AGPAT2 (LPAAT-beta) is an endoplasmic-reticulum membrane acyltransferase that uses acyl-CoA to acylate lysophosphatidic acid at the sn-2 position, producing phosphatidic acid and CoA. This reaction supplies a central intermediate of glycerophospholipid and triacylglycerol synthesis. AGPAT2 also forms functional complexes with CDP-diacylglycerol synthases CDS1 and CDS2, supporting their stability and lipid flux through the CDP-diacylglycerol branch. In mammalian cell models, its PA-producing activity also supports DRP1-dependent formation of ER tubules. It is important for normal adipose tissue development; biallelic pathogenic variants cause congenital generalized lipodystrophy type 1, with severe loss of adipose tissue and metabolic disease.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT places conserved ER localization at PTN000046633. Reason: The cached PTHR10434 PAINT table assigns the ER IBD to PTN000046633. Human AGPAT2 co-localizes with ER markers in the primary experiments of PMID:21873652. This organelle-level assertion accurately describes its core site of action and retains the resolution chosen by PAINT; the separate ER-membrane annotations provide finer detail. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000046633 SUPPORTS TRANSFER The cached IBD assigns ER localization to this ancestral node; human AGPAT2 experimental evidence is among the descendant support, as expected for PAINT. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT assigns the conserved LPA acyltransferase activity at PTN000046632. Reason: The ancestral activity is retained by human AGPAT2, whose recombinant enzyme converts LPA plus acyl-CoA to PA. The human assays support the same reaction as GO:0003841 and provide no evidence of target-specific loss or substrate divergence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000046632 SUPPORTS TRANSFER The cached PAINT IBD includes GO:0003841 at this node; direct human enzymology corroborates inheritance of this activity. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A file:human/AGPAT2/AGPAT2-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl- |
| GO:0006654 phosphatidic acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT assigns phosphatidic-acid synthesis at PTN000046632. Reason: AGPAT2 performs the LPA-acylation step that produces PA, so it executes the annotated biosynthetic chemistry. The cached PAINT IBD and human biochemical evidence agree on this core process. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000046632 SUPPORTS TRANSFER The PA-synthesis IBD is present at this node and is consistent with experimentally demonstrated human LPA-to-PA conversion. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined electronic mappings identify the experimentally established LPA acyltransferase reaction. Reason: The GOA sources include EC:2.3.1.51, RHEA:19709 and substrate-specific Rhea reactions, InterPro IPR004552, and the mouse ortholog. Their common catalytic assertion matches human AGPAT2 assays; multiple evidence routes can validly support the same core activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: RHEA:19709 SUPPORTS TRANSFER This mapped reaction is LPA plus acyl-CoA to PA plus CoA, the human AGPAT2 reaction measured experimentally. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A file:human/AGPAT2/AGPAT2-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl- |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt subcellular-location mapping places AGPAT2 at the ER membrane. Reason: UniProt SL-0097 maps to the membrane of the ER, consistent with AGPAT2 membrane topology and the human-protein localization and microsomal-activity experiments in PMID:21873652. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0097 SUPPORTS TRANSFER The cached UniProt record explicitly assigns ER membrane localization with experimental support. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0008654 phospholipid biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: The AGPAT family mapping places AGPAT2 in phospholipid biosynthesis. Reason: AGPAT2 directly makes the phospholipid PA and supplies PA to the CDP-DAG phospholipid branch. This is genuine biosynthetic participation, and the broad InterPro process remains an accurate core assertion alongside the specific PA term. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR004552 SUPPORTS TRANSFER The AGP acyltransferase family mapping agrees with human LPA acylation and phospholipid-pathway biochemistry. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A PMID:34824276 AGPAT2 and CDS1/2 can directly interact |
