Monoglyceride lipase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P28321 (MGLL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=260 µM for rac-1₃-oleoylglycerol Ref.12 V_max=10.3 mmol/h/mg enzyme pH dependence: Active from pH 4.5 to 8.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Lipid droplet Membrane Mitochondrion Mitochondrion outer membrane
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	triglyceride catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway triglyceride metabolic process Inferred from mutant phenotype Ref.12. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell lipid particle Inferred from direct assay Ref.5 Ref.12. Source: SGD mitochondrial outer membrane Inferred from direct assay Ref.10. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	acylglycerol lipase activity Inferred from mutant phenotype Ref.12. Source: SGD serine hydrolase activity Inferred from sequence model Ref.9. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Monoglyceride lipase

PRO_0000203164

Sites

Active site

123

Nucleophile By similarity

Active site

251

Charge relay system By similarity

Active site

281

Charge relay system By similarity

Experimental info

Sequence conflict

244

I → V in CAA46971. Ref.1

Sequence conflict

290

K → E in CAA46971. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P28321 [UniParc].

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

313

35,563

        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' referencesShow '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. Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S37921.
RefSeq	NP_012829.1. NM_001179660.1.
3D structure databases
ProteinModelPortal	P28321.
SMR	P28321. Positions 5-307.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28321. 9 interactions.
MINT	MINT-4083889.
STRING	4932.YKL094W.
Protein family/group databases
MEROPS	S33.993.
Proteomic databases
PaxDb	P28321.
PeptideAtlas	P28321.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL094W; YKL094W; YKL094W.
GeneID	853768.
KEGG	sce:YKL094W.
Organism-specific databases
SGD	S000001577. YJU3.
Phylogenomic databases
eggNOG	COG2267.
GeneTree	ENSGT00390000011364.
HOGENOM	HOG000247969.
OMA	RHSLFIE.
OrthoDB	EOG4J6W0X.
Enzyme and pathway databases
UniPathway	UPA00256.
Gene expression databases
Genevestigator	P28321.
GermOnline	YKL094W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974861.

Entry information

Entry name

MGLL_YEAST

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XI

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents