DGAT2 (diacylglycerol O-acyltransferase 2) is an integral endoplasmic reticulum membrane enzyme that catalyzes the terminal and only committed step of triacylglycerol (TAG) biosynthesis: transfer of a long-chain acyl group from acyl-CoA to the sn-3 position of 1,2-diacyl-sn-glycerol (DAG), producing triacylglycerol and CoA (EC 2.3.1.20). It is a member of the DGAT2/MOGAT acyltransferase family and shares no sequence homology with the MBOAT-family enzyme DGAT1, which performs the same net reaction. DGAT2 is a multi-pass ER membrane protein whose catalytic region faces the cytosol; it concentrates at ER–lipid-droplet contact sites and is also found on the lipid droplet surface and in the perinuclear region. Predominantly expressed in liver and white adipose tissue, DGAT2 is the quantitatively major TAG-synthesizing enzyme and, in liver, preferentially channels endogenously synthesized fatty acids into triglyceride for storage in lipid droplets; it is a therapeutic target in hepatic steatosis. Beyond its principal DGAT activity it displays several related in vitro acyltransferase activities, including acyl-CoA:retinol O-fatty-acyltransferase (ARAT, EC 2.3.1.76), monoacylglycerol acyltransferase activity, and use of monoalkylglycerol as an acyl acceptor to form ether neutral lipids. DGAT2 forms multimeric complexes of its own subunits and interacts with the fatty-acid transporter SLC27A1.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: ER membrane is where DGAT2 acts, confirmed experimentally by IDA in this gene. Phylogenetic (IBA) support is consistent with the direct evidence. Reason: DGAT2 is an integral multi-pass ER membrane protein and this is its site of catalysis. Core localization, supported directly by PMID:27184406. |
| GO:0004144 diacylglycerol O-acyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: This is the defining molecular function of DGAT2, confirmed by multiple EXP/IDA annotations for this gene and by IBA across the family. Reason: Core molecular function (EC 2.3.1.20). Directly demonstrated for the human protein (PMID:11481335, PMID:27184406). |
| GO:0019432 triglyceride biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: TAG biosynthesis is the core biological process DGAT2 participates in, catalyzing its terminal committed step. Directly supported by IDA. Reason: Core biological process; concordant with IDA (PMID:27184406, PMID:11481335) and the UniProt PATHWAY (triacylglycerol biosynthesis). |
| GO:0046339 diacylglycerol metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: DAG is the acyl-acceptor substrate of DGAT2; the reaction consumes DAG, so participation in DAG metabolism is appropriate. Also has an IDA for this gene. Reason: Metabolic-process parent capturing DAG turnover by the enzyme; supported by IDA (PMID:11481335) and IBA. |
| GO:0003846 2-acylglycerol O-acyltransferase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: MGAT (2-acylglycerol O-acyltransferase) activity is a genuine in vitro side activity of the DGAT2/MOGAT-family fold, Rhea-mapped from reactions DGAT2 can catalyze, but it is not the principal physiological function. Reason: Real but secondary activity; the closely related family member MGAT3 likewise has both DGAT and MGAT activities in vitro (PMID:27184406). Non-core relative to DGAT2's DGAT activity. |
| GO:0004144 diacylglycerol O-acyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic (Rhea/EC 2.3.1.20) assertion of the core DGAT activity, redundant with the experimental annotations but correct. Reason: Correct core molecular function; do not demote a gene's own correct core MF merely because it is a redundant IEA. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic transfer of ER membrane localization, concordant with the experimental IDA for this gene. Reason: Correct core localization; redundant with PMID:27184406 IDA. |
| GO:0005811 lipid droplet | IEA GO_REF:0000120 | ACCEPT | Summary: Lipid droplet localization, concordant with the experimental IDA for this gene; DGAT2 concentrates at the lipid droplet surface / ER-LD contacts. Reason: Correct core localization; redundant with PMID:27184406 IDA. |
| GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Generic acyltransferase parent inferred from InterPro/ARBA family membership. Correct but uninformative given the specific GO:0004144 annotation. Reason: Redundant high-level grouping term; the specific diacylglycerol O-acyltransferase activity term already captures the function. |