| GO:0016020 membrane | IEA GO_REF:0000002 | ACCEPT | Summary: The InterPro family mapping correctly identifies AGPAT2 as a membrane protein. Reason: The IPR004552 membrane assertion agrees with the human AGPAT2 membrane topology, ER-marker imaging and microsomal activity. It accurately locates the core enzyme at the resolution of this family mapping; the separate ER-membrane annotations provide finer evidence-supported detail. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR004552 SUPPORTS TRANSFER The family membrane mapping agrees with the human protein evidence; no source-scoping failure is established. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad acyltransferase-family term can be refined to LPA O-acyltransferase activity. Reason: IPR002123 identifies an acyltransferase family, while human assays establish the acceptor and product: LPA is acylated by acyl-CoA to PA. GO:0003841 is a verified descendant of the original acyltransferase term and captures that reaction. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR002123 SUPPORTS TRANSFER The phospholipid/glycerol acyltransferase domain supports the broad activity; human enzymology resolves its LPA substrate specificity. Proposed replacements: 1-acylglycerol-3-phosphate O-acyltransferase activity Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara transfers ER localization from mouse Agpat2. Reason: The source protein Q8K3K7 / ENSMUSP00000028286 is the mouse Agpat2 ortholog. Human AGPAT2 ER-marker co-localization independently supports the transferred organelle-level location; no compartment refinement of this source assertion is needed. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q8K3K7 SUPPORTS TRANSFER The mouse donor is identified in GOA; direct experiments with human AGPAT2 support the transferred ER location. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0008544 epidermis development | IEA GO_REF:0000107 | UNDECIDED | Summary: A rat-ortholog transfer links AGPAT2 to epidermis development. Reason: The GOA donor is rat Agpat2 D4AC45 / ENSRNOP00000026408. Primary PMID:16150824 reports fetal-rat epidermal Agpat2 transcript changes during barrier development and measures total AGPAT activity across isoforms. That is relevant developmental evidence, but the exact donor annotation-to-paper link and the extent of conserved human AGPAT2 participation were not resolved. Retain this uncertainty rather than rejecting a developmental role simply because the protein is a lipid enzyme. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:D4AC45 UNRESOLVED Rat Agpat2 is the stated donor. The recovered fetal-epidermis study is relevant, but current annotation/reference linkage and human transfer remain unverified. |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: A rat-ortholog transfer links AGPAT2 to xenobiotic response. Reason: The donor is rat Agpat2 D4AC45 / ENSRNOP00000026408. PMID:19346281 reports a decreased AGPAT2-assigned protein spot after paroxetine exposure in rat hippocampus. GO:0009410 includes changes in gene expression or enzyme production, so it does not require xenobiotic detoxification chemistry. The exact current donor-reference chain and conservation of this context in humans remain unresolved; the human transfer cannot be adjudicated from the rat proteomic association alone. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:D4AC45 UNRESOLVED The rat donor is explicit in GOA. The paroxetine study supplies a plausible context-specific source, but the precise annotation link and human conservation were not established. |
| GO:0006654 phosphatidic acid biosynthetic process | TAS Reactome:R-HSA-1483166 | ACCEPT | Summary: Reactome places AGPAT2 in the PA-synthesis pathway. Reason: The pathway includes the AGPAT-catalyzed conversion of LPA to PA, a step that AGPAT2 performs directly. This supports the core PA-biosynthetic process. Supporting Evidence: Reactome:R-HSA-1483166 LPA is converted to PA by a LPA acyltransferase (AGPAT, also known as LPAAT). |
