ID   MGLL_YEAST              Reviewed;         313 AA.
AC   P28321; D6VXJ4;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Monoglyceride lipase {ECO:0000305};
DE            Short=MGL;
DE            EC=3.1.1.23 {ECO:0000269|PubMed:20554061};
DE   AltName: Full=Fatty acid ethyl ester hydrolase {ECO:0000303|PubMed:27036938};
DE            Short=FAEE hydrolase;
DE   AltName: Full=Monoacylglycerol hydrolase;
DE            Short=MAG hydrolase;
DE            Short=MGH;
DE   AltName: Full=Monoacylglycerol lipase;
DE            Short=MAG lipase;
DE            Short=MAGL;
DE   AltName: Full=Serine hydrolase YJU3;
GN   Name=YJU3; OrderedLocusNames=YKL094W; ORFNames=YKL441;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1626433; DOI=10.1002/yea.320080509;
RA   Forrova H., Kolarov J., Ghislain M., Goffeau A.;
RT   "Sequence of the novel essential gene YJU2 and two flanking reading frames
RT   located within a 3.2 kb EcoRI fragment from chromosome X of Saccharomyces
RT   cerevisiae.";
RL   Yeast 8:419-422(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8256524; DOI=10.1002/yea.320091016;
RA   Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA   Bolotin-Fukuhara M.;
RT   "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT   physically localizes the MRB1 gene and reveals eight new open reading
RT   frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL   Yeast 9:1149-1155(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA   Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT   "Identification and characterization of major lipid particle proteins of
RT   the yeast Saccharomyces cerevisiae.";
RL   J. Bacteriol. 181:6441-6448(1999).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11914276; DOI=10.1101/gad.970902;
RA   Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA   Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA   Gerstein M., Roeder G.S., Snyder M.;
RT   "Subcellular localization of the yeast proteome.";
RL   Genes Dev. 16:707-719(2002).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   IDENTIFICATION AS A SERINE HYDROLASE BY MASS SPECTROMETRY.
RX   PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA   Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA   Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT   "Synergistic computational and experimental proteomics approaches for more
RT   accurate detection of active serine hydrolases in yeast.";
RL   Mol. Cell. Proteomics 3:209-225(2004).
RN   [10]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA   Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA   Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT   "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT   accumulation of a subclass of preproteins.";
RL   Mol. Biol. Cell 17:1436-1450(2006).
RN   [11]
RP   FUNCTION.
RX   PubMed=19529773; DOI=10.1371/journal.pone.0005942;
RA   Muccioli G.G., Sia A., Muchowski P.J., Stella N.;
RT   "Genetic manipulation of palmitoylethanolamide production and inactivation
RT   in Saccharomyces cerevisiae.";
RL   PLoS ONE 4:E5942-E5942(2009).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
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   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA   Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA   Wagner B., Karas M., Daum G.;
RT   "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT   lipidome meets proteome.";
RL   Biochim. Biophys. Acta 1811:1165-1176(2011).
RN   [14]
RP   LIPASE MOTIF.
RX   DOI=10.1007/s11515-011-1142-6;
RA   Grillitsch K., Daum G.;
RT   "Triacylglycerol lipases of the yeast.";
RL   Front. Biol. 6:219-230(2011).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24868093; DOI=10.1194/jlr.m050229;
RA   Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA   Haas J., Walther T.C., Farese R.V. Jr.;
RT   "High-confidence proteomic analysis of yeast lipid droplets identifies
RT   additional droplet proteins and reveals connections to dolichol synthesis
RT   and sterol acetylation.";
RL   J. Lipid Res. 55:1465-1477(2014).
RN   [16]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=27036938; DOI=10.1074/jbc.m115.705541;
RA   Heier C., Taschler U., Radulovic M., Aschauer P., Eichmann T.O., Grond S.,
RA   Wolinski H., Oberer M., Zechner R., Kohlwein S.D., Zimmermann R.;
RT   "Monoacylglycerol lipases act as evolutionarily conserved regulators of
RT   non-oxidative ethanol metabolism.";
RL   J. Biol. Chem. 291:11865-11875(2016).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP   AND FUNCTION.
