Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Monoglyceride lipase

Gene

MGLL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (By similarity). Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333).By similarity1 Publication

Catalytic activityi

Hydrolyzes glycerol monoesters of long-chain fatty acids.By similarity

Kineticsi

  1. KM=110 µM for 2-arachidonoyglycerol1 Publication
  1. Vmax=120 nmol/min/mg enzyme toward 2-arachidonoyglycerol1 Publication

Pathwayi: triacylglycerol degradation

This protein is involved in the pathway triacylglycerol degradation, which is part of Glycerolipid metabolism.By similarity
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 sitei122Nucleophile1 Publication1
Active sitei239Charge relay system1 Publication1
Active sitei269Charge relay system1 Publication1

GO - Molecular functioni

  • acylglycerol lipase activity Source: UniProtKB
  • lysophospholipase activity Source: ProtInc
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciZFISH:HS01140-MONOMER.
BRENDAi3.1.1.23. 2681.
ReactomeiR-HSA-1482883. Acyl chain remodeling of DAG and TAG.
R-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-426048. Arachidonate production from DAG.
UniPathwayiUPA00256.

Protein family/group databases

ESTHERihuman-MGLL. Monoglyceridelipase_lysophospholip.
MEROPSiS33.979.

Chemistry databases

SwissLipidsiSLP:000000315.

Names & Taxonomyi

Protein namesi
Recommended name:
Monoglyceride lipaseImported (EC:3.1.1.231 Publication)
Short name:
MGLImported
Alternative name(s):
HU-K51 Publication
Lysophospholipase homolog
Lysophospholipase-like
Monoacylglycerol lipase1 Publication
Short name:
MAGL1 Publication
Gene namesi
Name:MGLLImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17038. MGLL.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi11343.
OpenTargetsiENSG00000074416.
PharmGKBiPA30789.

Chemistry databases

ChEMBLiCHEMBL4191.
GuidetoPHARMACOLOGYi1399.

Polymorphism and mutation databases

BioMutaiMGLL.
DMDMi47117287.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001912651 – 303Monoglyceride lipaseAdd BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphothreonineBy similarity1
Modified residuei58Nitrated tyrosineBy similarity1

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ99685.
PaxDbiQ99685.
PeptideAtlasiQ99685.
PRIDEiQ99685.

PTM databases

iPTMnetiQ99685.
PhosphoSitePlusiQ99685.

Expressioni

Tissue specificityi

Detected in adipose tissue, lung, liver, kidney, brain and heart.1 Publication

Gene expression databases

BgeeiENSG00000074416.
CleanExiHS_MGLL.
ExpressionAtlasiQ99685. baseline and differential.
GenevisibleiQ99685. HS.

Organism-specific databases

HPAiHPA011348.
HPA011993.
HPA011994.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi116471. 4 interactors.
IntActiQ99685. 3 interactors.
MINTiMINT-1414843.
STRINGi9606.ENSP00000265052.

Chemistry databases

BindingDBiQ99685.

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 18Combined sources3
Beta strandi21 – 23Combined sources3
Beta strandi29 – 35Combined sources7
Beta strandi42 – 48Combined sources7
Helixi55 – 58Combined sources4
Helixi59 – 67Combined sources9
Beta strandi70 – 75Combined sources6
Helixi94 – 110Combined sources17
Beta strandi116 – 121Combined sources6
Helixi123 – 134Combined sources12
Turni136 – 138Combined sources3
Beta strandi140 – 146Combined sources7
Beta strandi148 – 151Combined sources4
Helixi153 – 168Combined sources16
Helixi181 – 183Combined sources3
Helixi188 – 195Combined sources8
Beta strandi198 – 200Combined sources3
Helixi207 – 223Combined sources17
Helixi224 – 226Combined sources3
Beta strandi231 – 236Combined sources6
Beta strandi240 – 242Combined sources3
Helixi244 – 253Combined sources10
Beta strandi257 – 264Combined sources8
Helixi271 – 273Combined sources3
Helixi276 – 292Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HJUX-ray2.20A/B2-303[»]
3JW8X-ray2.10A/B1-303[»]
3JWEX-ray2.70A/B1-303[»]
3PE6X-ray1.35A1-303[»]
4UUQX-ray2.36A/B1-303[»]
ProteinModelPortaliQ99685.
SMRiQ99685.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99685.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1455. Eukaryota.
COG2267. LUCA.
GeneTreeiENSGT00390000011364.
HOGENOMiHOG000003227.
HOVERGENiHBG049220.
InParanoidiQ99685.
KOiK01054.
PhylomeDBiQ99685.
TreeFamiTF329184.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99685-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG
60 70 80 90 100
AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV
110 120 130 140 150
LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL
160 170 180 190 200
ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI
210 220 230 240 250
CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL
260 270 280 290 300
MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA

SPP
Length:303
Mass (Da):33,261
Last modified:May 10, 2004 - v2
Checksum:i80E754F126EE64DE
GO
Isoform 2 (identifier: Q99685-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → METGPEDPSSM
     161-190: Missing.