| GO:0042572 retinol metabolic process | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Inter-ontology inference from the retinol O-fatty-acyltransferase (ARAT) activity. DGAT2 can esterify retinol in vitro, so participation in retinol metabolism follows, but this is a secondary activity. Reason: Downstream of the ARAT side activity (GO:0050252); genuine but non-core relative to TAG synthesis. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Perinuclear region localization, consistent with UniProt "Cytoplasm, perinuclear region (PubMed:27184406)". Reflects perinuclear ER. Reason: Consistent with observed perinuclear ER distribution but peripheral to the core ER-membrane localization. |
| GO:0050252 retinol O-fatty-acyltransferase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: ARAT activity (EC 2.3.1.76), electronic assertion redundant with the EXP annotation. A real secondary activity of DGAT-family enzymes. Reason: Genuine side activity but non-core; DGAT1 is the major ARAT in the relevant tissues (PMID:16214399). |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Colocalization with mitochondrion, transferred electronically from the mouse ortholog. DGAT2 has been reported at ER-mitochondria contact/ mitochondria-associated membranes; the colocalizes_with qualifier is weak. Reason: Weak colocalization claim from an ortholog; peripheral and not the site of catalysis, but retained as it derives from experimental mouse evidence. ORGANELLES check (2026-10-25): the action holds, and colocalizes_with is the right qualifier. The mouse source Q9DCV3 carries one IDA (BHF-UCL) from PMID:19049983, now cached with full text. That study shows murine DGAT2 co-localizing with mitochondria by immunofluorescence and enriched in Percoll-purified MAM, an ER subdomain, together with calnexin; the authors favour a model in which MAM-resident DGAT2 associates peripherally with mitochondria through an N-terminal targeting signal, and leave open whether it is a true mitochondrial protein. The mitochondrion claim is therefore a contact-site association, not residence, which is what colocalizes_with says. Non-core, since catalysis is on the ER membrane and lipid droplets. The MAM location is added as a separate NEW row (rule 4). Supporting Evidence: PMID:19049983 Based on our data, we favor a model in which DGAT2 is enriched in MAM, and DGAT2 in this compartment associates with mitochondria as a peripheral protein via its N terminus. PMID:19049983 Our findings raise the question of whether DGAT2 is a true mitochondrial enzyme or is present in a compartment, such MAM, which is associated with mitochondria. |
| GO:0044233 mitochondria-associated endoplasmic reticulum membrane contact site | IC PMID:19049983 The endoplasmic reticulum enzyme DGAT2 is found in mitochond... | NEW | Summary: Proposed location for the DGAT2 pool that associates with mitochondria. Rodent DGAT2 is enriched in purified mitochondria-associated membranes, and the membrane-embedded ER enzyme reaches mitochondria through that contact site rather than by import. Reason: Lines of evidence agree (ORGANELLES rule 4, 2026-10-25). (1) Direct fractionation in a cached full-text paper: Percoll-purified MAM from McArdle RH7777 cells stably expressing DGAT2 contained DGAT2 enriched several-fold over microsomes, with calnexin as the ER marker, and DGAT activity in livers of DGAT1-knockout mice (where it reflects DGAT2) was about two-fold higher in the mitochondria-plus-MAM fraction than in microsomes (PMID:19049983). (2) Topology: UniProt records human DGAT2 as a multi-pass ER-membrane protein with two TM helices and both termini cytoplasmic, so a mitochondrial pool can only be an ER membrane apposed to mitochondria, not an imported mitochondrial protein; the N-terminal targeting signal the authors map (residues 61-66) lies on the cytoplasmic side, just before the first TM helix. (3) Function: triacylglycerol synthesis is a MAM-enriched lipid-synthetic activity. IC rather than ISS or IDA because the assays are rodent and no human MAM fraction has been examined. The MAM term overlaps both ER membrane and mitochondrial membrane, so it records the contact