PubMed:26779719). Endocannabinoid-mediated
CC retrograde synaptic suppression is intact in deficient mice
CC (PubMed:20159446). {ECO:0000269|PubMed:20147530,
CC ECO:0000269|PubMed:20159446, ECO:0000269|PubMed:23103940,
CC ECO:0000269|PubMed:26779719}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39734.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK081509; BAC38241.1; -; mRNA.
DR EMBL; AK086747; BAC39734.1; ALT_FRAME; mRNA.
DR EMBL; AK087884; BAC40033.1; -; mRNA.
DR EMBL; AK136372; BAE22951.1; -; mRNA.
DR EMBL; BC016105; AAH16105.2; -; mRNA.
DR CCDS; CCDS39370.1; -.
DR RefSeq; NP_659164.2; NM_144915.3.
DR AlphaFoldDB; Q91WC9; -.
DR SMR; Q91WC9; -.
DR STRING; 10090.ENSMUSP00000043088; -.
DR BindingDB; Q91WC9; -.
DR ChEMBL; CHEMBL5656; -.
DR ESTHER; mouse-DGLB; Lipase_3.
DR iPTMnet; Q91WC9; -.
DR PhosphoSitePlus; Q91WC9; -.
DR SwissPalm; Q91WC9; -.
DR EPD; Q91WC9; -.
DR MaxQB; Q91WC9; -.
DR PaxDb; Q91WC9; -.
DR PeptideAtlas; Q91WC9; -.
DR PRIDE; Q91WC9; -.
DR ProteomicsDB; 279861; -.
DR Antibodypedia; 24853; 101 antibodies from 21 providers.
DR DNASU; 231871; -.
DR Ensembl; ENSMUST00000045593; ENSMUSP00000043088; ENSMUSG00000039206.
DR GeneID; 231871; -.
DR KEGG; mmu:231871; -.
DR UCSC; uc009akj.1; mouse.
DR CTD; 221955; -.
DR MGI; MGI:2442032; Daglb.
DR VEuPathDB; HostDB:ENSMUSG00000039206; -.
DR eggNOG; KOG2088; Eukaryota.
DR GeneTree; ENSGT00940000156486; -.
DR HOGENOM; CLU_008300_2_1_1; -.
DR InParanoid; Q91WC9; -.
DR OMA; ARYIYRR; -.
DR OrthoDB; 191418at2759; -.
DR PhylomeDB; Q91WC9; -.
DR TreeFam; TF312928; -.
DR BRENDA; 3.1.1.116; 3474.
DR Reactome; R-MMU-426048; Arachidonate production from DAG.
DR BioGRID-ORCS; 231871; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Daglb; mouse.
DR PRO; PR:Q91WC9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91WC9; protein.
DR Bgee; ENSMUSG00000039206; Expressed in stroma of bone marrow and 216 other tissues.
DR Genevisible; Q91WC9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0071926; P:endocannabinoid signaling pathway; IBA:GO_Central.
DR GO; GO:0006690; P:icosanoid metabolic process; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; IMP:MGI.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..669
FT /note="Diacylglycerol lipase-beta"
FT /id="PRO_0000248351"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 467
FT /note="A -> T (in Ref. 1; BAC38241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73905 MW; 22FBCE0DC7A78522 CRC64;
MPGMVLFGRR WSLASDDLVF PGSFELFLRV LWWIVSLTLY LTHRRRLDCP GGVLLSTYLI
VLLVLLAVII CTVLAIVCVS MRGTICNPGP RKSMSKLLYI RLALFLPEMV WASLGAAWVA
KGIQCDRTVV IGIIATVIVS WIVIAATMVT IIFVFDPLGG KMAPYPPCIP EHLDSNSSNR
LLTGLKTAAK SVWETRVQFC CCCVGQDDNT RVAFSSTADL FSTYFSDTDL VPSDIAAGFT
LLHQQQDNIS HSREPPEVVT HTPGQPQETE LDAEVENCHH YMPFAAAAYG WPLYIYRNPF
TGLCRIGGDC CRARDIEYDA VEGDQHNCHF ASILKTTGLQ YRDFIHISFH DKVYELPFIV
VLDHRKESVV VAVRGTMSLQ DVLTDLSAES ETLELGIELQ DCVAHKGIAQ AARYIHRRLV
NDGILSQAFS VAPEYQLVLV GHSLGAGAAA LLAIMLRGAY PQVRAYAFSP PRGLLSKSLY
EYSKDFVVSL ILGMDVIPRL SVTNMEDLKR RILRVIANCN KPKYKILLHG CWYGLFGGSP
DNFPTELDEG TQGALTQPLL GEQTLLTRYS PGYCSSDSPL DSPTKYPTLY PPGRIIHLEE
EGGSGRFGCC SAAQYRARWA HEAEFSKILI GPKMLIDHMP DVMIRALDRV LADRTACVSC
PGQGGSSVP
