UniProtKB - Q9ERM3 (DGAT1_RAT)
Diacylglycerol O-acyltransferase 1
Dgat1
Functioni
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats. In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (By similarity).
Also present in female mammary glands, where it produces fat in the milk (By similarity).
May be involved in VLDL (very low density lipoprotein) assembly (By similarity).
In contrast to DGAT2 it is not essential for survival (By similarity).
Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (By similarity).
Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (By similarity).
Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
By similarityCatalytic activityi
- EC:2.3.1.20By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:2.3.1.76By similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H+ = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-dihexadecanoyl-1,2-hexadecanediol + 2 CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
: glycerolipid metabolism Pathwayi
This protein is involved in the pathway glycerolipid metabolism, which is part of Lipid metabolism.View all proteins of this organism that are known to be involved in the pathway glycerolipid metabolism and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 401 | Acyl-CoABy similarity | 1 | |
Binding sitei | 415 | Acyl-CoABy similarity | 1 | |
Active sitei | 426 | By similarity | 1 | |
Sitei | 427 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 488 | Acyl-CoABy similarity | 1 |
GO - Molecular functioni
- 2-acylglycerol O-acyltransferase activity Source: RGD
- acyltransferase activity Source: RGD
- diacylglycerol binding Source: RGD
- diacylglycerol O-acyltransferase activity Source: RGD
- fatty acid binding Source: RGD
- identical protein binding Source: RGD
- O-acyltransferase activity Source: GO_Central
- retinol O-fatty-acyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- diacylglycerol metabolic process Source: UniProtKB
- fatty acid homeostasis Source: RGD
- glycerolipid metabolic process Source: RGD
- insulin secretion Source: RGD
- ketone body metabolic process Source: RGD
- lipid storage Source: RGD
- long-chain fatty-acyl-CoA metabolic process Source: RGD
- monoacylglycerol biosynthetic process Source: UniProtKB
- positive regulation of fatty acid oxidation Source: RGD
- positive regulation of hepatic stellate cell activation Source: RGD
- positive regulation of triglyceride biosynthetic process Source: RGD
- regulation of eating behavior Source: RGD
- regulation of intestinal lipid absorption Source: RGD
- regulation of vitamin A metabolic process Source: RGD
- response to human chorionic gonadotropin Source: RGD
- triglyceride biosynthetic process Source: RGD
- very-low-density lipoprotein particle assembly Source: RGD
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 2.3.1.20, 5301 |
Reactomei | R-RNO-1482883, Acyl chain remodeling of DAG and TAG R-RNO-6798695, Neutrophil degranulation R-RNO-75109, Triglyceride biosynthesis |
UniPathwayi | UPA00230 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 628673, Dgat1 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: GO_Central
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- integral component of membrane Source: UniProtKB
- intracellular membrane-bounded organelle Source: RGD
- membrane Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 92 | CytoplasmicCuratedAdd BLAST | 92 | |
Transmembranei | 93 – 127 | Helical; Name=1By similarityAdd BLAST | 35 | |
Topological domaini | 128 – 139 | LumenalCuratedAdd BLAST | 12 | |
Transmembranei | 140 – 165 | Helical; Name=2By similarityAdd BLAST | 26 | |
Topological domaini | 166 – 170 | CytoplasmicCurated | 5 | |
Transmembranei | 171 – 193 | Helical; Name=3By similarityAdd BLAST | 23 | |
Topological domaini | 194 – 200 | LumenalCurated | 7 | |
Transmembranei | 201 – 232 | Helical; Name=4By similarityAdd BLAST | 32 | |
Topological domaini | 233 – 284 | CytoplasmicCuratedAdd BLAST | 52 | |
Transmembranei | 285 – 319 | Helical; Name=5By similarityAdd BLAST | 35 | |
Topological domaini | 320 – 326 | LumenalCurated | 7 | |
Transmembranei | 327 – 364 | Helical; Name=6By similarityAdd BLAST | 38 | |
Topological domaini | 365 – 410 | CytoplasmicCuratedAdd BLAST | 46 | |
Transmembranei | 411 – 431 | Helical; Name=7By similarityAdd BLAST | 21 | |
Topological domaini | 432 – 439 | LumenalCurated | 8 | |
Transmembranei | 440 – 458 | Helical; Name=8By similarityAdd BLAST | 19 | |
Topological domaini | 459 – 460 | CytoplasmicCurated | 2 | |
Transmembranei | 461 – 492 | Helical; Name=9By similarityAdd BLAST | 32 | |
Topological domaini | 493 – 498 | LumenalCurated | 6 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207656 | 1 – 498 | Diacylglycerol O-acyltransferase 1Add BLAST | 498 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 20 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | Q9ERM3 |
PeptideAtlasi | Q9ERM3 |
Interactioni
Subunit structurei
Homodimer or homotetramer; both forms have similar enzymatic activities.
By similarityGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000035110 |
Chemistry databases
BindingDBi | Q9ERM3 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 96 | Involved in homomerizationBy similarityAdd BLAST | 96 | |
Regioni | 1 – 66 | DisorderedBy similarityAdd BLAST | 66 | |
Regioni | 128 – 139 | Extracellular loop 1 (EL1)By similarityAdd BLAST | 12 | |
Regioni | 140 – 498 | MBOAT foldBy similarityAdd BLAST | 359 | |
Regioni | 235 – 287 | Intracellular loop 1 (IL1)By similarityAdd BLAST | 53 | |
Regioni | 365 – 410 | Intracellular loop 2 (IL2)By similarityAdd BLAST | 46 | |
Regioni | 385 – 393 | Acyl-CoA bindingBy similarity | 9 | |
Regioni | 391 – 405 | Amphipathic helix (AH)By similarityAdd BLAST | 15 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 371 – 377 | FYXDWWN motifBy similarity | 7 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0380, Eukaryota |
InParanoidi | Q9ERM3 |
OrthoDBi | 1275897at2759 |
PhylomeDBi | Q9ERM3 |
Family and domain databases
InterProi | View protein in InterPro IPR027251, Diacylglycerol_acylTrfase1 IPR004299, MBOAT_fam IPR014371, Oat_ACAT_DAG_ARE |
PANTHERi | PTHR10408, PTHR10408, 1 hit |
Pfami | View protein in Pfam PF03062, MBOAT, 1 hit |
PIRSFi | PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit PIRSF500231, Oat_dag, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
10 20 30 40 50
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVREAAVS PDLGAGGDAP
60 70 80 90 100
APAPAPAHTR DKDRQTSVGD GHWELRCHRL QDSLFSSDSG FSNYRGILNW
110 120 130 140 150
CVVMLILSNA RLSLENLIKY GILVDPIQVV SLFLKDPYSW PAPCLIIASN
160 170 180 190 200
IFIVATFQIE KRLSVGALTE QMGLLLHVVN LATIICFPAA VALLVESITP
210 220 230 240 250
VGSLFALASY SIIFLKLSSY RDVNLWCRQR RVKAKAVSAG KKVSGAAAQN
260 270 280 290 300
TVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT
310 320 330 340 350
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY
360 370 380 390 400
WLFHSCLNAV AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF
410 420 430 440 450
YKPMLRLGSN KWMARTGVFW ASAFFHEYLV SIPLRMFRLW AFTAMMAQVP
460 470 480 490
LAWIVNRFFQ GNYGNAAVWV TLIIGQPVAV LMYVHDYYVL NYDAPVGA
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketQ8BHI5 | Q8BHI5_RAT | O-acyltransferase | Dgat1 DGAT, rCG_59622 | 500 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF296131 mRNA Translation: AAG10084.1 |
RefSeqi | NP_445889.1, NM_053437.1 |
Genome annotation databases
GeneIDi | 84497 |
KEGGi | rno:84497 |
UCSCi | RGD:628673, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF296131 mRNA Translation: AAG10084.1 |
RefSeqi | NP_445889.1, NM_053437.1 |
3D structure databases
SMRi | Q9ERM3 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000035110 |
Chemistry databases
BindingDBi | Q9ERM3 |
ChEMBLi | CHEMBL6129 |
Proteomic databases
PaxDbi | Q9ERM3 |
PeptideAtlasi | Q9ERM3 |
Genome annotation databases
GeneIDi | 84497 |
KEGGi | rno:84497 |
UCSCi | RGD:628673, rat |
Organism-specific databases
CTDi | 8694 |
RGDi | 628673, Dgat1 |
Phylogenomic databases
eggNOGi | KOG0380, Eukaryota |
InParanoidi | Q9ERM3 |
OrthoDBi | 1275897at2759 |
PhylomeDBi | Q9ERM3 |
Enzyme and pathway databases
UniPathwayi | UPA00230 |
BRENDAi | 2.3.1.20, 5301 |
Reactomei | R-RNO-1482883, Acyl chain remodeling of DAG and TAG R-RNO-6798695, Neutrophil degranulation R-RNO-75109, Triglyceride biosynthesis |
Miscellaneous databases
PROi | PR:Q9ERM3 |
Family and domain databases
InterProi | View protein in InterPro IPR027251, Diacylglycerol_acylTrfase1 IPR004299, MBOAT_fam IPR014371, Oat_ACAT_DAG_ARE |
PANTHERi | PTHR10408, PTHR10408, 1 hit |
Pfami | View protein in Pfam PF03062, MBOAT, 1 hit |
PIRSFi | PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit PIRSF500231, Oat_dag, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DGAT1_RAT | |
Accessioni | Q9ERM3Primary (citable) accession number: Q9ERM3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 18, 2001 |
Last sequence update: | March 1, 2001 | |
Last modified: | February 23, 2022 | |
This is version 121 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families