site without asserting residence in the mitochondrion. The pool is non-core; core_functions locations are left at the ER membrane and lipid droplet. Supporting Evidence: PMID:19049983 Immunoblotting showed that DGAT2 and calnexin were present in the microsomal fraction and were also enriched several-fold in MAM PMID:19049983 DGAT activity, which should reflect only that of DGAT2, was ∼2-fold higher in the mitochondria plus MAM fraction than in the microsomal fraction PMID:19049983 Biochemical fractionation revealed that DGAT2 is present in mitochondria-associated membranes, specialized domains of the ER that are highly enriched in lipid synthetic enzymes and interact tightly with mitochondria. file:human/DGAT2/DGAT2-uniprot.txt Endoplasmic reticulum membrane file:human/DGAT2/DGAT2-uniprot.txt TRANSMEM 70..88 |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | ACCEPT | Summary: ER localization transferred from the mouse ortholog; concordant with the human IDA (PMID:14521909) placing DGAT2 on the ER. Reason: Correct core localization; redundant with human IDA. |
| GO:0006651 diacylglycerol biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DGAT2 consumes DAG to make TAG rather than synthesizing DAG in its primary reaction, but its in vitro MGAT activity generates DAG from monoacylglycerol, so participation in DAG biosynthesis is defensible as a minor activity. Reason: Supported only via the secondary MGAT activity; not a core function. |
| GO:0007584 response to nutrient | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Broad physiological process transferred from the rat ortholog. DGAT2 expression/activity responds to nutritional state, but this is an indirect, high-level role. Reason: Organism-level physiological association from an ortholog; not a direct molecular function of the enzyme. |
| GO:0010867 positive regulation of triglyceride biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DGAT2 executes the committed step of TAG biosynthesis rather than regulating the pathway; the "positive regulation" framing conflates catalysis with regulation. Reason: Awkward regulatory framing of what is a catalytic role; the direct term is triglyceride biosynthetic process (GO:0019432), already annotated as core. |
| GO:0019915 lipid storage | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DGAT2 makes the TAG that is stored in lipid droplets, so it contributes to lipid storage. Transferred from the mouse ortholog. Reason: Physiological consequence of TAG synthesis; peripheral to the molecular core. |
| GO:0034383 low-density lipoprotein particle clearance | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Indirect systemic lipoprotein effect transferred from the mouse ortholog; a downstream consequence of altered hepatic TAG synthesis rather than a direct DGAT2 function. Reason: Distal physiological association; not a direct molecular/cellular function of the enzyme. |
| GO:0035336 long-chain fatty-acyl-CoA metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: DGAT2 uses long-chain fatty acyl-CoA as its acyl donor, consuming it in the acyltransfer reaction. Also directly annotated by IDA for this gene. Reason: Directly reflects the acyl-CoA-dependent chemistry of the enzyme; concordant with IDA (PMID:11481335). |
| GO:0035356 intracellular triglyceride homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DGAT2 is a major determinant of intracellular TAG levels; transferred from the mouse ortholog. Reason: Homeostatic/physiological framing of TAG synthesis; peripheral to the molecular core (which is captured by GO:0019432). |
| GO:0042632 cholesterol homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cholesterol homeostasis is an indirect systemic effect transferred from the mouse ortholog, not a direct function of a TAG-synthesizing enzyme. Reason: Distal physiological association; DGAT2 does not act on cholesterol. |
| GO:0042803 protein homodimerization activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DGAT2 forms multimeric complexes of several DGAT2 subunits (UniProt SUBUNIT, By similarity); homodimerization/oligomerization is plausible. Transferred from the mouse ortholog. Reason: Consistent with UniProt "Forms multimeric complexes consisting of several DGAT2 subunits"; a structural property, not the core catalytic function. |
