GPAM encodes mitochondrial glycerol-3-phosphate acyltransferase 1, which transfers a fatty acyl group from acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid. This early glycerolipid-biosynthetic reaction supplies precursors for membrane phospholipids and triacylglycerols. GPAT1 associates with the mitochondrial outer membrane through an amphipathic surface and an N-terminal targeting region. The selected protein sequence has an internal or terminal difference from the characterized human protein, so its precise activity and regulation remain to be established.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004366 glycerol-3-phosphate O-acyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: glycerol-3-phosphate O-acyltransferase activity: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000044 | ACCEPT | Summary: mitochondrial outer membrane: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0005886 plasma membrane | IEA GO_REF:0000002 | REMOVE | Summary: plasma membrane: The human GPAT1 structure and functional study localize GPAT1 to the mitochondrial outer membrane and identify its mitochondrial-targeting region. The electronic plasma-membrane assignment lacks a distinct localization mechanism and conflicts with that supported placement. Reason: The human GPAT1 structure and functional study localize GPAT1 to the mitochondrial outer membrane and identify its mitochondrial-targeting region. The electronic plasma-membrane assignment lacks a distinct localization mechanism and conflicts with that supported placement. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: lipid metabolic process: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0008654 phospholipid biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: phospholipid biosynthetic process: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0016024 CDP-diacylglycerol biosynthetic process | IEA GO_REF:0000104 | ACCEPT | Summary: CDP-diacylglycerol biosynthetic process: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: GPAT1 catalyzes the initial acyl-CoA-dependent step that supplies lysophosphatidic acid for glycerolipid synthesis at the mitochondrial outer membrane. Participation in downstream lipid biosynthetic routes does not mean GPAT1 catalyzes every later reaction. The human structural study independently establishes GPAT1 identity and membrane association. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000002 | MODIFY | Summary: acyltransferase activity: The acyltransferase assignment is correct but glycerol-3-phosphate O-acyltransferase activity identifies the physiological acceptor and reaction. Reason: The acyltransferase assignment is correct but glycerol-3-phosphate O-acyltransferase activity identifies the physiological acceptor and reaction. Proposed replacements: glycerol-3-phosphate O-acyltransferase activity Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups | IEA GO_REF:0000002 | MODIFY | Summary: acyltransferase activity, transferring groups other than amino-acyl groups: The acyltransferase assignment is correct but glycerol-3-phosphate O-acyltransferase activity identifies the physiological acceptor and reaction. Reason: The acyltransferase assignment is correct but glycerol-3-phosphate O-acyltransferase activity identifies the physiological acceptor and reaction. Proposed replacements: glycerol-3-phosphate O-acyltransferase activity Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: mitochondrial membrane: Mitochondrial association is correct but the outer-membrane location is more precise. Reason: Mitochondrial association is correct but the outer-membrane location is more precise. Supporting Evidence: PMID:36522428 Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. file:HORSE/GPAM/GPAM-bioinformatics/RESULTS.md The downloaded human Q9HCL2 sequence (828 residues) and selected horse A0A9L0TTC1 sequence (790 residues) share 94.2% identity among 790 paired residues. Paired coverage is 95.4% of human and 100.0% of horse. |
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