ale1 (lpt1; SPBC16A3.10; UniProt O42916) encodes the ER MBOAT-family lysophospholipid acyltransferase, the ortholog of S. cerevisiae Ale1/Lpt1. It reacylates lysophosphatidylcholine and lysophosphatidylethanolamine (and, more weakly, LPA) with acyl-CoA in the Lands-cycle remodelling of glycerophospholipids. Function is assigned by orthology; it is in the ER in a genome-wide screen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: LPA acyltransferase activity (PAINT/EC): MBOAT-family Ale1 acylates several lysophospholipids, including LPA; the main substrates are lyso-PC and lyso-PE. Reason: By similarity to the S. cerevisiae ortholog Lpt1/Ale1, which acylated a wide range of lysophospholipid acceptors including lysophosphatidic acid (PMID:17890783); UniProt's catalytic-activity lines for ale1 include the LPA acyl-CoA acyltransferase reaction alongside the lyso-PC and lyso-PE reactions, and the S. pombe protein is an MBOAT-family member (Pfam MBOAT). No S. pombe biochemistry. LPA acylation is a genuine but secondary activity; the core activities are lyso-PC/lyso-PE reacylation, so the term is kept as non-core. Supporting Evidence: PMID:17890783 Lpt1 catalyzed acyltransferase activity with a wide variety of lysophospholipids as acceptors, including lysophosphatidic acid file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA file:SCHPO/ale1/ale1-uniprot.txt Pfam; PF03062; MBOAT; 1. |
| GO:0003841 1-acylglycerol-3-phosphate O-acyltransferase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: LPA acyltransferase activity (PAINT/EC): MBOAT-family Ale1 acylates several lysophospholipids, including LPA; the main substrates are lyso-PC and lyso-PE. Reason: By similarity to the S. cerevisiae ortholog Lpt1/Ale1, which acylated a wide range of lysophospholipid acceptors including lysophosphatidic acid (PMID:17890783); UniProt's catalytic-activity lines for ale1 include the LPA acyl-CoA acyltransferase reaction alongside the lyso-PC and lyso-PE reactions, and the S. pombe protein is an MBOAT-family member (Pfam MBOAT). No S. pombe biochemistry. LPA acylation is a genuine but secondary activity; the core activities are lyso-PC/lyso-PE reacylation, so the term is kept as non-core. Supporting Evidence: PMID:17890783 Lpt1 catalyzed acyltransferase activity with a wide variety of lysophospholipids as acceptors, including lysophosphatidic acid file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA file:SCHPO/ale1/ale1-uniprot.txt Pfam; PF03062; MBOAT; 1. |
| 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's curated subcellular location for ale1 is the ER membrane (multi-pass, with predicted helical TRANSMEM segments); UniProt's RP line credits subcellular location and function to PMID:17890783, whose abstract shows the S. cerevisiae ortholog Lpt1-GFP at the ER. The root ER term is kept beside the ER-membrane rows (organelle policy). Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass file:SCHPO/ale1/ale1-uniprot.txt TRANSMEM 15..35 |
| GO:0005789 endoplasmic reticulum membrane | IC GO_REF:0000036 | ACCEPT | Summary: ER membrane; consistent. Reason: UniProt's curated subcellular location for ale1 is ER membrane, multi-pass, consistent with its predicted helical TRANSMEM segments; the ER location is credited (RP line) to PMID:17890783, which localised the S. cerevisiae ortholog Lpt1 to the ER. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass file:SCHPO/ale1/ale1-uniprot.txt TRANSMEM 15..35 |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: ER membrane; consistent. Reason: UniProt's curated subcellular location for ale1 is ER membrane, multi-pass, consistent with its predicted helical TRANSMEM segments; the ER location is credited (RP line) to PMID:17890783, which localised the S. cerevisiae ortholog Lpt1 to the ER. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass file:SCHPO/ale1/ale1-uniprot.txt TRANSMEM 15..35 |
| GO:0006646 phosphatidylethanolamine biosynthetic process | IC GO_REF:0000111 | ACCEPT | Summary: Curator inference: lyso-PE reacylation remodels PE (Lands cycle). Reason: UniProt's curated FUNCTION (ECO:0000269, PMID:17890783) and catalytic-activity lines give acyl-CoA-dependent reacylation of lyso-PE to diacyl-PE; this is PE formation by Lands-cycle remodelling rather than de novo synthesis. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a |