| GO:0016024 CDP-diacylglycerol biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: AGPAT2 catalyzes the PA-forming step in the CDP-diacylglycerol biosynthetic route. Reason: The UniPathway mapping identifies step 2 of the glycerol-3-phosphate-to-CDP-DAG route. AGPAT2 performs this step itself. Primary PMID:34824276 further demonstrates functional association with CDS1/2 and altered lipid flux through the CDP-DAG branch. CDS enzymes perform the subsequent cytidylyltransferase reaction; direct PA channeling was proposed but not visualized. The existing process annotation is supported by catalytic participation rather than precursor necessity alone. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniPathway:UPA00557 SUPPORTS TRANSFER The cached UniProt pathway places AGPAT2 at the LPA-acylation step; primary CDS-complex and flux experiments independently support this biosynthetic route. Supporting Evidence: file:human/AGPAT2/AGPAT2-uniprot.txt diacylglycerol from sn-glycerol 3-phosphate: step 2/3. PMID:34824276 AGPAT2 and CDS1/2 can directly interact |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | TAS Reactome:R-HSA-75885 | ACCEPT | Summary: Reactome assigns AGPAT2 to the LPA-to-PA acylation reaction. Reason: The reaction consumes LPA and acyl-CoA and produces PA at the ER membrane. AGPAT2 is a catalytic member of this enzyme set, matching its independently measured LPA acyltransferase activity. Supporting Evidence: Reactome:R-HSA-75885 1-acyl-lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) by the enzymes 1-acyl-sn-glycerol-3-phosphate acyltransferases |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:21873652 Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms ... | ACCEPT | Summary: Human AGPAT2 localizes to ER membranes in cellular imaging and fractionation experiments. Reason: The full primary study shows human AGPAT2-EGFP co-localization with sec61-beta in CHO cells and calnexin in primary mouse hepatocytes, together with microsomal AGPAT activity. The assayed protein is human even when the host cells are rodent. These results support its core ER-membrane location. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IMP PMID:15629135 Enzymatic activity of naturally occurring 1-acylglycerol-3-p... | ACCEPT | Summary: Wild-type human AGPAT2 and disease variants were assayed for LPA-to-PA conversion. Reason: PMID:15629135 describes assays of overexpressing CHO-cell lysates using labeled LPA and oleoyl-CoA. Several patient-associated variants have very low residual activity, others retain 15-40%, and A239V retains about 90%. The experiment supports the wild-type catalytic function without treating every tested variant as an enzymatic null. The local source is abstract-only; the established activity is also supported by the full primary human assays in PMID:21873652. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IDA PMID:19075029 The microsomal cardiolipin remodeling enzyme acyl-CoA lysoca... | ACCEPT | Summary: The ALCAT1 study explicitly includes recombinant human AGPAT2 in its acyltransferase assays. Reason: External full text of PMID:19075029 identifies human AGPAT2 cDNA TC116102, HEK293 membrane preparations expressing AGPAT2, radiolabeled acyl-CoA assays with lysophospholipid acceptors, and the AGPAT2 control in Figure 2A. This recovers the gene-specific experiment underlying the IDA. The paper title foregrounds ALCAT1 but does not limit the proteins actually assayed. Supporting Evidence: file:human/AGPAT2/AGPAT2-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl- |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IDA PMID:21873652 Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms ... | ACCEPT | Summary: Human AGPAT2 was biochemically characterized with LPA and multiple acyl-CoA donors. Reason: The full study measures labeled LPA-to-PA conversion by human AGPAT2 expressed in HEK293 cells and determines substrate specificity and kinetics. These are direct assays of GO:0003841. Oleoyl-LPA and oleoyl-CoA were preferred in this assay system; that preference is not a claim of absolute substrate exclusivity. Supporting Evidence: PMID:21873652 The in vitro substrate specificities of AGPAT1 and AGPAT2 are quite similar for lysophosphatidic acid and acyl-CoA. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IDA PMID:9242711 Human lysophosphatidic acid acyltransferase. cDNA cloning, e... | ACCEPT | Summary: The cloned human LPAAT-beta protein has LPA acyltransferase activity in COS7-cell assays. Reason: The cached primary abstract explicitly reports recombinant human protein activity, LPA acceptor preference and arachidonyl-CoA donor preference. Retain the experimentally established core MF, with substrate preferences bounded to this assay; later human assays independently establish the same reaction. Supporting Evidence: PMID:9242711 Recombinant protein produced in COS 7 cells exhibited LPAAT activity with a preference for LPA as the acceptor phosphoglycerol and arachidonyl coenzyme A as the acyl donor. |