| GO:0045722 positive regulation of gluconeogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Effect on gluconeogenesis is an indirect metabolic consequence transferred from the rat ortholog, not a direct DGAT2 function. Reason: Distal physiological association; not a direct molecular function. |
| GO:0046322 negative regulation of fatty acid oxidation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: By channeling fatty acids into TAG, DGAT2 can reduce their availability for oxidation; this is an indirect effect transferred from the rat ortholog. Reason: Indirect metabolic consequence of TAG synthesis; peripheral to the molecular core. |
| GO:0046339 diacylglycerol metabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assertion of DAG metabolism, redundant with the IDA and IBA annotations to the same term. DAG is the acyl-acceptor substrate. Reason: Correct; DAG is directly metabolized (consumed) by the enzyme. Redundant with IDA (PMID:11481335). |
| GO:0050746 regulation of lipoprotein metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Systemic lipoprotein-metabolism effect transferred from the rat ortholog; an indirect consequence of hepatic TAG synthesis. Reason: Distal physiological association; not a direct molecular function. |
| GO:0055089 fatty acid homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: By esterifying fatty acids into TAG, DGAT2 contributes to fatty acid homeostasis; transferred from the mouse ortholog. Reason: Physiological consequence of the acyltransfer reaction; peripheral to the molecular core. |
| GO:0060613 fat pad development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Adipose/fat-pad development role transferred from the mouse ortholog, reflecting DGAT2's importance for TAG storage in adipose tissue. Reason: Developmental/physiological role of an ortholog; not the molecular core function of the enzyme. |
| GO:0071400 cellular response to oleic acid | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cellular response to oleic acid (a preferred DGAT2 substrate) transferred from the mouse ortholog; oleate loading drives DGAT2-dependent TAG synthesis and lipid droplet growth. Reason: Consistent with DGAT2's preference for unsaturated acyl-CoA, but a physiological response rather than the core molecular function. |
| GO:0090181 regulation of cholesterol metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Indirect effect on cholesterol metabolism transferred from the rat ortholog; not a direct DGAT2 function. Reason: Distal physiological association; DGAT2 does not act on cholesterol. |
| GO:0097006 regulation of plasma lipoprotein particle levels | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Systemic effect on plasma lipoprotein levels transferred from the mouse ortholog; an indirect consequence of hepatic TAG/VLDL production. Reason: Distal physiological association; not a direct molecular function. |
| GO:0019432 triglyceride biosynthetic process | TAS Reactome:R-HSA-75109 | ACCEPT | Summary: Reactome-asserted participation in triglyceride biosynthesis, the core process for DGAT2. Concordant with the IDA and IBA annotations. Reason: Core biological process; authoritative Reactome pathway assertion. |
| GO:0019432 triglyceride biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway-based electronic assertion of TAG biosynthesis; redundant with the experimental and Reactome annotations for the same term. Reason: Correct core biological process (UPA00282, triacylglycerol biosynthesis). |
| GO:0004144 diacylglycerol O-acyltransferase activity | EXP PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | ACCEPT | Summary: The original cloning paper showed DGAT2 expression stimulated triglyceride synthesis, dependent on fatty acyl-CoA and diacylglycerol, establishing DGAT activity for the human enzyme. Reason: Primary experimental evidence for the core molecular function. Supporting Evidence: PMID:11481335 DGAT2 activity was dependent on the presence of fatty acyl-CoA and diacylglycerol, indicating that this protein is a DGAT. |
