Q9D850 · DIESL_MOUSE
- ProteinDGAT1/2-independent enzyme synthesizing storage lipids
- GeneTmem68
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids329 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the alternative triglyceride biosynthesis pathway, which mediates formation of triacylglycerol from diacylglycerol and membrane phospholipids (By similarity).
Synthesizes triacylglycerol at the expense of membrane phospholipids, such as phosphatidylcholine (PC) and its ether-linked form (ePC), thereby altering the composition of membranes (By similarity).
The alternative triglyceride biosynthesis pathway is probably required to provide the energy required for rapid growth when fuel sources are limiting (PubMed:37648867).
It maintains mitochondrial function during periods of extracellular lipid starvation (PubMed:37648867).
Can also use acyl-CoA as donor: acts as a acyl-CoA:monoacylglycerol acyltransferase (MGAT), but also shows acyl-CoA:diacylglycerol acyltransferase (DGAT) activity (PubMed:36768334).
Synthesizes triacylglycerol at the expense of membrane phospholipids, such as phosphatidylcholine (PC) and its ether-linked form (ePC), thereby altering the composition of membranes (By similarity).
The alternative triglyceride biosynthesis pathway is probably required to provide the energy required for rapid growth when fuel sources are limiting (PubMed:37648867).
It maintains mitochondrial function during periods of extracellular lipid starvation (PubMed:37648867).
Can also use acyl-CoA as donor: acts as a acyl-CoA:monoacylglycerol acyltransferase (MGAT), but also shows acyl-CoA:diacylglycerol acyltransferase (DGAT) activity (PubMed:36768334).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacylglycerol = a 1-acyl-sn-glycero-3-phosphocholine + a triacylglycerolThis reaction proceeds in the forward direction.
- 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + a 1,2-diacylglycerol = 1-O-alkyl-sn-glycero-3-phosphocholine + a triacylglycerolThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
Activity regulation
Acyltransferase activity is specifically inhibited by TMX1 at the endoplasmic reticulum, restricting accumulation of triacylglycerol.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 129 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | phospholipid:diacylglycerol acyltransferase activity | |
Biological Process | triglyceride biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDGAT1/2-independent enzyme synthesizing storage lipids
- EC number
- Short namesDIESL
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D850
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-50 | Lumenal | ||||
Sequence: MIDNNQTCAAGQDSVPYVTCMIYVLEEWLGVEQLEDYLNFANHLLWVFTP | ||||||
Transmembrane | 51-71 | Helical | ||||
Sequence: LILLILPYFTIFLLYLTIIFL | ||||||
Topological domain | 72-120 | Cytoplasmic | ||||
Sequence: HIYKRKNVLKEAYSHNLWDGARKTVATLWDGHAAVWHGYEVHGMEKIPE | ||||||
Transmembrane | 121-141 | Helical | ||||
Sequence: GAALIIFYHGAIPIDFYYFMA | ||||||
Topological domain | 142-329 | Lumenal | ||||
Sequence: KIFIQKGRTCRVVADHFVFKIPGFSLLLDVFCALHGPREKCVEILRSGHLLAISPGGVREALLSDETYNIIWGNRKGFAQVAIDAKVPIIPMFTQNIREGFRSLGGTRLFKWLYEKFRYPFAPMYGGFPVKLRTFLGDPIPYDPKVTAEELAEKTKNAVQALIDKHQRIPGNIRSALLDRFHKEQKAH |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are indistinguishable from their wild-type counterparts 1 week after birth but grow at a much slower rate between weeks 4 and 4 (PubMed:37648867).
The weight difference observed after 4 weeks is maintained throughout adulthood, suggesting that it is required to support rapid growth at a specific time point after birth, which coincides with a dietary switch from milk to chow (PubMed:37648867).
ells shown decreased triacylglycerol levels at 3.5 weeks of age (PubMed:37648867).
The weight difference observed after 4 weeks is maintained throughout adulthood, suggesting that it is required to support rapid growth at a specific time point after birth, which coincides with a dietary switch from milk to chow (PubMed:37648867).
ells shown decreased triacylglycerol levels at 3.5 weeks of age (PubMed:37648867).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000254593 | 1-329 | DGAT1/2-independent enzyme synthesizing storage lipids | |||
Sequence: MIDNNQTCAAGQDSVPYVTCMIYVLEEWLGVEQLEDYLNFANHLLWVFTPLILLILPYFTIFLLYLTIIFLHIYKRKNVLKEAYSHNLWDGARKTVATLWDGHAAVWHGYEVHGMEKIPEGAALIIFYHGAIPIDFYYFMAKIFIQKGRTCRVVADHFVFKIPGFSLLLDVFCALHGPREKCVEILRSGHLLAISPGGVREALLSDETYNIIWGNRKGFAQVAIDAKVPIIPMFTQNIREGFRSLGGTRLFKWLYEKFRYPFAPMYGGFPVKLRTFLGDPIPYDPKVTAEELAEKTKNAVQALIDKHQRIPGNIRSALLDRFHKEQKAH | ||||||
Glycosylation | 5 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with highest level in the brain, followed by lung and duodenum, and lowest levels in tongue, testis, skin and ileum.
Gene expression databases
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9D850-1
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
- Length329
- Mass (Da)37,810
- Last updated2001-06-01 v1
- Checksum764A967BED835758
Q9D850-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8Y5P2 | A8Y5P2_MOUSE | Tmem68 | 50 |
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK008493 EMBL· GenBank· DDBJ | BAB25698.1 EMBL· GenBank· DDBJ | mRNA | ||
AK048210 EMBL· GenBank· DDBJ | BAC33273.1 EMBL· GenBank· DDBJ | mRNA | ||
AK084881 EMBL· GenBank· DDBJ | BAC39301.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088600 EMBL· GenBank· DDBJ | BAC40445.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147765 EMBL· GenBank· DDBJ | BAE28123.1 EMBL· GenBank· DDBJ | mRNA | ||
AK162563 EMBL· GenBank· DDBJ | BAE36969.1 EMBL· GenBank· DDBJ | mRNA | ||
AK165916 EMBL· GenBank· DDBJ | BAE38459.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166237 EMBL· GenBank· DDBJ | BAE38652.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016240 EMBL· GenBank· DDBJ | AAH16240.1 EMBL· GenBank· DDBJ | mRNA |