Psd1 (YNL169C) is the mitochondrial phosphatidylserine decarboxylase of Saccharomyces cerevisiae (EC 4.1.1.65), a type I PSD that decarboxylates phosphatidylserine to phosphatidylethanolamine and produces the majority of cellular PE. It is synthesized as a proenzyme that is imported into mitochondria and undergoes autocatalytic serine-dependent cleavage at an LGST motif into a membrane-anchored beta subunit and a pyruvoyl-containing alpha subunit; the active enzyme sits in the inner membrane with its catalytic site facing the intermembrane space and acts on PS imported from the ER. A minor pool of Psd1 is dual-targeted to the ER, where it supports lipid droplet biogenesis. Inner-membrane PE made by Psd1 is needed for respiratory complex III activity, normal mitochondrial morphology and fusion (including Mgm1 processing); psd1 psd2 double mutants are ethanolamine auxotrophs. Psd1 is also needed for efficient mitophagy after nitrogen starvation, probably because PE supply limits recruitment of lipidated Atg8 to mitochondria, whereas Psd2 matters more for stationary-phase mitophagy.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004609 phosphatidylserine decarboxylase activity | EXP PMID:6427211 Coordinate regulation of phosphatidylserine decarboxylase ac... | ACCEPT | Summary: Carson et al. 1984 characterized membrane PS decarboxylase activity in yeast (pre-cloning; the bulk of activity is Psd1). Core activity. Supporting Evidence: PMID:6427211 catalyze the decarboxylation of exogenous phosphatidylserine |
| GO:0004609 phosphatidylserine decarboxylase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN000007430 (type I PSDs incl. Arabidopsis, fly, S. pombe, rat and Psd1). Core activity. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | IDA PMID:23124206 Phosphatidylethanolamine biosynthesis in mitochondria: phosp... | ACCEPT | Summary: Tamura et al. 2012: in vitro Psd1-dependent PE production from fluorescent PS in isolated mitochondria. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA from InterPro/RHEA:20828/EC 4.1.1.65/UniRule. Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | IMP PMID:29290583 Lipid Homeostasis Is Maintained by Dual Targeting of the Mit... | ACCEPT | Summary: Friedman et al. 2018: Psd1 targeting variants and psd1 mutants alter PE synthesis. Core activity. Supporting Evidence: PMID:29290583 our analysis indicates that the TMR of Psd1 is both necessary and sufficient for dual targeting of Psd1 to mitochondria and ER membranes |
| GO:0004609 phosphatidylserine decarboxylase activity | IMP PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | ACCEPT | Summary: Gok et al. 2022: ER-localized Psd1 generates PE; mutant analysis. Supporting Evidence: PMID:34818062 PE generated by ER-localized Psd1 is required for normal LD morphology |
| GO:0004609 phosphatidylserine decarboxylase activity | IMP PMID:8407984 Phosphatidylserine decarboxylase from Saccharomyces cerevisi... | ACCEPT | Summary: Trotter et al. 1993: psd1 mutants and null allele lose most PSD activity. Supporting Evidence: PMID:8407984 Null mutations created by disrupting the PSD gene with TRP1 demonstrate that the gene is not essential for cell growth PMID:8407984 Analysis of lipid synthesis and enzyme activity in null mutants indicates that there are two PSD genes. |
| GO:0004609 phosphatidylserine decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways (PHOS-PWY, PHOSLIPSYN2-PWY-1, PWY-5669 PE biosynthesis I, PWY3O-2) assigns Psd1 to PS -> PE + CO2 (EC 4.1.1.65). Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways (PHOS-PWY, PHOSLIPSYN2-PWY-1, PWY-5669 PE biosynthesis I, PWY3O-2) assigns Psd1 to PS -> PE + CO2 (EC 4.1.1.65). Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways (PHOS-PWY, PHOSLIPSYN2-PWY-1, PWY-5669 PE biosynthesis I, PWY3O-2) assigns Psd1 to PS -> PE + CO2 (EC 4.1.1.65). Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0004609 phosphatidylserine decarboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways (PHOS-PWY, PHOSLIPSYN2-PWY-1, PWY-5669 PE biosynthesis I, PWY3O-2) assigns Psd1 to PS -> PE + CO2 (EC 4.1.1.65). Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005739 mitochondrion | HDA PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. | ACCEPT | Summary: Detected in purified mitochondria by proteomics. Correct (inner membrane enzyme). Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: Detected in purified mitochondria by proteomics. Correct (inner membrane enzyme). Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: Detected in purified mitochondria by proteomics. Correct (inner membrane enzyme). Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: IBA is_active_in mitochondrion from PTN000007431. Correct. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane |
| GO:0005739 mitochondrion | IDA PMID:29290583 Lipid Homeostasis Is Maintained by Dual Targeting of the Mit... | ACCEPT | Summary: Fluorescence microscopy of Psd1-EGFP shows mitochondrial (and ER) localization. Supporting Evidence: PMID:29290583 our analysis indicates that the TMR of Psd1 is both necessary and sufficient for dual targeting of Psd1 to mitochondria and ER membranes |
| GO:0005739 mitochondrion | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro IPR033661 (type 1 eukaryotic PSD) to mitochondrion. Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005739 mitochondrion | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways PHOS-PWY places the step in mitochondria. Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0005743 mitochondrial inner membrane | EXP PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. | ACCEPT | Summary: Inner membrane localization from submitochondrial fractionation/topology studies. Core location. Supporting Evidence: PMID:22984266 we report that in yeast the Psd1 Ξ²-subunit (Psd1Ξ²) is integrated into the mitochondrial inner membrane and serves as an anchor for the intermembrane space-localized Ξ±-subunit (Psd1Ξ±) PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005743 mitochondrial inner membrane | EXP PMID:22984266 Processing and topology of the yeast mitochondrial phosphati... | ACCEPT | Summary: Inner membrane localization from submitochondrial fractionation/topology studies. Core location. Supporting Evidence: PMID:22984266 we report that in yeast the Psd1 Ξ²-subunit (Psd1Ξ²) is integrated into the mitochondrial inner membrane and serves as an anchor for the intermembrane space-localized Ξ±-subunit (Psd1Ξ±) PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005743 mitochondrial inner membrane | EXP PMID:29290583 Lipid Homeostasis Is Maintained by Dual Targeting of the Mit... | ACCEPT | Summary: Inner membrane localization from submitochondrial fractionation/topology studies. Core location. Supporting Evidence: PMID:22984266 we report that in yeast the Psd1 Ξ²-subunit (Psd1Ξ²) is integrated into the mitochondrial inner membrane and serves as an anchor for the intermembrane space-localized Ξ±-subunit (Psd1Ξ±) PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005743 mitochondrial inner membrane | EXP PMID:3005242 Subcellular and submitochondrial localization of phospholipi... | ACCEPT | Summary: Inner membrane localization from submitochondrial fractionation/topology studies. Core location. Supporting Evidence: PMID:22984266 we report that in yeast the Psd1 Ξ²-subunit (Psd1Ξ²) is integrated into the mitochondrial inner membrane and serves as an anchor for the intermembrane space-localized Ξ±-subunit (Psd1Ξ±) PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005743 mitochondrial inner membrane | IDA PMID:23124206 Phosphatidylethanolamine biosynthesis in mitochondria: phosp... | ACCEPT | Summary: Psd1 decarboxylates PS in the inner membrane; embedded in IM with catalytic site in IMS. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:33718843 Mitochondrial PE is produced by phosphatidylserine decarboxylase-1 (Psd1), an enzyme that is embedded in the IM with its catalytic site in the IMS |