| GO:0005783 endoplasmic reticulum | IDA PMID:21873652 Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms ... | ACCEPT | Summary: Human AGPAT2 co-localizes with endoplasmic-reticulum markers. Reason: The full primary human-protein imaging experiments support this original organelle-level IDA. The ER is the site of its core lipid synthesis; the additional ER-membrane annotation from the study provides compatible finer resolution and does not make this assertion non-core. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6799350 | UNDECIDED | Summary: Reactome models AGPAT2 at the plasma membrane after specific-granule exocytosis. Reason: The live event R-HSA-6799350 explicitly includes AGPAT2 in its output plasma-membrane protein set. Its primary reference is the human neutrophil fraction-proteomics study PMID:23650620. The exact AGPAT2-specific supplemental localization evidence and validation of surface delivery were not recovered. ER localization in other cells does not exclude a neutrophil pool, so the earlier incompatibility claim is withdrawn and the location remains unresolved. Propagation Review Root cause: UNRESOLVED Sources checked: Reactome:R-HSA-6806323 UNRESOLVED The output set explicitly contains AGPAT2 at the plasma membrane; primary gene-specific evidence for this exocytosis-associated location remains unverified. |
| GO:0035579 specific granule membrane | TAS Reactome:R-HSA-6799350 | UNDECIDED | Summary: Reactome explicitly includes AGPAT2 among specific-granule membrane proteins. Reason: AGPAT2 is a member of input set R-HSA-6799368 and entity R-HSA-6799353 in the live event. The cited human neutrophil fraction-proteomics study is PMID:23650620, but the AGPAT2-specific supplemental assignment and independent localization confirmation were not recovered. Granule localization is neither verified by the generic event summary nor contradicted by the ER experiments. Propagation Review Root cause: UNRESOLVED Sources checked: Reactome:R-HSA-6799353 UNRESOLVED The human AGPAT2 entity is explicitly assigned to specific-granule membrane; the primary experimental detail behind this assignment is unresolved. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IDA PMID:9212163 Cloning and expression of two human lysophosphatidic acid ac... | ACCEPT | Summary: Human LPAAT-beta expression increases LPA-to-PA activity in cell-free extracts. Reason: The primary abstract describes fluorescent-LPA conversion assays after expression of both human cDNAs in mammalian cells. This direct biochemical result supports the IDA independently of the separate bacterial-complementation experiment. Full article access remains incomplete, but this established activity is corroborated by the recovered later human primary experiments. Supporting Evidence: PMID:9212163 leads to increased LPAAT activity in cell-free extracts using an in vitro assay that measures the conversion of fluorescently labeled LPA to PA. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-75885 | ACCEPT | Summary: The curated LPA-acylation reaction occurs at the ER membrane. Reason: Reactome explicitly locates the AGPAT enzyme reaction at the ER membrane; human AGPAT2 imaging and microsomal assays independently support that location for this enzyme. Supporting Evidence: Reactome:R-HSA-75885 At the endoplasmic reticulum (ER) membrane, 1-acyl-lysophosphatidic acid (LPA) is acylated to phosphatidic acid (PA) PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0001819 positive regulation of cytokine production | IMP PMID:9212163 Cloning and expression of two human lysophosphatidic acid ac... | UNDECIDED | Summary: The cited study reports enhanced cytokine production after LPAAT overexpression and IL-1beta stimulation. Reason: The abstract reports increased TNF-alpha and IL-6 transcription and synthesis in the LPAAT expression experiments. This is relevant positive evidence for GO:0001819, whose definition covers increased cytokine production; lipid enzymology does not preclude that contextual regulatory effect. The full experiment, beta-versus-alpha results and controls were not recovered, so the experimental annotation remains unresolved rather than being overruled from an abstract or the absence of a core immune role. Supporting Evidence: PMID:9212163 This increase in LPAAT activity correlates with enhancement of transcription and synthesis of tumor necrosis factor-alpha and interleukin-6 from cells upon stimulation with interleukin-1beta |