| GO:0006656 phosphatidylcholine biosynthetic process | IC GO_REF:0000111 | ACCEPT | Summary: Curator inference: lyso-PC reacylation remodels PC (Lands cycle). Reason: UniProt's curated FUNCTION (ECO:0000269, PMID:17890783) and catalytic-activity lines give acyl-CoA-dependent reacylation of lyso-PC to diacyl-PC; this is PC formation by Lands-cycle remodelling rather than de novo synthesis. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2- |
| GO:0016020 membrane | IBA GO_REF:0000033 | TOO GENERAL | Summary: Generic membrane; true, but entailed by the endoplasmic reticulum membrane rows. Reason: Ale1 is a multi-pass membrane protein (predicted helical TRANSMEM segments; UniProt curated location ER membrane, by similarity to the S. cerevisiae ortholog Lpt1, which localised to the ER in PMID:17890783). The more specific GO:0005789 endoplasmic reticulum membrane is asserted elsewhere in this review and entails this term. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass file:SCHPO/ale1/ale1-uniprot.txt TRANSMEM 15..35 |
| GO:0030258 lipid modification | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Lipid modification by sn-2 reacylation of lysophospholipids (Lands-cycle remodelling); true but peripheral to the specific acyltransferase and glycerophospholipid-biosynthesis rows. Reason: UniProt's curated FUNCTION (ECO:0000269, credited to PMID:17890783 on the S. cerevisiae ortholog Lpt1) has ale1 incorporating unsaturated acyl chains into the sn-2 position of phospholipids, which is a lipid modification. The PAINT node is consistent with MBOAT-family membership. No more specific descendant of lipid modification is asserted for the gene, so the term is kept as non-core rather than modified. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt InterPro; IPR004299; MBOAT_fam. |
| GO:0046474 glycerophospholipid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference: glycerophospholipid synthesis/remodelling. Reason: UniProt's curated FUNCTION (ECO:0000269, PMID:17890783) describes sn-2 acylation of phospholipids; the catalytic-activity lines give lyso-PA, lyso-PC and lyso-PE as acceptors, all glycerophospholipid-forming reactions. MBOAT family membership (Pfam MBOAT) is consistent with the PAINT node. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt DR Pfam; PF03062; MBOAT; 1. |
| GO:0047184 1-acylglycerophosphocholine O-acyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Lyso-PC acyltransferase activity (PAINT/EC; S. cerevisiae Ale1 ortholog). Reason: UniProt's curated FUNCTION line (ECO:0000269, credited to PMID:17890783, which characterised the S. cerevisiae ortholog Lpt1 with lyso-PC among its acceptors) and catalytic-activity line give lyso-PC + acyl-CoA -> PC; MBOAT family membership supports the PAINT node. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2- |
| GO:0047184 1-acylglycerophosphocholine O-acyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Lyso-PC acyltransferase activity (PAINT/EC; S. cerevisiae Ale1 ortholog). Reason: UniProt's curated FUNCTION line (ECO:0000269, credited to PMID:17890783, which characterised the S. cerevisiae ortholog Lpt1 with lyso-PC among its acceptors) and catalytic-activity line give lyso-PC + acyl-CoA -> PC, the reaction this EC/RHEA mapping encodes. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2- |
| GO:0106262 1-acylglycerophosphoethanolamine O-acyltransferase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Lyso-PE acyltransferase activity (EC/RHEA). Reason: UniProt's curated FUNCTION line (ECO:0000269, credited to PMID:17890783, which characterised the S. cerevisiae ortholog Lpt1 with lyso-PE among its acceptors) and catalytic-activity line give lyso-PE + acyl-CoA -> PE, the RHEA:32995 reaction behind this row. Supporting Evidence: file:SCHPO/ale1/ale1-uniprot.txt Membrane-bound O-acyltransferase that mediates the incorporation of unsaturated acyl chains into the sn-2 position of phospholipids file:SCHPO/ale1/ale1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a |
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