MGLL_SCHPO
ID MGLL_SCHPO Reviewed; 378 AA.
AC O94305;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative monoglyceride lipase {ECO:0000305};
DE Short=MGL;
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:P28321};
DE AltName: Full=Fatty acid ethyl ester hydrolase {ECO:0000250|UniProtKB:P28321};
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;
GN Name=mgl1; ORFNames=SPCC5E4.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA21960.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and
CC glycerol. Has a strong preference for monounsaturated monoglycerides.
CC Required for efficient degradation of MAG, short-lived intermediates of
CC glycerolipid metabolism which may also function as lipid signaling
CC molecules. Controls inactivation of the signaling lipid N-
CC palmitoylethanolamine (PEA). Involved in fatty acid ethyl ester (FAEE)
CC catabolism. FAEEs are non-oxidative metabolites of ethanol that are
CC transiently incorporated into lipid droplets (LDs). Their mobilization
CC by LD-resident FAEE hydrolases facilitates a controlled metabolism of
CC these potentially toxic lipid metabolites.
CC {ECO:0000250|UniProtKB:P28321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P28321};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000250|UniProtKB:P28321}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P28321}.
CC Cytoplasm {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P28321}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P28321}. Note=Although the protein is identified
CC in the cytoplasm, several membrane systems and lipid droplets, MGL
CC activity is only measured in membrane fractions and lipid droplets.
CC {ECO:0000250|UniProtKB:P28321}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Monoacylglycerol
CC lipase family. {ECO:0000255}.
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DR EMBL; CU329672; CAA21960.1; -; Genomic_DNA.
DR PIR; T41456; T41456.
DR RefSeq; NP_587904.1; NM_001022896.2.
DR AlphaFoldDB; O94305; -.
DR SMR; O94305; -.
DR IntAct; O94305; 1.
DR STRING; 4896.SPCC5E4.05c.1; -.
DR ESTHER; schpo-SPCC5E4.05C; Monoglyceridelipase_lysophospholip.
DR iPTMnet; O94305; -.
DR MaxQB; O94305; -.
DR PaxDb; O94305; -.
DR PRIDE; O94305; -.
DR EnsemblFungi; SPCC5E4.05c.1; SPCC5E4.05c.1:pep; SPCC5E4.05c.
DR GeneID; 2538799; -.
DR KEGG; spo:SPCC5E4.05c; -.
DR PomBase; SPCC5E4.05c; mgl1.
DR VEuPathDB; FungiDB:SPCC5E4.05c; -.
DR eggNOG; KOG1455; Eukaryota.
DR HOGENOM; CLU_026209_5_2_1; -.
DR InParanoid; O94305; -.
DR OMA; FHGFSDH; -.
DR PhylomeDB; O94305; -.
DR Reactome; R-SPO-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-SPO-426048; Arachidonate production from DAG.
DR UniPathway; UPA00256; -.
DR PRO; PR:O94305; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:PomBase.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISO:PomBase.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IC:PomBase.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid droplet; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..378
FT /note="Putative monoglyceride lipase"
FT /id="PRO_0000312656"
FT REGION 276..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT COMPBIAS 289..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 378 AA; 41624 MW; BFB219E181B04259 CRC64;
MADLYTKDWT DVKDKPVARV VFIHGFGEHV NAYPEFFEAL NERNIEVYTF DQRGFGHSRK
GGPKKQGCTG GWSLVFPDLD YQILRASDTE LPLFLWGHSM GGGLALRYGI SGTHRHKLAG
VIAQAPMLRC HPDTEPNFLL RKALTLVSKV HPNFLFDSDV QSQHITRDEA VNQRLQDDPL
VSSVGSLQVF SDMLNRGTKT IELAPQFFLP LLITHGTDDN VTCSDSSKEF YENAGTKDKT
YQSYPGFYHS LHIEKKPEVY EYLDKVAAWI YEHSKPSETV KSEQETAVEH PKPTATTSAP
SASPTGVPVE EESHKATSDA VPPAEAKPEP VPASAAERAP TSESTTVPET IVASTTKVIS
EPAPRVTTAA TADIVTNK
