Carnitine O-palmitoyltransferase 1, liver isoform (CPT1A) is the liver-type isoform of carnitine palmitoyltransferase 1, a multi-pass protein of the mitochondrial outer membrane with a large cytoplasmic C-terminal catalytic domain. It catalyzes the committed, rate-limiting step of long-chain fatty acid entry into mitochondria for beta-oxidation, transferring the acyl group of long-chain acyl-CoA thioesters (e.g. palmitoyl-CoA) onto L-carnitine to form long-chain acylcarnitine plus CoA (EC 2.3.1.21). As the principal regulatory node of the carnitine shuttle, its activity is allosterically inhibited by malonyl-CoA, coupling fatty-acid oxidation to fatty-acid synthesis and nutritional state. Loss-of-function variants cause carnitine palmitoyltransferase 1A deficiency, an autosomal recessive disorder of fatty-acid oxidation presenting with hypoketotic hypoglycemia. Beyond its canonical acyltransferase role, CPT1A has reported secondary activities, including a lysine succinyltransferase activity and a catalysis-independent scaffolding function that recruits ZDHHC4 to promote MAVS palmitoylation and sustain the type I interferon response.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004095 carnitine O-palmitoyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) assignment of the defining molecular function of CPT1A, transfer of a long-chain acyl group from acyl-CoA to carnitine. This is strongly supported by direct experimental characterization of the human enzyme and is the core function of the gene. Reason: The carnitine O-palmitoyltransferase activity (EC 2.3.1.21) is the well-established catalytic function of CPT1A and is the correct level of specificity. It is corroborated by multiple experimental annotations in this dataset. Supporting Evidence: PMID:14517221 Carnitine palmitoyltransferase 1A (CPT1A) is the |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic assignment placing CPT1A activity in the mitochondrion. Correct but less specific than the experimentally supported mitochondrial outer membrane localization. Reason: The mitochondrion is a true but general compartment; the specific and informative localization is the mitochondrial outer membrane (GO:0005741), which is captured by experimental annotations. Retained as non-core parent term. Supporting Evidence: PMID:11350182 alters neither mitochondrial targeting nor stability of the CPT1A |
| GO:0006631 fatty acid metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic assignment of a general fatty acid metabolic role. True but a broad parent of the more specific beta-oxidation / long-chain fatty acid metabolic terms. Reason: CPT1A is genuinely involved in fatty acid metabolism, but this term is a general parent; the specific process is long-chain fatty acid import for beta-oxidation (GO:0006635, GO:0001676). Kept as non-core. Supporting Evidence: PMID:14517221 key regulatory enzyme of |
| GO:0009437 carnitine metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic assignment of a carnitine metabolic role, consistent with CPT1A producing acylcarnitine from carnitine as part of the carnitine shuttle. Reason: CPT1A consumes L-carnitine to generate long-chain acylcarnitine, directly participating in carnitine metabolism; supported experimentally (PMID:11350182, IDA in this dataset). Supporting Evidence: PMID:14517221 Carnitine palmitoyltransferase 1A (CPT1A) is the |
| GO:0004095 carnitine O-palmitoyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment (ARBA/RHEA/EC 2.3.1.21) of the core carnitine O-palmitoyltransferase activity, matching the experimentally established function. Reason: Correct and specific molecular function, consistent with the RHEA:12661 reaction and EC 2.3.1.21 in the UniProt record and multiple experimental annotations. Supporting Evidence: PMID:14517221 Carnitine palmitoyltransferase 1A (CPT1A) is the |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment of the mitochondrial outer membrane localization, matching the experimentally verified subcellular location of CPT1A. Reason: The mitochondrial outer membrane is the correct, specific compartment for CPT1A and is supported experimentally (PMID:11350182, PMID:14517221) and by the UniProt SUBCELLULAR LOCATION statement. Supporting Evidence: PMID:16651524 an outer mitochondrial membrane enzyme |
| GO:0006853 carnitine shuttle | IEA GO_REF:0000117 | ACCEPT | Summary: Electronic (ARBA) assignment of the carnitine shuttle process. CPT1A catalyzes the first, committed step of the carnitine shuttle that imports long-chain fatty acids into mitochondria. Reason: CPT1A performs the rate-limiting acylcarnitine-forming step of the carnitine shuttle; a correct and specific process term. Corroborated by the Reactome TAS annotation to the same term. Supporting Evidence: PMID:16651524 controls entry of fatty acids into mitochondria and, thereby, fatty acid oxidation |
| GO:0016746 acyltransferase activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro-based electronic assignment of the general acyltransferase activity (from the carnitine acyltransferase domain IPR000542). This is a broad parent of the specific carnitine O-palmitoyltransferase activity. Reason: Not wrong, but a general parent of GO:0004095 which is annotated more precisely. The specific carnitine O-palmitoyltransferase activity should be preferred as the informative molecular function. Proposed replacements: carnitine O-palmitoyltransferase activity |
