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P28321

- MGLL_YEAST

UniProt

P28321 - MGLL_YEAST

Protein

Monoglyceride lipase

Gene

YJU3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA).2 Publications

    Catalytic activityi

    Hydrolyzes glycerol monoesters of long-chain fatty acids.

    Kineticsi

    1. KM=260 µM for rac-13-oleoylglycerol1 Publication

    Vmax=10.3 mmol/h/mg enzyme1 Publication

    pH dependencei

    Active from pH 4.5 to 8.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231NucleophileBy similarity
    Active sitei251 – 2511Charge relay systemBy similarity
    Active sitei281 – 2811Charge relay systemBy similarity

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: SGD

    GO - Biological processi

    1. triglyceride catabolic process Source: UniProtKB-UniPathway
    2. triglyceride metabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:G3O-31885-MONOMER.
    YEAST:G3O-31885-MONOMER.
    ReactomeiREACT_189024. Acyl chain remodeling of DAG and TAG.
    UniPathwayiUPA00256.

    Protein family/group databases

    MEROPSiS33.993.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Monoglyceride lipase (EC:3.1.1.23)
    Short name:
    MGL
    Alternative name(s):
    Monoacylglycerol hydrolase
    Short name:
    MAG hydrolase
    Short name:
    MGH
    Monoacylglycerol lipase
    Short name:
    MAG lipase
    Short name:
    MAGL
    Serine hydrolase YJU3
    Gene namesi
    Name:YJU3
    Ordered Locus Names:YKL094W
    ORF Names:YKL441
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001577. YJU3.

    Subcellular locationi

    Cytoplasm. Endoplasmic reticulum. Lipid droplet. Mitochondrion outer membrane
    Note: Although the protein was identified in the cytoplasm, several membrane systems and lipid droplets, MGL activity was only measured in membrane fractions and lipid droplets.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. lipid particle Source: SGD
    3. membrane Source: SGD
    4. mitochondrial outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Lipid droplet, Membrane, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Monoglyceride lipasePRO_0000203164Add
    BLAST

    Proteomic databases

    MaxQBiP28321.
    PaxDbiP28321.
    PeptideAtlasiP28321.

    Expressioni

    Gene expression databases

    GenevestigatoriP28321.

    Interactioni

    Protein-protein interaction databases

    BioGridi34039. 30 interactions.
    IntActiP28321. 9 interactions.
    MINTiMINT-4083889.
    STRINGi4932.YKL094W.

    Structurei

    3D structure databases

    ProteinModelPortaliP28321.
    SMRiP28321. Positions 5-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2267.
    GeneTreeiENSGT00390000011364.
    HOGENOMiHOG000247969.
    OMAiNLSECKA.
    OrthoDBiEOG7Q8CZ5.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P28321-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPYPYKVQT TVPELQYENF DGAKFGYMFW PVQNGTNEVR GRVLLIHGFG    50
    EYTKIQFRLM DHLSLNGYES FTFDQRGAGV TSPGRSKGVT DEYHVFNDLE 100
    HFVEKNLSEC KAKGIPLFMW GHSMGGGICL NYACQGKHKN EISGYIGSGP 150
    LIILHPHTMY NKPTQIIAPL LAKFLPRVRI DTGLDLKGIT SDKAYRAFLG 200
    SDPMSVPLYG SFRQIHDFMQ RGAKLYKNEN NYIQKNFAKD KPVIIMHGQD 250
    DTINDPKGSE KFIQDCPSAD KELKLYPGAR HSIFSLETDK VFNTVFNDMK 300
    QWLDKHTTTE AKP 313
    Length:313
    Mass (Da):35,563
    Last modified:October 5, 2010 - v2
    Checksum:i5E0C3B431406DDF0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441I → V in CAA46971. (PubMed:1626433)Curated
    Sequence conflicti290 – 2901K → E in CAA46971. (PubMed:1626433)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66245 Genomic DNA. Translation: CAA46971.1.
    X71133 Genomic DNA. Translation: CAA50463.1.
    Z28094 Genomic DNA. Translation: CAA81932.1.
    BK006944 Genomic DNA. Translation: DAA09064.1.
    PIRiS37921.
    RefSeqiNP_012829.1. NM_001179660.1.

    Genome annotation databases

    EnsemblFungiiYKL094W; YKL094W; YKL094W.
    GeneIDi853768.
    KEGGisce:YKL094W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66245 Genomic DNA. Translation: CAA46971.1 .
    X71133 Genomic DNA. Translation: CAA50463.1 .
    Z28094 Genomic DNA. Translation: CAA81932.1 .
    BK006944 Genomic DNA. Translation: DAA09064.1 .
    PIRi S37921.
    RefSeqi NP_012829.1. NM_001179660.1.

    3D structure databases

    ProteinModelPortali P28321.
    SMRi P28321. Positions 5-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34039. 30 interactions.
    IntActi P28321. 9 interactions.
    MINTi MINT-4083889.
    STRINGi 4932.YKL094W.

    Protein family/group databases

    MEROPSi S33.993.

    Proteomic databases

    MaxQBi P28321.
    PaxDbi P28321.
    PeptideAtlasi P28321.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL094W ; YKL094W ; YKL094W .
    GeneIDi 853768.
    KEGGi sce:YKL094W.

    Organism-specific databases

    SGDi S000001577. YJU3.

    Phylogenomic databases

    eggNOGi COG2267.
    GeneTreei ENSGT00390000011364.
    HOGENOMi HOG000247969.
    OMAi NLSECKA.
    OrthoDBi EOG7Q8CZ5.

    Enzyme and pathway databases

    UniPathwayi UPA00256 .
    BioCyci MetaCyc:G3O-31885-MONOMER.
    YEAST:G3O-31885-MONOMER.
    Reactomei REACT_189024. Acyl chain remodeling of DAG and TAG.

    Miscellaneous databases

    NextBioi 974861.

    Gene expression databases

    Genevestigatori P28321.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the novel essential gene YJU2 and two flanking reading frames located within a 3.2 kb EcoRI fragment from chromosome X of Saccharomyces cerevisiae."
      Forrova H., Kolarov J., Ghislain M., Goffeau A.
      Yeast 8:419-422(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI physically localizes the MRB1 gene and reveals eight new open reading frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases."
      Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F., Bolotin-Fukuhara M.
      Yeast 9:1149-1155(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae."
      Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.
      J. Bacteriol. 181:6441-6448(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    6. Cited for: SUBCELLULAR LOCATION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast."
      Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S., Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.
      Mol. Cell. Proteomics 3:209-225(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A SERINE HYDROLASE BY MASS SPECTROMETRY.
    10. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
      Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
      Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Genetic manipulation of palmitoylethanolamide production and inactivation in Saccharomyces cerevisiae."
      Muccioli G.G., Sia A., Muchowski P.J., Stella N.
      PLoS ONE 4:E5942-E5942(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae."
      Heier C., Taschler U., Rengachari S., Oberer M., Wolinski H., Natter K., Kohlwein S.D., Leber R., Zimmermann R.
      Biochim. Biophys. Acta 1801:1063-1071(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiMGLL_YEAST
    AccessioniPrimary (citable) accession number: P28321
    Secondary accession number(s): D6VXJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2140 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3