| GO:0005743 mitochondrial inner membrane | IDA PMID:33718843 Impaired phosphatidylethanolamine metabolism activates a rev... | ACCEPT | Summary: Psd1 decarboxylates PS in the inner membrane; embedded in IM with catalytic site in IMS. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:33718843 Mitochondrial PE is produced by phosphatidylserine decarboxylase-1 (Psd1), an enzyme that is embedded in the IM with its catalytic site in the IMS |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000120 | ACCEPT | Summary: UniProt subcellular location/UniRule mapping to mitochondrial inner membrane. Correct. Supporting Evidence: file:yeast/PSD1/PSD1-uniprot.txt Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:29290583 Lipid Homeostasis Is Maintained by Dual Targeting of the Mit... | ACCEPT | Summary: Friedman et al. 2018 showed dual targeting of Psd1 to mitochondria and ER via its TMR. Minor but functional pool. Supporting Evidence: PMID:29290583 our analysis indicates that the TMR of Psd1 is both necessary and sufficient for dual targeting of Psd1 to mitochondria and ER membranes |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | ACCEPT | Summary: Gok et al. 2022 imaged Psd1 on the ER membrane, concentrated near nascent lipid droplets; ER-Psd1 makes PE for LD biogenesis. Supporting Evidence: PMID:34818062 Here, we show that Psd1 can target on the ER membrane to a subset of LDs, particularly under conditions that promote LD biogenesis. PMID:34818062 PE generated by ER-localized Psd1 is required for normal LD morphology |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | ACCEPT | Summary: Gok et al. 2022 imaged Psd1 on the ER membrane, concentrated near nascent lipid droplets; ER-Psd1 makes PE for LD biogenesis. Supporting Evidence: PMID:34818062 Here, we show that Psd1 can target on the ER membrane to a subset of LDs, particularly under conditions that promote LD biogenesis. PMID:34818062 PE generated by ER-localized Psd1 is required for normal LD morphology |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping to ER membrane. Supported by imaging data. Supporting Evidence: PMID:29290583 our analysis indicates that the TMR of Psd1 is both necessary and sufficient for dual targeting of Psd1 to mitochondria and ER membranes |
| GO:0005811 lipid droplet | IDA PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | KEEP AS NON CORE | Summary: Psd1 targets ER subdomains associated with a subset of lipid droplets during LD biogenesis. Located at ER-LD sites rather than a stable LD-surface protein. Reason: Transient, minor location associated with ER-Psd1. Supporting Evidence: PMID:34818062 Here, we show that Psd1 can target on the ER membrane to a subset of LDs, particularly under conditions that promote LD biogenesis. |
| GO:0005811 lipid droplet | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular location (Lipid droplet) mapping, derived from Gok et al. 2022. Minor location. Reason: Minor location. Supporting Evidence: PMID:34818062 Here, we show that Psd1 can target on the ER membrane to a subset of LDs, particularly under conditions that promote LD biogenesis. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA places the PSD step in the cytosol. Psd1 is an inner mitochondrial membrane (and ER membrane) enzyme acting on membrane PS; cytosol is wrong and conflicts with the PHOS-PWY mitochondrion row. Reason: Localization default of the pathway conversion; contradicted by extensive localization data. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA places the PSD step in the cytosol. Psd1 is an inner mitochondrial membrane (and ER membrane) enzyme acting on membrane PS; cytosol is wrong and conflicts with the PHOS-PWY mitochondrion row. Reason: Localization default of the pathway conversion; contradicted by extensive localization data. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA places the PSD step in the cytosol. Psd1 is an inner mitochondrial membrane (and ER membrane) enzyme acting on membrane PS; cytosol is wrong and conflicts with the PHOS-PWY mitochondrion row. Reason: Localization default of the pathway conversion; contradicted by extensive localization data. Supporting Evidence: PMID:23124206 PS is transferred from the mitochondrial outer membrane to the inner membrane independently of Psd1p, Ups1p, and Ups2p and decarboxylated to PE by Psd1p in the inner membrane PMID:3005242 Phosphatidylserine decarboxylase and phosphatidylglycerolphosphate synthase were localized exclusively in the inner mitochondrial membrane |