| GO:0001666 response to hypoxia | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer of a rat-ortholog phenotype/expression annotation. Reflects downstream physiology rather than CPT1A's molecular function. Reason: Response to hypoxia is a plausible physiological context for fatty-acid oxidation regulation but is transferred from the rat ortholog and is not a core molecular activity of CPT1A. Retained as non-core. |
| GO:0001676 long-chain fatty acid metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: Electronic assignment of long-chain fatty acid metabolic process, matching the substrate specificity of CPT1A (long-chain acyl-CoA thioesters). Reason: CPT1A acts specifically on long-chain acyl-CoA substrates to enable their mitochondrial oxidation; this specific process term is well supported (also IDA PMID:11350182 in this dataset). Supporting Evidence: PMID:14517221 hepatic long-chain fatty acid beta-oxidation |
| GO:0006006 glucose metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. Reflects the indirect metabolic influence of fatty-acid oxidation on glucose handling rather than a direct role. Reason: Any effect on glucose metabolism is downstream/indirect (fatty-acid oxidation spares glucose); not a core CPT1A function. Retained as non-core. |
| GO:0006631 fatty acid metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic assignment of the general fatty acid metabolic process, duplicating the IBA annotation to the same broad parent term. Reason: True but general; the specific process is long-chain fatty acid import for beta-oxidation. Kept as non-core parent. |
| GO:0006635 fatty acid beta-oxidation | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic assignment (ARBA/UniPathway UPA00659) of fatty acid beta-oxidation. CPT1A catalyzes the rate-limiting import step required for mitochondrial beta-oxidation of long-chain fatty acids. Reason: CPT1A is the committed step controlling long-chain fatty-acid entry for beta-oxidation; a correct and central process term, corroborated by TAS (PMID:7892212) and ISS annotations. Supporting Evidence: PMID:9691089 decreased rate of fatty acid beta-oxidation |
| GO:0006641 triglyceride metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. UniProt notes a role in hepatic triglyceride metabolism (by similarity), but this is a downstream/indirect physiological consequence. Reason: Consistent with a hepatic triglyceride-metabolism role inferred by similarity, but indirect relative to the core acyltransferase function. Retained as non-core. |
| GO:0007584 response to nutrient | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog capturing nutritional regulation of CPT1A/fatty-acid oxidation. Reason: Reflects physiological regulation (CPT1A is induced by fatty acids and regulated by nutritional state) rather than a core molecular function. Retained as non-core. |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog. Off-context response term with no direct mechanistic link to CPT1A's function established for human. Reason: Xenobiotic-response annotation transferred from the rat ortholog does not inform CPT1A's molecular function and is a likely over-annotation for the human gene. |
| GO:0009437 carnitine metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: Electronic assignment of carnitine metabolic process, duplicating the IBA/IDA annotations. Consistent with CPT1A consuming carnitine to form acylcarnitine. Reason: CPT1A directly participates in carnitine metabolism as part of the carnitine shuttle; correct process term corroborated by experimental (IDA) evidence. Supporting Evidence: PMID:16651524 catalyze acyl transfer from various fatty |
| GO:0031667 response to nutrient levels | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog capturing regulation by nutritional state (fasting/feeding). Reason: Reflects physiological regulation of CPT1A rather than its core molecular activity. Retained as non-core. |
| GO:0032000 positive regulation of fatty acid beta-oxidation | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog. CPT1A is the enzyme that carries out the rate-limiting step of beta-oxidation; framing this as CPT1A positively regulating beta-oxidation is largely self-referential. Reason: CPT1A executes the committed step of long-chain beta-oxidation (captured by GO:0006635); a separate positive-regulation term for the enzyme regulating the very process it catalyzes is an over-annotation. |
| GO:0042755 eating behavior | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog. Eating-behavior/energy-homeostasis roles are best established for the brain isoform CPT1C, not the liver CPT1A. Reason: Feeding-behavior control via malonyl-CoA sensing is chiefly attributed to the brain-specific CPT1C (PMID:16651524); assigning eating behavior to liver CPT1A by ortholog transfer is a likely over-annotation. Supporting Evidence: PMID:16651524 CPT1c KO mice have lower body weight and food intake |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog of self-association. CPT1A is reported to form homo-oligomers (homohexamer/homotrimer, by similarity), but the bare identical protein binding term is uninformative about function. Reason: Although CPT1A oligomerizes, identical protein binding is an uninformative binding term that does not describe a molecular function; over-annotation. |