| GO:0004144 diacylglycerol O-acyltransferase activity | EXP PMID:16214399 Acyl coenzyme A dependent retinol esterification by acyl coe... | ACCEPT | Summary: This study of DGAT/MGAT enzymes assayed their acyltransferase activities; the DGAT annotation reflects DGAT-family diacylglycerol acyltransferase activity examined in the full paper. Reason: Experimental annotation for the core molecular function; consistent with the enzyme's established DGAT activity. Supporting Evidence: PMID:16214399 enzymes involved in the synthesis of triacylglycerol, namely acyl coenzyme A:diacylglycerol acyltransferase (DGAT) |
| GO:0050252 retinol O-fatty-acyltransferase activity | EXP PMID:16214399 Acyl coenzyme A dependent retinol esterification by acyl coe... | KEEP AS NON CORE | Summary: DGAT/MGAT enzymes were shown to carry out the acyl-CoA:retinol acyltransferase (ARAT) reaction; this establishes the ARAT side activity (EC 2.3.1.76) for DGAT-family enzymes including DGAT2. Reason: Genuine secondary activity confirmed experimentally; non-core relative to DGAT activity (DGAT1 is the major ARAT in the tissues studied). Supporting Evidence: PMID:16214399 are capable of carrying out the acyl coenzyme A:retinol acyltransferase (ARAT) reaction |
| GO:0006640 monoacylglycerol biosynthetic process | IDA PMID:28420705 Synthesis of neutral ether lipid monoalkyl-diacylglycerol by... | KEEP AS NON CORE | Summary: In vitro, DGAT2 uses 1-monoalkylglycerol as an acyl acceptor to form monoalkyl-monoacylglycerol, but DGAT2 is highly selective against this substrate (~35-fold preference for 1-monooleoylglycerol) and is a minor contributor to ether-lipid/MAMAG synthesis. Reason: Real but minor in vitro side activity; not a core physiological function of DGAT2. Supporting Evidence: PMID:28420705 DGAT1, DGAT2, MGAT2, MGAT3, AWAT2/MFAT, and DC3 carried out both acylation steps resulting in synthesis of the final product, MADAG. |
| GO:0006651 diacylglycerol biosynthetic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from the mouse ortholog. DGAT2 consumes DAG in its primary reaction; DAG biosynthesis is supported only via its secondary MGAT activity (acylation of monoacylglycerol to DAG). Reason: Attributable to the secondary MGAT activity, not the core DGAT reaction. |
| GO:0005515 protein binding | IPI PMID:30970241 The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Co... | MARK AS OVER ANNOTATED | Summary: IPI capturing the interaction between DGAT2 and SLC27A1/FATP1 (WITH UniProtKB:Q6PCB7), reported in the context of ER-lipid-droplet contact formation. The bare "protein binding" term is uninformative about function. Reason: Bare protein binding conveys no specific function; the underlying SLC27A1 interaction is captured in the notes/core functions. Not removed (IPI). Supporting Evidence: PMID:30970241 The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact Formation. |
| GO:0004144 diacylglycerol O-acyltransferase activity | IDA PMID:27184406 Biochemical characterization of human acyl coenzyme A: 2-mon... | ACCEPT | Summary: Direct assay confirmed DGAT activity for human DGAT2 alongside characterization of the related MGAT3 enzyme. Reason: Direct experimental evidence for the core molecular function. Supporting Evidence: PMID:27184406 MGAT3 is more closely related to DGAT2 than to MGAT1 and MGAT2. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:27184406 Biochemical characterization of human acyl coenzyme A: 2-mon... | ACCEPT | Summary: Direct evidence localizing DGAT2 to the ER membrane; DGAT2 also concentrates around the lipid droplet surface (contrasted with MGAT3). Reason: Core localization, directly observed. Supporting Evidence: PMID:27184406 unlike DGAT2, does not become concentrated around the lipid droplet surface |
| GO:0005811 lipid droplet | IDA PMID:27184406 Biochemical characterization of human acyl coenzyme A: 2-mon... | ACCEPT | Summary: DGAT2 becomes concentrated around the lipid droplet surface, directly observed; consistent with its role in local TAG synthesis for lipid droplet growth. Reason: Core localization at the ER-lipid-droplet interface, directly observed. Supporting Evidence: PMID:27184406 unlike DGAT2, does not become concentrated around the lipid droplet surface |
| GO:0019432 triglyceride biosynthetic process | IDA PMID:27184406 Biochemical characterization of human acyl coenzyme A: 2-mon... | ACCEPT | Summary: Direct evidence that DGAT2 is required for synthesis and storage of intracellular triglycerides; DGAT2 expression stimulated lipid droplet growth. Reason: Core biological process, directly demonstrated. Supporting Evidence: PMID:27184406 MGAT3 stimulated lipid droplet growth, but unlike DGAT2, does not become concentrated around the lipid droplet surface |
