Q99685 · MGLL_HUMAN
- ProteinMonoglyceride lipase
- GeneMGLL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids303 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Converts monoacylglycerides to free fatty acids and glycerol (PubMed:19029917, PubMed:20079333, PubMed:21049984, PubMed:22969151, PubMed:24368842).
Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (PubMed:19029917, PubMed:20079333, PubMed:21049984, PubMed:22969151, PubMed:24368842).
Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333).
Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain (PubMed:19029917, PubMed:20079333, PubMed:21049984, PubMed:22969151, PubMed:24368842).
Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (PubMed:20079333).
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.
Catalytic activity
- a 1-acylglycerol + H2O = a fatty acid + glycerol + H+This reaction proceeds in the forward direction.
- a 2-acylglycerol + H2O = a fatty acid + glycerol + H+This reaction proceeds in the forward direction.
- 1-octanoylglycerol + H2O = glycerol + H+ + octanoateThis reaction proceeds in the forward direction.
- 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-decanoylglycerol + H2O = decanoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-tetradecanoylglycerol + H2O = glycerol + H+ + tetradecanoateThis reaction proceeds in the forward direction.
- 2-hexadecanoylglycerol + H2O = glycerol + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H+This reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H+This reaction proceeds in the forward direction.
- 2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H+This reaction proceeds in the forward direction.
- 1-hexadecanoylglycerol + H2O = glycerol + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-octadecanoylglycerol + H2O = glycerol + H+ + octadecanoateThis reaction proceeds in the forward direction.
- H2O + prostaglandin E2 1-glyceryl ester = glycerol + H+ + prostaglandin E2This reaction proceeds in the forward direction.
- H2O + prostaglandin D2-1-glycerol ester = glycerol + H+ + prostaglandin D2This reaction proceeds in the forward direction.
- 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 + H2O = 15-deoxy-Delta(12,14)-prostaglandin J2 + glycerol + H+This reaction proceeds in the forward direction.
- H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H+ + prostaglandin F2alphaThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
110 μM | 2-arachidonoyglycerol | |||||
15 μM | 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ2-G) |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
120 nmol/min/mg | toward 2-arachidonoyglycerol | ||||
89 nmol/min/mg | toward 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ2-G) |
Pathway
Glycerolipid metabolism; triacylglycerol degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 122 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 239 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 269 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | acylglycerol lipase activity | |
Molecular Function | lysophospholipase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | acylglycerol catabolic process | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | inflammatory response | |
Biological Process | lipid metabolic process | |
Biological Process | monoacylglycerol catabolic process | |
Biological Process | regulation of endocannabinoid signaling pathway | |
Biological Process | regulation of inflammatory response | |
Biological Process | regulation of sensory perception of pain | |
Biological Process | regulation of signal transduction | |
Biological Process | triglyceride catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameMonoglyceride lipase
- EC number
- Short namesMGL
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99685
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 194 | Does not affect ability to hydrolyze 1- or 2-monoacylglycerol. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 201 | Does not affect ability to hydrolyze 1- or 2-monoacylglycerol. | ||||
Sequence: C → A | ||||||
Mutagenesis | 208 | Does not affect ability to hydrolyze 1- or 2-monoacylglycerol. | ||||
Sequence: C → A | ||||||
Mutagenesis | 242 | Reduced 1-monoacylglycerol lipase activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 350 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000191265 | 1-303 | UniProt | Monoglyceride lipase | |||
Sequence: MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP | |||||||
Modified residue | 10 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 58 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in adipose tissue, lung, liver, kidney, brain and heart.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99685 | ADRB2 P07550 | 2 | EBI-721306, EBI-491169 | |
BINARY | Q99685 | HPCAL1 P37235 | 3 | EBI-721306, EBI-749311 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q99685-1
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.
- Name1
- Length303
- Mass (Da)33,261
- Last updated2004-05-10 v2
- Checksum80E754F126EE64DE
Q99685-2
- Name2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JAM4 | C9JAM4_HUMAN | MGLL | 77 | ||
H7C5K5 | H7C5K5_HUMAN | MGLL | 181 | ||
H7C4E0 | H7C4E0_HUMAN | MGLL | 209 | ||
A0A3B3ITT3 | A0A3B3ITT3_HUMAN | MGLL | 262 | ||
A0A0C4DFN3 | A0A0C4DFN3_HUMAN | MGLL | 313 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U67963 EMBL· GenBank· DDBJ | AAB39616.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AJ270950 EMBL· GenBank· DDBJ | CAC43316.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091314 EMBL· GenBank· DDBJ | BAG52334.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315529 EMBL· GenBank· DDBJ | BAG37910.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK304844 EMBL· GenBank· DDBJ | BAH14267.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456835 EMBL· GenBank· DDBJ | CAG33116.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC023593 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC117480 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471052 EMBL· GenBank· DDBJ | EAW79330.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CH471052 EMBL· GenBank· DDBJ | EAW79331.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
BC000551 EMBL· GenBank· DDBJ | AAH00551.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC006230 EMBL· GenBank· DDBJ | AAH06230.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BX640777 EMBL· GenBank· DDBJ | CAE45873.1 EMBL· GenBank· DDBJ | mRNA |