| GO:0006122 mitochondrial electron transport, ubiquinol to cytochrome c | IMP PMID:30926815 Phosphatidylethanolamine made in the inner mitochondrial mem... | MARK AS OVER ANNOTATED | Summary: Calzada et al. 2019 showed inner-membrane PE made by Psd1 is needed for full complex III activity. Psd1 supplies a lipid that complex III needs; it does not itself transfer electrons. Reason: Indirect effect of the lipid product; Psd1 is not a participant in ubiquinol-cytochrome c electron transfer. Supporting Evidence: PMID:30926815 Our work supports a specific role of IM-synthesized PE in complex III activity |
| GO:0006646 phosphatidylethanolamine biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN000007430. Core process. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0006646 phosphatidylethanolamine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: UniRule/UniPathway UPA00558 (PE from CDP-DAG, step 2/2) mapping. Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0006646 phosphatidylethanolamine biosynthetic process | IMP PMID:29290583 Lipid Homeostasis Is Maintained by Dual Targeting of the Mit... | ACCEPT | Summary: psd1 mutants and targeting variants show Psd1 makes most cellular PE, from both mitochondrial and ER locations. Supporting Evidence: PMID:29290583 our analysis indicates that the TMR of Psd1 is both necessary and sufficient for dual targeting of Psd1 to mitochondria and ER membranes |
| GO:0006646 phosphatidylethanolamine biosynthetic process | IMP PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | ACCEPT | Summary: ER-localized Psd1 contributes PE needed for LD morphology. Supporting Evidence: PMID:34818062 PE generated by ER-localized Psd1 is required for normal LD morphology |
| GO:0006646 phosphatidylethanolamine biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways PWY-5669 (PE biosynthesis I) RCA. Correct. Supporting Evidence: PMID:23124206 In yeast, the majority of PE is produced from phosphatidylserine (PS) by a mitochondrion-located PS decarboxylase, Psd1p. |
| GO:0006656 phosphatidylcholine biosynthetic process | IDA PMID:6427211 Coordinate regulation of phosphatidylserine decarboxylase ac... | KEEP AS NON CORE | Summary: Carson et al. 1984 showed membrane PS decarboxylase couples with phospholipid N-methyltransferases to make PC from PS. PSD performs the PS->PE step of the de novo (CDP-DAG/methylation) route to PC, upstream of Cho2/Opi3. Reason: Correct upstream step of de novo PC synthesis, but the direct product and core process is PE. Supporting Evidence: PMID:6427211 endogenous, prelabeled phosphatidylserine can be utilized for the biosynthesis of phosphatidylcholine by the coupled action of the hydroxylamine-sensitive decarboxylase and the phospholipid N-methyltransferases |
| GO:0008654 phospholipid biosynthetic process | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro IPR003817/IPR033177 to phospholipid biosynthetic process. Correct general term. Reason: True, but entailed by the more specific GO:0006646 phosphatidylethanolamine biosynthetic process, accepted in this review. Supporting Evidence: PMID:8407984 Phosphatidylserine decarboxylase plays a pivotal role in the synthesis of phospholipid by the mitochondria. |
| GO:0008654 phospholipid biosynthetic process | RCA GO_REF:0000123 | TOO GENERAL | Summary: YeastPathways superpathway RCA. Correct general term. Reason: True, but entailed by the more specific GO:0006646 phosphatidylethanolamine biosynthetic process, accepted in this review. Supporting Evidence: PMID:8407984 Phosphatidylserine decarboxylase plays a pivotal role in the synthesis of phospholipid by the mitochondria. |
| GO:0008654 phospholipid biosynthetic process | RCA GO_REF:0000123 | TOO GENERAL | Summary: YeastPathways superpathway RCA. Correct general term. Reason: True, but entailed by the more specific GO:0006646 phosphatidylethanolamine biosynthetic process, accepted in this review. Supporting Evidence: PMID:8407984 Phosphatidylserine decarboxylase plays a pivotal role in the synthesis of phospholipid by the mitochondria. |