RX   PubMed=26869448; DOI=10.1016/j.bbalip.2016.02.005;
RA   Aschauer P., Rengachari S., Lichtenegger J., Schittmayer M., Das K.M.,
RA   Mayer N., Breinbauer R., Birner-Gruenberger R., Gruber C.C., Zimmermann R.,
RA   Gruber K., Oberer M.;
RT   "Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase
RT   Yju3p.";
RL   Biochim. Biophys. Acta 1861:462-470(2016).
CC   -!- FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and
CC       glycerol (PubMed:20554061). Has a strong preference for monounsaturated
CC       monoglycerides (PubMed:26869448). Required for efficient degradation of
CC       MAG, short-lived intermediates of glycerolipid metabolism which may
CC       also function as lipid signaling molecules. Controls inactivation of
CC       the signaling lipid N-palmitoylethanolamine (PEA) (PubMed:19529773).
CC       Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-
CC       oxidative metabolites of ethanol that are transiently incorporated into
CC       lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases
CC       facilitates a controlled metabolism of these potentially toxic lipid
CC       metabolites (PubMed:27036938). {ECO:0000269|PubMed:19529773,
CC       ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:26869448,
CC       ECO:0000269|PubMed:27036938}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC         EC=3.1.1.23; Evidence={ECO:0000269|PubMed:20554061};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid ethyl ester + H2O = a fatty acid + ethanol +
CC         H(+); Xref=Rhea:RHEA:50148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16236, ChEBI:CHEBI:28868, ChEBI:CHEBI:78206;
CC         Evidence={ECO:0000269|PubMed:27036938};
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:20554061,
CC         ECO:0000269|PubMed:26869448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC         Evidence={ECO:0000305|PubMed:20554061};
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:0000269|PubMed:20554061};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC         Evidence={ECO:0000305|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         ECO:0000269|PubMed:27036938};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC         Evidence={ECO:0000305|PubMed:20554061, ECO:0000305|PubMed:27036938};
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:0000305|PubMed:20554061};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethyl hexadecanoate + H2O = ethanol + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:50132, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:84932;
CC         Evidence={ECO:0000269|PubMed:27036938};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50133;
CC         Evidence={ECO:0000305|PubMed:27036938};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethyl (9Z)-octadecenoate + H2O = (9Z)-octadecenoate + ethanol
CC         + H(+); Xref=Rhea:RHEA:50136, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16236, ChEBI:CHEBI:30823, ChEBI:CHEBI:84940;
CC         Evidence={ECO:0000269|PubMed:27036938};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50137;
CC         Evidence={ECO:0000305|PubMed:27036938};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethyl (9Z)-hexadecenoate + H2O = (9Z)-hexadecenoate + ethanol
CC         + H(+); Xref=Rhea:RHEA:50144, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16236, ChEBI:CHEBI:32372, ChEBI:CHEBI:84934;
CC         Evidence={ECO:0000269|PubMed:27036938};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50145;
CC         Evidence={ECO:0000305|PubMed:27036938};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethyl octadecanoate + H2O = ethanol + H(+) + octadecanoate;
CC         Xref=Rhea:RHEA:50316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16236, ChEBI:CHEBI:25629, ChEBI:CHEBI:84936;
CC         Evidence={ECO:0000269|PubMed:27036938};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50317;
CC         Evidence={ECO:0000305|PubMed:27036938};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=260 uM for rac-1(3)-oleoylglycerol {ECO:0000269|PubMed:20554061};
CC         Vmax=10.3 mmol/h/mg enzyme {ECO:0000269|PubMed:20554061};
CC       pH dependence:
CC         Active from pH 4.5 to 8. {ECO:0000269|PubMed:20554061};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC       {ECO:0000269|PubMed:20554061}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC       ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21820081,
CC       ECO:0000269|PubMed:24868093}. Cytoplasm {ECO:0000269|PubMed:11914276}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:14562095}. Mitochondrion
CC       outer membrane {ECO:0000269|PubMed:16407407}. Note=Although the protein
CC       is identified in the cytoplasm, several membrane systems and lipid
CC       droplets, MGL activity is only measured in membrane fractions and lipid
CC       droplets. {ECO:0000269|PubMed:20554061}.
CC   -!- MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Monoacylglycerol
CC       lipase family. {ECO:0000305}.
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DR   EMBL; X66245; CAA46971.1; -; Genomic_DNA.