| GO:1990578 perinuclear endoplasmic reticulum membrane | IDA PMID:27184406 Biochemical characterization of human acyl coenzyme A: 2-mon... | ACCEPT | Summary: DGAT2 localizes to the perinuclear ER membrane / perinuclear cytoplasmic region, directly observed; consistent with UniProt "Cytoplasm, perinuclear region (PubMed:27184406)". Reason: Specific ER-membrane sub-location, directly observed; consistent with the core ER-membrane localization. |
| GO:0005739 mitochondrion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS colocalization with mitochondrion from the mouse ortholog; DGAT2 has been reported at ER-mitochondria contacts / mitochondria-associated membranes. The colocalizes_with qualifier is a weak spatial claim. Reason: Weak colocalization from an ortholog; not the primary site of catalysis. ORGANELLES check (2026-10-25): the action holds. Same source as the Ensembl IEA row, mouse Q9DCV3 IDA from PMID:19049983, which places DGAT2 in MAM associated peripherally with mitochondria; colocalizes_with fits. The MAM location is recorded as a NEW row beside the IEA row. Supporting Evidence: PMID:19049983 Based on our data, we favor a model in which DGAT2 is enriched in MAM, and DGAT2 in this compartment associates with mitochondria as a peripheral protein via its N terminus. PMID:19049983 Our findings raise the question of whether DGAT2 is a true mitochondrial enzyme or is present in a compartment, such MAM, which is associated with mitochondria. |
| GO:0005789 endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: ISS transfer of ER membrane localization from the mouse ortholog; concordant with the human IDA. Reason: Correct core localization; redundant with PMID:27184406 IDA. |
| GO:0005811 lipid droplet | ISS GO_REF:0000024 | ACCEPT | Summary: ISS colocalization with lipid droplet from the mouse ortholog; concordant with the human IDA localizing DGAT2 to the lipid droplet surface. Reason: Correct core localization; redundant with PMID:27184406 IDA. |
| GO:0019915 lipid storage | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Lipid storage role transferred by ISS from the mouse ortholog; DGAT2 makes the TAG stored in lipid droplets. Reason: Physiological consequence of TAG synthesis; peripheral to the molecular core. |
| GO:0042632 cholesterol homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cholesterol homeostasis by ISS from the mouse ortholog; an indirect systemic effect, not a direct DGAT2 function. Reason: Distal physiological association; DGAT2 does not act on cholesterol. |
| GO:0048471 perinuclear region of cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Perinuclear cytoplasm localization by ISS from the mouse ortholog; consistent with UniProt "Cytoplasm, perinuclear region" and the perinuclear ER membrane IDA. Reason: Consistent with observed perinuclear ER distribution; peripheral to the core ER-membrane localization. |
| GO:0055089 fatty acid homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Fatty acid homeostasis by ISS from the mouse ortholog; DGAT2 esterifies fatty acids into TAG. Reason: Physiological consequence of the acyltransfer reaction; peripheral to the core. |
| GO:0060613 fat pad development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Fat pad development by ISS from the mouse ortholog; reflects DGAT2's role in adipose TAG storage. Reason: Developmental/physiological role of an ortholog; not the molecular core. |
| GO:0071400 cellular response to oleic acid | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cellular response to oleic acid by ISS from the mouse ortholog; oleate is a preferred DGAT2 substrate and drives DGAT2-dependent TAG synthesis. Reason: Physiological response consistent with the enzyme's substrate preference; not the core molecular function. |
| GO:0097006 regulation of plasma lipoprotein particle levels | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Regulation of plasma lipoprotein levels by ISS from the mouse ortholog; an indirect systemic consequence of hepatic TAG/VLDL production. Reason: Distal physiological association; not a direct molecular function. |
| GO:0034383 low-density lipoprotein particle clearance | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: LDL particle clearance by ISS from the mouse ortholog; a downstream systemic effect of altered hepatic TAG metabolism. Reason: Distal physiological association; not a direct molecular/cellular function. |
| GO:0005783 endoplasmic reticulum | IDA PMID:14521909 A novel diacylglycerol acyltransferase (DGAT2) is decreased ... | ACCEPT | Summary: DGAT2 protein was directly detected on the endoplasmic reticulum. Reason: Core localization, directly observed in human cells. Supporting Evidence: PMID:14521909 DGAT2 protein was detected on endoplasmic reticulum. |
| GO:0005789 endoplasmic reticulum membrane | IC PMID:14521909 A novel diacylglycerol acyltransferase (DGAT2) is decreased ... | ACCEPT | Summary: Curator inference (IC) of ER membrane localization from the ER detection, appropriate for a multi-pass integral membrane protein. Reason: Correct core localization; DGAT2 is a multi-pass ER membrane protein. Supporting Evidence: PMID:14521909 DGAT2 protein was detected on endoplasmic reticulum. |
| GO:0016020 membrane | IDA PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | KEEP AS NON CORE | Summary: DGAT2 activity was assayed in cellular membranes; localization to membrane is correct but this is a high-level parent of its specific ER membrane localization. Reason: Correct but generic; the specific ER membrane term (GO:0005789) already captures the localization. Supporting Evidence: PMID:11481335 stimulated triglyceride synthesis 6-fold in assays with cellular membranes |
| GO:0035336 long-chain fatty-acyl-CoA metabolic process | IDA PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | ACCEPT | Summary: DGAT2 activity requires fatty acyl-CoA as the acyl donor, which it consumes in the acyltransfer reaction; directly demonstrated in the cloning paper. Reason: Directly reflects the acyl-CoA-dependent chemistry of the core reaction. Supporting Evidence: PMID:11481335 DGAT2 activity was dependent on the presence of fatty acyl-CoA and diacylglycerol |
| GO:0035356 intracellular triglyceride homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Intracellular TAG homeostasis by ISS from the mouse ortholog; DGAT2 is a major determinant of cellular TAG levels. Reason: Homeostatic framing of TAG synthesis; peripheral to the molecular core (captured by GO:0019432). |
| GO:0046339 diacylglycerol metabolic process | IDA PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | ACCEPT | Summary: DGAT2 activity is dependent on diacylglycerol, its acyl-acceptor substrate, which it consumes; directly demonstrated. Reason: DAG is directly metabolized (consumed) by the enzyme; core-adjacent. Supporting Evidence: PMID:11481335 DGAT2 activity was dependent on the presence of fatty acyl-CoA and diacylglycerol |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-1482889 | ACCEPT | Summary: Reactome-asserted ER membrane localization; concordant with the experimental IDA/IC. Reason: Correct core localization; authoritative Reactome assertion. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-549192 | ACCEPT | Summary: Reactome-asserted ER membrane localization from the DGAT2 TAG-synthesis reaction; concordant with experimental evidence. Reason: Correct core localization; authoritative Reactome assertion. |
| GO:0004144 diacylglycerol O-acyltransferase activity | IDA PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | ACCEPT | Summary: Direct assay of the cloned human DGAT2 demonstrated diacylglycerol O-acyltransferase activity dependent on acyl-CoA and DAG. Reason: Primary direct experimental evidence for the core molecular function. Supporting Evidence: PMID:11481335 DGAT2 activity was dependent on the presence of fatty acyl-CoA and diacylglycerol, indicating that this protein is a DGAT. |
| GO:0019432 triglyceride biosynthetic process | IDA PMID:11481335 Cloning of DGAT2, a second mammalian diacylglycerol acyltran... | ACCEPT | Summary: DGAT2 expression stimulated triglyceride synthesis 6-fold, directly demonstrating participation in TAG biosynthesis. Reason: Core biological process, directly demonstrated. Supporting Evidence: PMID:11481335 The expression of DGAT2 in insect cells stimulated triglyceride synthesis 6-fold in assays with cellular membranes |
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