MGLL_MOUSE
ID MGLL_MOUSE Reviewed; 303 AA.
AC O35678; Q3V2R0; Q9D9G8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Monoglyceride lipase {ECO:0000312|MGI:MGI:1346042};
DE Short=MGL;
DE EC=3.1.1.23 {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566, ECO:0000269|PubMed:9341166};
DE AltName: Full=Monoacylglycerol lipase;
DE Short=MAGL;
GN Name=Mgll {ECO:0000312|MGI:MGI:1346042};
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, ACTIVE SITE, AND MUTAGENESIS OF SER-122; ASP-239; ASP-243;
RP HIS-269; HIS-272; HIS-284 AND HIS-292.
RC TISSUE=Adipose tissue;
RX PubMed=9341166; DOI=10.1074/jbc.272.43.27218;
RA Karlsson M., Contreras J.A., Hellman U., Tornqvist H., Holm C.;
RT "cDNA cloning, tissue distribution, and identification of the catalytic
RT triad of monoglyceride lipase. Evolutionary relationship to esterases,
RT lysophospholipases, and haloperoxidases.";
RL J. Biol. Chem. 272:27218-27223(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=11470505; DOI=10.1016/s0378-1119(01)00559-5;
RA Karlsson M., Reue K., Xia Y.-R., Lusis A.J., Langin D., Tornqvist H.,
RA Holm C.;
RT "Exon-intron organization and chromosomal localization of the mouse
RT monoglyceride lipase gene.";
RL Gene 272:11-18(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-58, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [6]
RP FUNCTION.
RX PubMed=17700715; DOI=10.1038/sj.bjp.0707425;
RA Comelli F., Giagnoni G., Bettoni I., Colleoni M., Costa B.;
RT "The inhibition of monoacylglycerol lipase by URB602 showed an anti-
RT inflammatory and anti-nociceptive effect in a murine model of acute
RT inflammation.";
RL Br. J. Pharmacol. 152:787-794(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=18096503; DOI=10.1016/j.chembiol.2007.11.006;
RA Blankman J.L., Simon G.M., Cravatt B.F.;
RT "A comprehensive profile of brain enzymes that hydrolyze the
RT endocannabinoid 2-arachidonoylglycerol.";
RL Chem. Biol. 14:1347-1356(2007).
RN [8]
RP FUNCTION.
RX PubMed=19029917; DOI=10.1038/nchembio.129;
RA Long J.Z., Li W., Booker L., Burston J.J., Kinsey S.G., Schlosburg J.E.,
RA Pavon F.J., Serrano A.M., Selley D.E., Parsons L.H., Lichtman A.H.,
RA Cravatt B.F.;
RT "Selective blockade of 2-arachidonoylglycerol hydrolysis produces
RT cannabinoid behavioral effects.";
RL Nat. Chem. Biol. 5:37-44(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20554061; DOI=10.1016/j.bbalip.2010.06.001;
RA Heier C., Taschler U., Rengachari S., Oberer M., Wolinski H., Natter K.,
RA Kohlwein S.D., Leber R., Zimmermann R.;
RT "Identification of Yju3p as functional orthologue of mammalian
RT monoglyceride lipase in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1801:1063-1071(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10 AND SER-189, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20729846; DOI=10.1038/nn.2616;
RA Schlosburg J.E., Blankman J.L., Long J.Z., Nomura D.K., Pan B.,
RA Kinsey S.G., Nguyen P.T., Ramesh D., Booker L., Burston J.J., Thomas E.A.,
RA Selley D.E., Sim-Selley L.J., Liu Q.S., Lichtman A.H., Cravatt B.F.;
RT "Chronic monoacylglycerol lipase blockade causes functional antagonism of
RT the endocannabinoid system.";
RL Nat. Neurosci. 13:1113-1119(2010).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21454566; DOI=10.1074/jbc.m110.215434;
RA Taschler U., Radner F.P., Heier C., Schreiber R., Schweiger M.,
RA Schoiswohl G., Preiss-Landl K., Jaeger D., Reiter B., Koefeler H.C.,
RA Wojciechowski J., Theussl C., Penninger J.M., Lass A., Haemmerle G.,
RA Zechner R., Zimmermann R.;
RT "Monoglyceride lipase deficiency in mice impairs lipolysis and attenuates
RT diet-induced insulin resistance.";
RL J. Biol. Chem. 286:17467-17477(2011).