DR   EMBL; X71133; CAA50463.1; -; Genomic_DNA.
DR   EMBL; Z28094; CAA81932.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09064.1; -; Genomic_DNA.
DR   PIR; S37921; S37921.
DR   RefSeq; NP_012829.1; NM_001179660.1.
DR   PDB; 4ZWN; X-ray; 2.49 A; A/B/C/D=2-313.
DR   PDB; 4ZXF; X-ray; 2.50 A; A/B/C/D=1-313.
DR   PDBsum; 4ZWN; -.
DR   PDBsum; 4ZXF; -.
DR   AlphaFoldDB; P28321; -.
DR   SMR; P28321; -.
DR   BioGRID; 34039; 70.
DR   IntAct; P28321; 9.
DR   MINT; P28321; -.
DR   STRING; 4932.YKL094W; -.
DR   SwissLipids; SLP:000000055; -.
DR   ESTHER; yeast-mgll; Monoglyceridelipase_lysophospholip.
DR   MEROPS; S33.993; -.
DR   iPTMnet; P28321; -.
DR   MaxQB; P28321; -.
DR   PaxDb; 4932-YKL094W; -.
DR   PeptideAtlas; P28321; -.
DR   EnsemblFungi; YKL094W_mRNA; YKL094W; YKL094W.
DR   GeneID; 853768; -.
DR   KEGG; sce:YKL094W; -.
DR   AGR; SGD:S000001577; -.
DR   SGD; S000001577; YJU3.
DR   VEuPathDB; FungiDB:YKL094W; -.
DR   eggNOG; KOG1455; Eukaryota.
DR   GeneTree; ENSGT00390000011364; -.
DR   HOGENOM; CLU_026209_5_0_1; -.
DR   InParanoid; P28321; -.
DR   OMA; LVWHGPM; -.
DR   OrthoDB; 4295233at2759; -.
DR   BioCyc; MetaCyc:G3O-31885-MONOMER; -.
DR   BioCyc; YEAST:G3O-31885-MONOMER; -.
DR   UniPathway; UPA00256; -.
DR   BioGRID-ORCS; 853768; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P28321; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P28321; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IMP:SGD.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0017171; F:serine hydrolase activity; HDA:SGD.
DR   GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006641; P:triglyceride metabolic process; IMP:SGD.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   PANTHER; PTHR11614:SF87; MONOGLYCERIDE LIPASE; 1.
DR   PANTHER; PTHR11614; PHOSPHOLIPASE-RELATED; 1.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid droplet;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Monoglyceride lipase"
FT                   /id="PRO_0000203164"
FT   MOTIF           121..125
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000305|Ref.14"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:26869448"
FT   ACT_SITE        251
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:26869448"
FT   ACT_SITE        281
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:26869448"
FT   CONFLICT        244
FT                   /note="I -> V (in Ref. 1; CAA46971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="K -> E (in Ref. 1; CAA46971)"
FT                   /evidence="ECO:0000305"
FT   STRAND          16..20
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          23..30
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           57..65
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           92..113
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           124..135
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   TURN            137..141
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           156..161
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           164..170
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   TURN            171..174
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           212..227
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           232..236
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          243..248
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           256..265
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   STRAND          269..276
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   TURN            283..286
FT                   /evidence="ECO:0007829|PDB:4ZWN"
FT   HELIX           289..305
FT                   /evidence="ECO:0007829|PDB:4ZWN"
SQ   SEQUENCE   313 AA;  35563 MW;  5E0C3B431406DDF0 CRC64;
     MAPYPYKVQT TVPELQYENF DGAKFGYMFW PVQNGTNEVR GRVLLIHGFG EYTKIQFRLM
     DHLSLNGYES FTFDQRGAGV TSPGRSKGVT DEYHVFNDLE HFVEKNLSEC KAKGIPLFMW
     GHSMGGGICL NYACQGKHKN EISGYIGSGP LIILHPHTMY NKPTQIIAPL LAKFLPRVRI
     DTGLDLKGIT SDKAYRAFLG SDPMSVPLYG SFRQIHDFMQ RGAKLYKNEN NYIQKNFAKD
     KPVIIMHGQD DTINDPKGSE KFIQDCPSAD KELKLYPGAR HSIFSLETDK VFNTVFNDMK
     QWLDKHTTTE AKP
//