| GO:0001961 positive regulation of cytokine-mediated signaling pathway | IC PMID:9212163 Cloning and expression of two human lysophosphatidic acid ac... | UNDECIDED | Summary: Cytokine-signaling enhancement was inferred from the LPAAT overexpression study. Reason: The reported IL-1beta-dependent cytokine responses are compatible with positive regulation of cytokine-mediated signaling, which does not require AGPAT2 to be a receptor or transcription factor. The full gene-specific signaling assays and the precise basis for the IC were not recovered. The abstract alone does not settle whether increased cytokine production establishes this additional signaling-process claim. Propagation Review Root cause: UNRESOLVED Sources checked: PMID:9212163 UNRESOLVED The reported enhanced cytokine outputs are relevant, but the full experimental basis and specific curator inference were not resolved. Supporting Evidence: PMID:9212163 suggesting LPAAT overexpression may amplify cellular signaling responses from cytokines. |
| GO:0006654 phosphatidic acid biosynthetic process | IGI PMID:9212163 Cloning and expression of two human lysophosphatidic acid ac... | ACCEPT | Summary: Human LPAAT-beta complements a bacterial LPA-acyltransferase defect and restores PA production. Reason: The primary abstract explicitly reports expression of the two human cDNAs in an E. coli plsC mutant, growth complementation and a lipid shift from LPA toward PA. This tests human enzyme function in a heterologous host and supports its direct PA-biosynthetic role. Supporting Evidence: PMID:9212163 complements its growth defect and shifts the equilibrium of cellular lipid content from LPA to PA and other lipids. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | NAS PMID:9461603 Characterization of a human lysophosphatidic acid acyltransf... | ACCEPT | Summary: The NAS assigns the established LPA acyltransferase function to AGPAT2. Reason: The cached abstract of PMID:9461603 focuses on the MHC-encoded alpha paralog and explicitly compares it with the previously described human LPAAT. Full article access is incomplete, so the exact AGPAT2-specific statement has not been located. The NAS activity is independently established by human AGPAT2 assays; retain it without claiming the original paper contains no beta-protein data. Supporting Evidence: PMID:9461603 LPAAT is the enzyme that in lipid metabolism converts lysophosphatidic acid (LPA) into phosphatidic acid (PA). PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A |
| GO:0005783 endoplasmic reticulum | ISS GO_REF:0000024 | ACCEPT | Summary: Curator sequence-similarity transfer places AGPAT2 in the ER. Reason: The mouse Agpat2 ortholog Q8K3K7 is the stated source. Direct experiments with human AGPAT2 independently confirm ER localization, so the transfer is biologically supported at its original organelle-level resolution. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q8K3K7 SUPPORTS TRANSFER The mouse source is consistent with direct human ER-marker co-localization; the source-level location is preserved. Supporting Evidence: PMID:21873652 When co-expressed, both isoforms co-localize to the endoplasmic reticulum. |
| GO:0006644 phospholipid metabolic process | NAS PMID:9461603 Characterization of a human lysophosphatidic acid acyltransf... | ACCEPT | Summary: AGPAT2 participates directly in phospholipid metabolism by making PA. Reason: The NAS uses a paper whose abstract emphasizes the MHC alpha paralog, with the exact beta-related statement unresolved. Human AGPAT2 LPA acylation nevertheless directly establishes phospholipid metabolism. This broad process describes the core chemistry and remains valid beside more specific PA- and CDP-DAG-biosynthetic annotations. Supporting Evidence: PMID:15629135 conversion of [(3)H]LPA to [(3)H]PA in the presence of oleoyl-coenzyme A |
| GO:0006654 phosphatidic acid biosynthetic process | TAS PMID:9212163 Cloning and expression of two human lysophosphatidic acid ac... | ACCEPT | Summary: The original human LPAAT cloning study assigns LPA-to-PA synthesis to LPAAT-beta. Reason: The stated reaction, cell-free activity assays and heterologous complementation all support AGPAT2 performing the PA-forming step. This is direct biosynthetic participation. Supporting Evidence: PMID:9212163 catalyzes the conversion of LPA to PA. |
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