| GO:0008654 phospholipid biosynthetic process | RCA GO_REF:0000123 | TOO GENERAL | Summary: YeastPathways superpathway RCA. Correct general term. Reason: True, but entailed by the more specific GO:0006646 phosphatidylethanolamine biosynthetic process, accepted in this review. Supporting Evidence: PMID:8407984 Phosphatidylserine decarboxylase plays a pivotal role in the synthesis of phospholipid by the mitochondria. |
| GO:0010636 positive regulation of mitochondrial fusion | IMP PMID:23045528 Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochond... | KEEP AS NON CORE | Summary: psd1 cells show fragmented mitochondria and impaired fusion in mating, attributed to reduced mitochondrial PE altering membrane properties and s-Mgm1 biogenesis. Downstream effect of Psd1's lipid product. Reason: Supported by curator IMP; mechanism is via PE supply rather than a dedicated fusion-regulatory activity. Supporting Evidence: PMID:23045528 Here, we show that mitochondrial-localized Psd1, the key yeast enzyme that synthesizes PE, is required for proper mitochondrial morphology and fusion. |
| GO:0010954 positive regulation of protein processing | IMP PMID:23045528 Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochond... | MARK AS OVER ANNOTATED | Summary: Loss of Psd1 impairs biogenesis of short Mgm1 (Pcp1-mediated processing). This reflects the PE dependence of Mgm1 alternative topogenesis; Psd1 does not regulate protease activity directly. Reason: Indirect consequence of lipid composition; over-interpretation as regulation of protein processing. Supporting Evidence: PMID:23045528 The loss of Psd1 also impairs the biogenesis of s-Mgm1, a protein essential for mitochondrial fusion |
| GO:0016540 protein autoprocessing | IDA PMID:25829489 Phosphatidylserine decarboxylase 1 autocatalysis and functio... | ACCEPT | Summary: Onguka et al. 2015: Psd1 self-cleaves at the LGST motif (serine required) without a mitochondrial-specific factor. Autoprocessing is the substrate itself doing the cleavage. Supporting Evidence: PMID:25829489 To become catalytically active, Psd1p undergoes an autocatalytic processing step involving a conserved LGST motif PMID:25829489 only the serine residue is absolutely required for Psd1p autocatalysis and function |
| GO:0016540 protein autoprocessing | IEA GO_REF:0000104 | ACCEPT | Summary: UniRule (HAMAP MF_03208) mapping for PSD proenzyme self-maturation. Correct. Supporting Evidence: PMID:25829489 To become catalytically active, Psd1p undergoes an autocatalytic processing step involving a conserved LGST motif |
| GO:0046474 glycerophospholipid biosynthetic process | IEA GO_REF:0000117 | TOO GENERAL | Summary: ARBA mapping to glycerophospholipid biosynthetic process. Correct general term. Reason: True, but entailed by the more specific GO:0006646 phosphatidylethanolamine biosynthetic process, accepted in this review. Supporting Evidence: PMID:8407984 Phosphatidylserine decarboxylase plays a pivotal role in the synthesis of phospholipid by the mitochondria. |
| GO:0140042 lipid droplet formation | IDA PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | KEEP AS NON CORE | Summary: Gok et al. 2022: Psd1 concentrates at ER sites of LD biogenesis. Reason: Real but secondary role of the minor ER pool, mediated by local PE production. Supporting Evidence: PMID:34818062 Here, we show that Psd1 can target on the ER membrane to a subset of LDs, particularly under conditions that promote LD biogenesis. |
| GO:0140042 lipid droplet formation | IMP PMID:34818062 ER-localized phosphatidylethanolamine synthase plays a conse... | KEEP AS NON CORE | Summary: Cells lacking ER-localized Psd1 (Psd1mito) show altered LD morphology/biogenesis in sensitized backgrounds. Reason: Secondary role of ER-Psd1 through PE supply. Supporting Evidence: PMID:34818062 PE generated by ER-localized Psd1 is required for normal LD morphology |
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