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P28321 (MGLL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monoglyceride lipase

Short name=MGL
EC=3.1.1.23
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 names
Name:YJU3
Ordered Locus Names:YKL094W
ORF Names:YKL441
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.11 Ref.12

Catalytic activity

Hydrolyzes glycerol monoesters of long-chain fatty acids.

Pathway

Glycerolipid metabolism; triacylglycerol degradation.

Subcellular location

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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.12

Miscellaneous

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

Sequence similarities

Belongs to the AB hydrolase superfamily. Monoacylglycerol lipase family.

Biophysicochemical properties

Kinetic parameters:

KM=260 µM for rac-13-oleoylglycerol Ref.12

Vmax=10.3 mmol/h/mg enzyme

pH dependence:

Active from pH 4.5 to 8.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Monoglyceride lipase
PRO_0000203164

Sites

Active site1231Nucleophile By similarity
Active site2511Charge relay system By similarity
Active site2811Charge relay system By similarity

Experimental info

Sequence conflict2441I → V in CAA46971. Ref.1
Sequence conflict2901K → E in CAA46971. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28321 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 5E0C3B431406DDF0

FASTA31335,563
        10         20         30         40         50         60 
MAPYPYKVQT TVPELQYENF DGAKFGYMFW PVQNGTNEVR GRVLLIHGFG EYTKIQFRLM 

        70         80         90        100        110        120 
DHLSLNGYES FTFDQRGAGV TSPGRSKGVT DEYHVFNDLE HFVEKNLSEC KAKGIPLFMW 

       130        140        150        160        170        180 
GHSMGGGICL NYACQGKHKN EISGYIGSGP LIILHPHTMY NKPTQIIAPL LAKFLPRVRI 

       190        200        210        220        230        240 
DTGLDLKGIT SDKAYRAFLG SDPMSVPLYG SFRQIHDFMQ RGAKLYKNEN NYIQKNFAKD 

       250        260        270        280        290        300 
KPVIIMHGQD DTINDPKGSE KFIQDCPSAD KELKLYPGAR HSIFSLETDK VFNTVFNDMK 

       310 
QWLDKHTTTE AKP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Subcellular localization of the yeast proteome."
Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P., Gerstein M., Roeder G.S., Snyder M.
Genes Dev. 16:707-719(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66245 Genomic DNA. Translation: CAA46971.1.
X71133 Genomic DNA. Translation: CAA50463.1.
Z28094 Genomic DNA. Translation: CAA81932.1.
BK006944 Genomic DNA. Translation: DAA09064.1.
PIRS37921.
RefSeqNP_012829.1. NM_001179660.1.

3D structure databases

ProteinModelPortalP28321.
SMRP28321. Positions 5-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34039. 30 interactions.
IntActP28321. 9 interactions.
MINTMINT-4083889.
STRING4932.YKL094W.

Protein family/group databases

MEROPSS33.993.

Proteomic databases

MaxQBP28321.
PaxDbP28321.
PeptideAtlasP28321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL094W; YKL094W; YKL094W.
GeneID853768.
KEGGsce:YKL094W.

Organism-specific databases

SGDS000001577. YJU3.

Phylogenomic databases

eggNOGCOG2267.
GeneTreeENSGT00390000011364.
HOGENOMHOG000247969.
OMANLSECKA.
OrthoDBEOG7Q8CZ5.

Enzyme and pathway databases

BioCycMetaCyc:G3O-31885-MONOMER.
YEAST:G3O-31885-MONOMER.
UniPathwayUPA00256.

Gene expression databases

GenevestigatorP28321.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 2 hits.
ProtoNetSearch...

Other

NextBio974861.

Entry information

Entry nameMGLL_YEAST
AccessionPrimary (citable) accession number: P28321
Secondary accession number(s): D6VXJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways