Q8NCG7 · DGLB_HUMAN
- ProteinDiacylglycerol lipase-beta
- GeneDAGLB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids672 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids (PubMed:14610053).
Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses. Functions also as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid + H+This reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 2-octadecanoylglycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadecadienoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z,12Z-octadecadienoyl)-glycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-2-O-(5Z,8Z,11Z,14Z-eicosatetraenyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-O-(5Z,8Z,11Z,14Z)-eicosatetraenylglycerol + H+This reaction proceeds in the forward direction.
- 1,2,3-tri-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H+This reaction proceeds in the forward direction.
- 1,2,3-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + 1,2-di-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H+
Cofactor
Activity regulation
Inhibited by p-hydroxy-mercuri-benzoate and HgCl2, but not by PMSF. Also inhibited by RHC80267, a drug that blocks 2-AG formation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
74.1 μM | diacylglycerol |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3.45 nmol/min/mg |
pH Dependence
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 443 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 495 | Charge relay system | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lysosomal membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | acylglycerol lipase activity | |
Molecular Function | lipase activity | |
Molecular Function | metal ion binding | |
Molecular Function | triglyceride lipase activity | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | cannabinoid biosynthetic process | |
Biological Process | diacylglycerol catabolic process | |
Biological Process | monoacylglycerol biosynthetic process | |
Biological Process | neuroblast proliferation | |
Biological Process | neurogenesis | |
Biological Process | positive regulation of triglyceride catabolic process | |
Biological Process | prostaglandin biosynthetic process | |
Biological Process | regulation of inflammatory response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameDiacylglycerol lipase-beta
- EC number
- Short namesDAGL-beta ; DGL-beta
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NCG7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-17 | Cytoplasmic | ||||
Sequence: MPGMVLFGRRWAIASDD | ||||||
Transmembrane | 18-38 | Helical | ||||
Sequence: LVFPGFFELVVRVLWWIGILT | ||||||
Topological domain | 39-58 | Extracellular | ||||
Sequence: LYLMHRGKLDCAGGALLSSY | ||||||
Transmembrane | 59-79 | Helical | ||||
Sequence: LIVLMILLAVVICTVSAIMCV | ||||||
Topological domain | 80-102 | Cytoplasmic | ||||
Sequence: SMRGTICNPGPRKSMSKLLYIRL | ||||||
Transmembrane | 103-123 | Helical | ||||
Sequence: ALFFPEMVWASLGAAWVADGV | ||||||
Topological domain | 124-132 | Extracellular | ||||
Sequence: QCDRTVVNG | ||||||
Transmembrane | 133-153 | Helical | ||||
Sequence: IIATVVVSWIIIAATVVSIII | ||||||
Topological domain | 154-672 | Cytoplasmic | ||||
Sequence: VFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 443 | Loss of activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 495 | Loss of activity. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_027275 | 664 | in dbSNP:rs2303361 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 947 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000248350 | 1-672 | UniProt | Diacylglycerol lipase-beta | |||
Sequence: MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 570 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 570 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 574 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 579 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 579 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 583 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 584 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NCG7 | CLP1 Q92989 | 3 | EBI-721948, EBI-2559831 | |
BINARY | Q8NCG7 | NOTCH2NLC P0DPK4 | 3 | EBI-721948, EBI-22310682 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8NCG7-1
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
- Length672
- Mass (Da)73,732
- Last updated2006-09-05 v2
- ChecksumAA953D737E0EFF44
Q8NCG7-2
- Name2
- Differences from canonical
- 1-281: Missing
Q8NCG7-3
- Name3
Q8NCG7-4
- Name4
- Differences from canonical
- 140-310: SWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDC → RTQIWCPATLRRASPCFISNRTISGTTKSLPRWSAMPQGAPS
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020245 | 1-281 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043309 | 140-310 | in isoform 4 | |||
Sequence: SWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDC → RTQIWCPATLRRASPCFISNRTISGTTKSLPRWSAMPQGAPS | ||||||
Alternative sequence | VSP_020246 | 249-267 | in isoform 3 | |||
Sequence: IRNNQEPAQVVCHAPGSSQ → TRATGNCPRNDGLTLLSLN | ||||||
Alternative sequence | VSP_020247 | 268-672 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 270 | in Ref. 3; BAC11175 | ||||
Sequence: D → Y | ||||||
Sequence conflict | 456 | in Ref. 2; BAC04258 | ||||
Sequence: L → V | ||||||
Sequence conflict | 545 | in Ref. 7; AAH27603 | ||||
Sequence: T → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF450090 EMBL· GenBank· DDBJ | AAL47020.1 EMBL· GenBank· DDBJ | mRNA | ||
AK093958 EMBL· GenBank· DDBJ | BAC04258.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074210 EMBL· GenBank· DDBJ | BAB85017.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK122748 EMBL· GenBank· DDBJ | BAG53702.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298955 EMBL· GenBank· DDBJ | BAG61052.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074584 EMBL· GenBank· DDBJ | BAC11073.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074744 EMBL· GenBank· DDBJ | BAC11175.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075128 EMBL· GenBank· DDBJ | BAC11420.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009412 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC072052 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH878731 EMBL· GenBank· DDBJ | EAW55033.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH878731 EMBL· GenBank· DDBJ | EAW55035.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236963 EMBL· GenBank· DDBJ | EAL23721.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC027603 EMBL· GenBank· DDBJ | AAH27603.1 EMBL· GenBank· DDBJ | mRNA |