ayr1 (SPAC23D3.11; UniProt Q09851) encodes the NADPH-dependent 1-acyldihydroxyacetone-phosphate reductase (EC 1.1.1.101). It reduces 1-acyl-DHAP to lysophosphatidic acid in the DHAP route of phosphatidic acid synthesis. By similarity to S. cerevisiae Ayr1, it sits on the ER and lipid droplets and may have a minor triacylglycerol lipase activity. It is in the ER in a genome-wide screen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000140 acylglycerone-phosphate reductase (NADP+) activity | IBA GO_REF:0000033 | ACCEPT | Summary: 1-acyl-DHAP reductase activity (PAINT/EC/similarity), converting acyl-DHAP to lysophosphatidic acid. Reason: UniProt curates the 1-acyl-DHAP reductase reaction and the DHAP-route function for ayr1 by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); no S. pombe enzyme assay exists. The SDR family membership (Pfam PF00106 adh_short) and the curated active-site and NADP-binding features are consistent with an NADPH-dependent reductase. Accepted as the core activity on the strength of the ortholog evidence. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a 1-acylglycerone 3-phosphate + NADPH + H(+) = a 1-acyl-sn- file:SCHPO/ayr1/ayr1-uniprot.txt Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). file:SCHPO/ayr1/ayr1-uniprot.txt Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| GO:0000140 acylglycerone-phosphate reductase (NADP+) activity | IEA GO_REF:0000120 | ACCEPT | Summary: 1-acyl-DHAP reductase activity (PAINT/EC/similarity), converting acyl-DHAP to lysophosphatidic acid. Reason: UniProt curates the 1-acyl-DHAP reductase reaction and the DHAP-route function for ayr1 by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); no S. pombe enzyme assay exists. The SDR family membership (Pfam PF00106 adh_short) and the curated active-site and NADP-binding features are consistent with an NADPH-dependent reductase. Accepted as the core activity on the strength of the ortholog evidence. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a 1-acylglycerone 3-phosphate + NADPH + H(+) = a 1-acyl-sn- file:SCHPO/ayr1/ayr1-uniprot.txt Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). file:SCHPO/ayr1/ayr1-uniprot.txt Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| GO:0000140 acylglycerone-phosphate reductase (NADP+) activity | ISS GO_REF:0000024 | ACCEPT | Summary: 1-acyl-DHAP reductase activity (PAINT/EC/similarity), converting acyl-DHAP to lysophosphatidic acid. Reason: UniProt curates the 1-acyl-DHAP reductase reaction and the DHAP-route function for ayr1 by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); no S. pombe enzyme assay exists. The SDR family membership (Pfam PF00106 adh_short) and the curated active-site and NADP-binding features are consistent with an NADPH-dependent reductase. Accepted as the core activity on the strength of the ortholog evidence. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a 1-acylglycerone 3-phosphate + NADPH + H(+) = a 1-acyl-sn- file:SCHPO/ayr1/ayr1-uniprot.txt Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). file:SCHPO/ayr1/ayr1-uniprot.txt Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| GO:0004806 triacylglycerol lipase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: TAG lipase activity by similarity to S. cerevisiae Ayr1, which has a minor lipase activity at lipid droplets; not shown in S. pombe. Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt records the TAG lipase reaction and a secondary TAG lipase activity for ayr1 with ECO:0000250 evidence from P40471; no S. pombe experiment. A genuine secondary activity of the ortholog, peripheral to the 1-acyl-DHAP reductase core, so kept as non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Also has triacylglycerol (TAG) lipase activity. file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + |
| GO:0004806 triacylglycerol lipase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: TAG lipase activity by similarity to S. cerevisiae Ayr1, which has a minor lipase activity at lipid droplets; not shown in S. pombe. Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt records the TAG lipase reaction and a secondary TAG lipase activity for ayr1 with ECO:0000250 evidence from P40471; no S. pombe experiment. A genuine secondary activity of the ortholog, peripheral to the 1-acyl-DHAP reductase core, so kept as non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Also has triacylglycerol (TAG) lipase activity. file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + |
| GO:0004806 triacylglycerol lipase activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: TAG lipase activity by similarity to S. cerevisiae Ayr1, which has a minor lipase activity at lipid droplets; not shown in S. pombe. Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt records the TAG lipase reaction and a secondary TAG lipase activity for ayr1 with ECO:0000250 evidence from P40471; no S. pombe experiment. A genuine secondary activity of the ortholog, peripheral to the 1-acyl-DHAP reductase core, so kept as non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Also has triacylglycerol (TAG) lipase activity. file:SCHPO/ayr1/ayr1-uniprot.txt Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | TOO GENERAL | Summary: Cytoplasm, observed in the S. pombe ORFeome screen; entailed by the ER, Golgi, vacuole and mitochondrial outer membrane locations asserted here. Reason: S. pombe experiment: UniProt records Cytoplasm from the ORFeome localization screen (ECO:0000269, PubMed:16823372), mapped here by GO_REF:0000044. The organelle locations asserted on this gene (endoplasmic reticulum, Golgi apparatus, vacuole, mitochondrial outer membrane) are all part_of cytoplasm in GO (checked with oaklib), so this term is true but already entailed. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Cytoplasm {ECO:0000269|PubMed:16823372} |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Mitochondrial outer membrane by similarity to S. cerevisiae Ayr1 (multi-localised); not shown in S. pombe. Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt gives the mitochondrial outer membrane location with ECO:0000250 evidence from P40471, where Ayr1 forms an NADPH-regulated channel; not observed in the S. pombe localization screen. Peripheral to the ER/lipid-droplet reductase function, so non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Mitochondrion outer membrane {ECO:0000250|UniProtKB:P40471} file:SCHPO/ayr1/ayr1-uniprot.txt Forms an NADPH-regulated cation- selective channel in the mitochondrial outer membrane. |