CC -!- FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol
CC (PubMed:9341166, PubMed:17700715, PubMed:18096503, PubMed:19029917,
CC PubMed:20554061, PubMed:20729846, PubMed:21454566). Hydrolyzes the
CC endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the
CC regulation of endocannabinoid signaling, nociperception and perception
CC of pain (PubMed:9341166, PubMed:17700715, PubMed:18096503,
CC PubMed:19029917, PubMed:20554061, PubMed:20729846, PubMed:21454566).
CC Regulates the levels of fatty acids that serve as signaling molecules
CC and promote cancer cell migration, invasion and tumor growth (By
CC similarity). {ECO:0000250|UniProtKB:Q99685,
CC ECO:0000269|PubMed:17700715, ECO:0000269|PubMed:18096503,
CC ECO:0000269|PubMed:19029917, ECO:0000269|PubMed:20554061,
CC ECO:0000269|PubMed:20729846, ECO:0000269|PubMed:21454566,
CC ECO:0000269|PubMed:9341166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:18096503,
CC ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21454566,
CC ECO:0000269|PubMed:9341166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000269|PubMed:18096503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000269|PubMed:18096503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate;
CC Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:20554061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964;
CC Evidence={ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:21454566};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000269|PubMed:21454566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937; Evidence={ECO:0000269|PubMed:20554061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956;
CC Evidence={ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:20554061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC Evidence={ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75555; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) +
CC prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230,
CC ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) +
CC prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406,
CC ChEBI:CHEBI:85232; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy-
CC Delta(12,14)-prostaglandin J2 + glycerol + H(+);
CC Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238;
CC Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H(+)
CC + prostaglandin F2alpha; Xref=Rhea:RHEA:48300, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:90233; Evidence={ECO:0000250|UniProtKB:Q99685};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:9341166}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18096503}.
CC Membrane; Peripheral membrane protein {ECO:0000269|PubMed:18096503}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35678-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35678-2; Sequence=VSP_010315;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11470505}.
CC -!- DISRUPTION PHENOTYPE: Mice display a reduction in monoglyceride
CC hydrolase activity and a concomitant increase in monoglyceride levels
CC in adipose tissue, brain, and liver (PubMed:20554061). Ten-fold
CC increase in brain 2-arachidonoylglycerol levels, combined with low
CC levels of brain arachidonic acid (PubMed:20554061, PubMed:20729846).
CC {ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:20729846}.
CC -!- MISCELLANEOUS: Short-term inhibition causes analgesia, while long-term
CC inhibition causes tolerance to endocannabinoids acting on brain
CC cannabinoid receptor CNR1, and a reduction in brain cannabinoid
CC receptor CNR1 activity.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Monoacylglycerol
CC lipase family. {ECO:0000305}.
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DR EMBL; AJ001118; CAA04544.1; -; mRNA.
DR EMBL; AJ316580; CAC69874.1; -; mRNA.
DR EMBL; AK006949; BAB24800.1; -; mRNA.
DR EMBL; AK131645; BAE20737.1; -; mRNA.
DR EMBL; BC057965; AAH57965.1; -; mRNA.
DR CCDS; CCDS20338.1; -. [O35678-1]
DR RefSeq; NP_001159721.1; NM_001166249.1.
DR RefSeq; NP_001159722.1; NM_001166250.1.
DR RefSeq; NP_001159723.1; NM_001166251.1.
DR RefSeq; NP_035974.1; NM_011844.4. [O35678-1]
DR AlphaFoldDB; O35678; -.
DR SMR; O35678; -.
DR BioGRID; 204809; 2.
DR IntAct; O35678; 1.
DR STRING; 10090.ENSMUSP00000109215; -.
DR BindingDB; O35678; -.
DR ChEMBL; CHEMBL5774; -.
DR DrugCentral; O35678; -.
DR GuidetoPHARMACOLOGY; 1399; -.
DR SwissLipids; SLP:000000321; -.
