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Protein

Monoglyceride lipase

Gene

YJU3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

Kineticsi

  1. KM=260 µM for rac-13-oleoylglycerol1 Publication
  1. Vmax=10.3 mmol/h/mg enzyme1 Publication

pH dependencei

Active from pH 4.5 to 8.1 Publication

Pathwayi: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway triacylglycerol degradation and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei123NucleophileBy similarity1
Active sitei251Charge relay systemBy similarity1
Active sitei281Charge relay systemBy similarity1

GO - Molecular functioni

  • acylglycerol lipase activity Source: SGD

GO - Biological processi

  • regulation of signal transduction Source: GO_Central
  • triglyceride catabolic process Source: UniProtKB-UniPathway
  • triglyceride metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:G3O-31885-MONOMER.
YEAST:G3O-31885-MONOMER.
ReactomeiR-SCE-1482883. Acyl chain remodeling of DAG and TAG.
R-SCE-426048. Arachidonate production from DAG.
UniPathwayiUPA00256.

Protein family/group databases

ESTHERiyeast-mgll. Monoglyceridelipase_lysophospholip.
MEROPSiS33.993.

Chemistry databases

SwissLipidsiSLP:000000055.

Names & Taxonomyi

Protein namesi
Recommended name:
Monoglyceride lipaseCurated (EC:3.1.1.231 Publication)
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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL094W.
SGDiS000001577. YJU3.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • lipid particle Source: SGD
  • membrane Source: SGD
  • mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002031641 – 313Monoglyceride lipaseAdd BLAST313

Proteomic databases

MaxQBiP28321.
PRIDEiP28321.

Interactioni

Protein-protein interaction databases

BioGridi34039. 32 interactors.
IntActiP28321. 9 interactors.
MINTiMINT-4083889.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 20Combined sources5
Beta strandi23 – 30Combined sources8
Beta strandi34 – 36Combined sources3
Beta strandi40 – 46Combined sources7
Helixi53 – 56Combined sources4
Helixi57 – 65Combined sources9
Beta strandi68 – 73Combined sources6
Turni79 – 81Combined sources3
Helixi84 – 86Combined sources3
Helixi92 – 113Combined sources22
Beta strandi117 – 122Combined sources6
Helixi124 – 135Combined sources12
Turni137 – 141Combined sources5
Beta strandi143 – 149Combined sources7
Beta strandi152 – 154Combined sources3
Helixi156 – 161Combined sources6
Helixi164 – 170Combined sources7
Turni171 – 174Combined sources4
Helixi186 – 189Combined sources4
Helixi193 – 201Combined sources9
Turni203 – 205Combined sources3
Helixi212 – 227Combined sources16
Helixi229 – 231Combined sources3
Helixi232 – 236Combined sources5
Beta strandi243 – 248Combined sources6
Beta strandi252 – 254Combined sources3
Helixi256 – 265Combined sources10
Beta strandi269 – 276Combined sources8
Turni283 – 286Combined sources4
Helixi289 – 305Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWNX-ray2.49A/B/C/D2-313[»]
4ZXFX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliP28321.
SMRiP28321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000011364.
HOGENOMiHOG000247969.
InParanoidiP28321.
KOiK01054.
OMAiKHERNTH.
OrthoDBiEOG092C4I0R.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

P28321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPYPYKVQT TVPELQYENF DGAKFGYMFW PVQNGTNEVR GRVLLIHGFG
60 70 80 90 100
EYTKIQFRLM DHLSLNGYES FTFDQRGAGV TSPGRSKGVT DEYHVFNDLE
110 120 130 140 150
HFVEKNLSEC KAKGIPLFMW GHSMGGGICL NYACQGKHKN EISGYIGSGP
160 170 180 190 200
LIILHPHTMY NKPTQIIAPL LAKFLPRVRI DTGLDLKGIT SDKAYRAFLG
210 220 230 240 250
SDPMSVPLYG SFRQIHDFMQ RGAKLYKNEN NYIQKNFAKD KPVIIMHGQD
260 270 280 290 300
DTINDPKGSE KFIQDCPSAD KELKLYPGAR HSIFSLETDK VFNTVFNDMK
310
QWLDKHTTTE AKP
Length:313
Mass (Da):35,563
Last modified:October 5, 2010 - v2
Checksum:i5E0C3B431406DDF0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti244I → V in CAA46971 (PubMed:1626433).Curated1
Sequence conflicti290K → E in CAA46971 (PubMed:1626433).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWNX-ray2.49A/B/C/D2-313[»]
4ZXFX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliP28321.
SMRiP28321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34039. 32 interactors.
IntActiP28321. 9 interactors.
MINTiMINT-4083889.

Chemistry databases

SwissLipidsiSLP:000000055.

Protein family/group databases

ESTHERiyeast-mgll. Monoglyceridelipase_lysophospholip.
MEROPSiS33.993.

Proteomic databases

MaxQBiP28321.
PRIDEiP28321.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YKL094W.
SGDiS000001577. YJU3.

Phylogenomic databases

GeneTreeiENSGT00390000011364.
HOGENOMiHOG000247969.
InParanoidiP28321.
KOiK01054.
OMAiKHERNTH.
OrthoDBiEOG092C4I0R.

Enzyme and pathway databases

UniPathwayiUPA00256.
BioCyciMetaCyc:G3O-31885-MONOMER.
YEAST:G3O-31885-MONOMER.
ReactomeiR-SCE-1482883. Acyl chain remodeling of DAG and TAG.
R-SCE-426048. Arachidonate production from DAG.

Miscellaneous databases

PROiP28321.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 133 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.