| GO:0005741 mitochondrial outer membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mitochondrial outer membrane by similarity to S. cerevisiae Ayr1 (multi-localised); not shown in S. pombe. Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt gives the mitochondrial outer membrane location with ECO:0000250 evidence from P40471, where Ayr1 forms an NADPH-regulated channel; not observed in the S. pombe localization screen. Peripheral to the ER/lipid-droplet reductase function, so non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Mitochondrion outer membrane {ECO:0000250|UniProtKB:P40471} file:SCHPO/ayr1/ayr1-uniprot.txt Forms an NADPH-regulated cation- selective channel in the mitochondrial outer membrane. |
| GO:0005773 vacuole | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Vacuole, observed in the S. pombe ORFeome localization screen. Reason: S. pombe experiment: UniProt records Vacuole from the ORFeome localization screen (ECO:0000269, PubMed:16823372), which this SubCell mapping transfers. A secondary location of a multi-localised protein, peripheral to the ER/lipid-droplet reductase function. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Vacuole {ECO:0000269|PubMed:16823372} |
| GO:0005783 endoplasmic reticulum | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome screen: ER. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent. Reason: UniProt records an ER location for ayr1 from the S. pombe ORFeome localization screen (ECO:0000269, PubMed:16823372), which also supports the HDA row; the PAINT/keyword inference agrees with that direct observation and with S. cerevisiae Ayr1 at the ER. Root organelle term kept as informative. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Endoplasmic reticulum {ECO:0000269|PubMed:16823372} |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000044 | ACCEPT | Summary: Mapping; consistent. Reason: UniProt records an ER location for ayr1 from the S. pombe ORFeome localization screen (ECO:0000269, PubMed:16823372), which also supports the HDA row; the PAINT/keyword inference agrees with that direct observation and with S. cerevisiae Ayr1 at the ER. Root organelle term kept as informative. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Endoplasmic reticulum {ECO:0000269|PubMed:16823372} |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Golgi apparatus, observed in the S. pombe ORFeome localization screen. Reason: S. pombe experiment: UniProt records Golgi apparatus from the ORFeome localization screen (ECO:0000269, PubMed:16823372); the SubCell mapping rests on that direct observation, so the organelle claim holds. Root organelle term kept; the location is peripheral to the ER/lipid-droplet reductase function, so non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Golgi apparatus {ECO:0000269|PubMed:16823372} |
| GO:0005811 lipid droplet | IBA GO_REF:0000033 | ACCEPT | Summary: Lipid droplet location (PAINT/similarity); S. cerevisiae Ayr1 is a lipid-droplet and ER enzyme. Reason: The lipid-droplet location is curated by UniProt by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); it has not been observed for the S. pombe protein (the ORFeome screen reported ER, Golgi, vacuole and cytoplasm). Accepted on the ortholog evidence as part of the ER/lipid-droplet core location. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Lipid droplet {ECO:0000250|UniProtKB:P40471} |
| GO:0005811 lipid droplet | IEA GO_REF:0000044 | ACCEPT | Summary: Lipid droplet location (PAINT/similarity); S. cerevisiae Ayr1 is a lipid-droplet and ER enzyme. Reason: The lipid-droplet location is curated by UniProt by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); it has not been observed for the S. pombe protein (the ORFeome screen reported ER, Golgi, vacuole and cytoplasm). Accepted on the ortholog evidence as part of the ER/lipid-droplet core location. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Lipid droplet {ECO:0000250|UniProtKB:P40471} |
| GO:0005811 lipid droplet | ISS GO_REF:0000024 | ACCEPT | Summary: Lipid droplet location (PAINT/similarity); S. cerevisiae Ayr1 is a lipid-droplet and ER enzyme. Reason: The lipid-droplet location is curated by UniProt by similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250); it has not been observed for the S. pombe protein (the ORFeome screen reported ER, Golgi, vacuole and cytoplasm). Accepted on the ortholog evidence as part of the ER/lipid-droplet core location. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Lipid droplet {ECO:0000250|UniProtKB:P40471} |
| GO:0006654 phosphatidic acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference: acyl-DHAP reduction yields LPA for PA synthesis. Reason: By similarity to S. cerevisiae Ayr1 (P40471, ECO:0000250), UniProt curates ayr1 as required for phosphatidic acid synthesis via the DHAP pathway, where its own reductase step makes lysophosphatidic acid, so the gene product performs a step of the process. No S. pombe-specific study. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). |
| GO:0019433 triglyceride catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of TAG catabolism (minor lipase activity of the S. cerevisiae ortholog). Reason: By similarity to S. cerevisiae Ayr1 (P40471): UniProt states, with ECO:0000250 evidence from P40471, that the protein mobilises TAGs from lipid particles by hydrolysis; consistent with the PAINT node. No S. pombe experiment; a secondary role, so non-core. Supporting Evidence: file:SCHPO/ayr1/ayr1-uniprot.txt Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs. |
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