Show »
Length:283
Mass (Da):31,149
Checksum:i5EE1BFA7CC9FBF26
GO

Sequence cautioni

The sequence AAB39616 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH00551 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH06230 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG37910 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAG33116 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW79330 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW79331 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti144L → P in BAG52334 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451381M → METGPEDPSSM in isoform 2. 1 Publication1
Alternative sequenceiVSP_045139161 – 190Missing in isoform 2. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67963 mRNA. Translation: AAB39616.1. Different initiation.
AJ270950 mRNA. Translation: CAC43316.1.
AK091314 mRNA. Translation: BAG52334.1.
AK315529 mRNA. Translation: BAG37910.1. Different initiation.
AK304844 mRNA. Translation: BAH14267.1.
CR456835 mRNA. Translation: CAG33116.1. Different initiation.
AC023593 Genomic DNA. No translation available.
AC117480 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79330.1. Different initiation.
CH471052 Genomic DNA. Translation: EAW79331.1. Different initiation.
BC000551 mRNA. Translation: AAH00551.1. Different initiation.
BC006230 mRNA. Translation: AAH06230.1. Different initiation.
BX640777 mRNA. Translation: CAE45873.1.
CCDSiCCDS43148.1. [Q99685-1]
CCDS58852.1. [Q99685-2]
RefSeqiNP_001003794.1. NM_001003794.2. [Q99685-1]
NP_001243514.1. NM_001256585.1. [Q99685-2]
NP_009214.1. NM_007283.6.
UniGeneiHs.277035.

Genome annotation databases

EnsembliENST00000398104; ENSP00000381176; ENSG00000074416. [Q99685-1]
ENST00000434178; ENSP00000402798; ENSG00000074416. [Q99685-1]
ENST00000453507; ENSP00000404146; ENSG00000074416. [Q99685-2]
GeneIDi11343.
KEGGihsa:11343.
UCSCiuc003ejw.4. human. [Q99685-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67963 mRNA. Translation: AAB39616.1. Different initiation.
AJ270950 mRNA. Translation: CAC43316.1.
AK091314 mRNA. Translation: BAG52334.1.
AK315529 mRNA. Translation: BAG37910.1. Different initiation.
AK304844 mRNA. Translation: BAH14267.1.
CR456835 mRNA. Translation: CAG33116.1. Different initiation.
AC023593 Genomic DNA. No translation available.
AC117480 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79330.1. Different initiation.
CH471052 Genomic DNA. Translation: EAW79331.1. Different initiation.
BC000551 mRNA. Translation: AAH00551.1. Different initiation.
BC006230 mRNA. Translation: AAH06230.1. Different initiation.
BX640777 mRNA. Translation: CAE45873.1.
CCDSiCCDS43148.1. [Q99685-1]
CCDS58852.1. [Q99685-2]
RefSeqiNP_001003794.1. NM_001003794.2. [Q99685-1]
NP_001243514.1. NM_001256585.1. [Q99685-2]
NP_009214.1. NM_007283.6.
UniGeneiHs.277035.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HJUX-ray2.20A/B2-303[»]
3JW8X-ray2.10A/B1-303[»]
3JWEX-ray2.70A/B1-303[»]
3PE6X-ray1.35A1-303[»]
4UUQX-ray2.36A/B1-303[»]
ProteinModelPortaliQ99685.
SMRiQ99685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116471. 4 interactors.
IntActiQ99685. 3 interactors.
MINTiMINT-1414843.
STRINGi9606.ENSP00000265052.

Chemistry databases

BindingDBiQ99685.
ChEMBLiCHEMBL4191.
GuidetoPHARMACOLOGYi1399.
SwissLipidsiSLP:000000315.

Protein family/group databases

ESTHERihuman-MGLL. Monoglyceridelipase_lysophospholip.
MEROPSiS33.979.

PTM databases

iPTMnetiQ99685.
PhosphoSitePlusiQ99685.

Polymorphism and mutation databases

BioMutaiMGLL.
DMDMi47117287.

Proteomic databases

MaxQBiQ99685.
PaxDbiQ99685.
PeptideAtlasiQ99685.
PRIDEiQ99685.

Protocols and materials databases

DNASUi11343.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398104; ENSP00000381176; ENSG00000074416. [Q99685-1]
ENST00000434178; ENSP00000402798; ENSG00000074416. [Q99685-1]
ENST00000453507; ENSP00000404146; ENSG00000074416. [Q99685-2]
GeneIDi11343.
KEGGihsa:11343.
UCSCiuc003ejw.4. human. [Q99685-1]

Organism-specific databases

CTDi11343.
DisGeNETi11343.
GeneCardsiMGLL.
HGNCiHGNC:17038. MGLL.
HPAiHPA011348.
HPA011993.
HPA011994.
MIMi609699. gene.
neXtProtiNX_Q99685.
OpenTargetsiENSG00000074416.
PharmGKBiPA30789.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1455. Eukaryota.
COG2267. LUCA.
GeneTreeiENSGT00390000011364.
HOGENOMiHOG000003227.
HOVERGENiHBG049220.
InParanoidiQ99685.
KOiK01054.
PhylomeDBiQ99685.
TreeFamiTF329184.

Enzyme and pathway databases

UniPathwayiUPA00256.
BioCyciZFISH:HS01140-MONOMER.
BRENDAi3.1.1.23. 2681.
ReactomeiR-HSA-1482883. Acyl chain remodeling of DAG and TAG.
R-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-426048. Arachidonate production from DAG.

Miscellaneous databases

ChiTaRSiMGLL. human.
EvolutionaryTraceiQ99685.
GenomeRNAii11343.
PROiQ99685.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000074416.
CleanExiHS_MGLL.
ExpressionAtlasiQ99685. baseline and differential.
GenevisibleiQ99685. HS.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR022742. Hydrolase_4.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMGLL_HUMAN
AccessioniPrimary (citable) accession number: Q99685
Secondary accession number(s): B3KRC2
, B7Z9D1, Q6IBG9, Q96AA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: November 2, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Short-term inhibition causes analgesia, while long-term inhibition causes tolerance to endocannabinoids acting on brain cannabinoid receptor CNR1, and a reduction in brain cannabinoid receptor CNR1 activity.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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.