DR SwissLipids; SLP:000000521; -.
DR ESTHER; mouse-MGLL; Monoglyceridelipase_lysophospholip.
DR MEROPS; S33.979; -.
DR iPTMnet; O35678; -.
DR PhosphoSitePlus; O35678; -.
DR SwissPalm; O35678; -.
DR jPOST; O35678; -.
DR MaxQB; O35678; -.
DR PaxDb; O35678; -.
DR PeptideAtlas; O35678; -.
DR PRIDE; O35678; -.
DR ProteomicsDB; 292234; -. [O35678-1]
DR ProteomicsDB; 292235; -. [O35678-2]
DR ABCD; O35678; 1 sequenced antibody.
DR Antibodypedia; 1635; 502 antibodies from 36 providers.
DR DNASU; 23945; -.
DR Ensembl; ENSMUST00000089449; ENSMUSP00000086872; ENSMUSG00000033174. [O35678-1]
DR Ensembl; ENSMUST00000113585; ENSMUSP00000109215; ENSMUSG00000033174. [O35678-1]
DR Ensembl; ENSMUST00000150180; ENSMUSP00000145068; ENSMUSG00000033174. [O35678-2]
DR GeneID; 23945; -.
DR KEGG; mmu:23945; -.
DR UCSC; uc009cvp.2; mouse. [O35678-1]
DR UCSC; uc009cvq.2; mouse. [O35678-2]
DR CTD; 11343; -.
DR MGI; MGI:1346042; Mgll.
DR VEuPathDB; HostDB:ENSMUSG00000033174; -.
DR eggNOG; KOG1455; Eukaryota.
DR GeneTree; ENSGT00390000011364; -.
DR InParanoid; O35678; -.
DR OrthoDB; 919091at2759; -.
DR PhylomeDB; O35678; -.
DR TreeFam; TF329184; -.
DR BRENDA; 3.1.1.23; 3474.
DR Reactome; R-MMU-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-MMU-426048; Arachidonate production from DAG.
DR UniPathway; UPA00256; -.
DR BioGRID-ORCS; 23945; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Mgll; mouse.
DR PRO; PR:O35678; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O35678; protein.
DR Bgee; ENSMUSG00000033174; Expressed in iris and 244 other tissues.
DR ExpressionAtlas; O35678; baseline and differential.
DR Genevisible; O35678; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043196; C:varicosity; IDA:MGI.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0030516; P:regulation of axon extension; IMP:MGI.
DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IMP:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Hydrolase; Lipid biosynthesis; Lipid degradation;
KW Lipid metabolism; Membrane; Nitration; Phosphoprotein; Reference proteome;
KW Serine esterase.
FT CHAIN 1..303
FT /note="Monoglyceride lipase"
FT /id="PRO_0000191266"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9341166"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:9341166"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:9341166"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 78..303
FT /note="VGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISI
FT LVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNK
FT SEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGA
FT YLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP ->
FT AVMLSAALQSALVIFVRLIWQIIFQGYPRGVCCGGRCHY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010315"
FT MUTAGEN 122
FT /note="S->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 239
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 243
FT /note="D->A: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 269
FT /note="H->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 272
FT /note="H->A: Reduces activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 284
FT /note="H->A: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:9341166"
FT MUTAGEN 292
FT /note="H->A: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:9341166"
SQ SEQUENCE 303 AA; 33388 MW; CB753ECDE38EBEC1 CRC64;
MPEASSPRRT PQNVPYQDLP HLVNADGQYL FCRYWKPSGT PKALIFVSHG AGEHCGRYDE
LAHMLKGLDM LVFAHDHVGH GQSEGERMVV SDFQVFVRDV LQHVDTIQKD YPDVPIFLLG
HSMGGAISIL VAAERPTYFS GMVLISPLVL ANPESASTLK VLAAKLLNFV LPNMTLGRID
SSVLSRNKSE VDLYNSDPLV CRAGLKVCFG IQLLNAVARV ERAMPRLTLP FLLLQGSADR
LCDSKGAYLL MESSRSQDKT LKMYEGAYHV LHRELPEVTN SVLHEVNSWV SHRIAAAGAG
CPP