| GO:0043279 response to alkaloid | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog. Off-context response term with no direct mechanistic link to human CPT1A function. Reason: Transferred response term that does not inform CPT1A's molecular function; likely over-annotation for the human gene. |
| GO:0045471 response to ethanol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. Ethanol modulates hepatic fatty-acid oxidation, but this is downstream physiology transferred from another species. Reason: Plausible physiological context for a hepatic fatty-acid-oxidation enzyme but not a core function; retained as non-core. |
| GO:0046320 regulation of fatty acid oxidation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. CPT1A is the principal regulatory point of fatty-acid oxidation (malonyl-CoA-sensitive), consistent with a regulatory role. Reason: CPT1A is the key regulatory node of fatty-acid oxidation, so a regulatory process annotation is defensible, but the informative statement is its catalytic role in beta-oxidation. Retained as non-core. Supporting Evidence: PMID:16651524 Malonyl-CoA is an established inhibitor of |
| GO:0050796 regulation of insulin secretion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. Fatty-acid oxidation influences beta-cell insulin secretion, but this is indirect physiology transferred across species. Reason: Indirect physiological effect rather than a core CPT1A activity; retained as non-core. |
| GO:0071398 cellular response to fatty acid | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Electronic transfer from the rat ortholog. CPT1A is transcriptionally up-regulated by fatty acids (UniProt INDUCTION; PMID:16271724), consistent with responding to fatty acids. Reason: Consistent with fatty-acid induction of CPT1A, but this is a regulatory/response context rather than the core molecular function. Retained as non-core. |
| GO:0097421 liver regeneration | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog. Highly indirect physiological context with no direct mechanistic tie to CPT1A's molecular function. Reason: Liver-regeneration annotation transferred from the rat ortholog is far removed from CPT1A's molecular activity; likely over-annotation. |
| GO:1904772 response to tetrachloromethane | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from the rat ortholog (a hepatotoxicant-exposure response). Off-context and does not inform CPT1A function. Reason: Toxicant-response term transferred from the rat ortholog; does not describe CPT1A's molecular function. Likely over-annotation. |
| GO:0001678 intracellular glucose homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Sequence-similarity transfer (from mouse Cpt1a) of a glucose-homeostasis role. Reflects the indirect metabolic coupling between fatty-acid oxidation and glucose handling. Reason: Effect on glucose homeostasis is downstream of the enzyme's fatty-acid-oxidation function rather than a direct activity; retained as non-core. |
| GO:0006635 fatty acid beta-oxidation | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of the fatty acid beta-oxidation process, consistent with CPT1A's role as the committed step of long-chain fatty-acid import for beta-oxidation. Reason: Correct central process term, corroborated by IEA, TAS (PMID:7892212) and the enzyme's established biology. Supporting Evidence: PMID:9691089 decreased rate of fatty acid beta-oxidation |
| GO:0006853 carnitine shuttle | TAS Reactome:R-HSA-200425 | ACCEPT | Summary: Reactome traceable-author-statement placing CPT1A in the carnitine shuttle pathway, where it catalyzes the initial acylcarnitine-forming step. Reason: Accurately reflects CPT1A's role as the first, rate-limiting step of the carnitine shuttle that imports long-chain fatty acids into mitochondria. Supporting Evidence: PMID:16651524 controls entry of fatty acids into mitochondria and, thereby, fatty acid oxidation |
| GO:0004095 carnitine O-palmitoyltransferase activity | EXP PMID:14517221 Functional and structural basis of carnitine palmitoyltransf... | ACCEPT | Summary: Experimental characterization of CPT1A carnitine O-palmitoyltransferase activity, including kinetics and disease-variant analysis in a heterologous yeast expression system. Reason: Directly supports the core catalytic function of CPT1A; disease-causing variants (e.g. G709E, G710E) abolish this activity, confirming its centrality. Supporting Evidence: PMID:14517221 mutations G709E and G710E, which abolish |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Immunofluorescence-based (HPA) localization of CPT1A to the mitochondrion. Correct but less specific than the mitochondrial outer membrane localization. Reason: Consistent with CPT1A localization; the more specific and informative compartment is the mitochondrial outer membrane (GO:0005741). Retained as non-core parent. |
| GO:0004095 carnitine O-palmitoyltransferase activity | EXP PMID:16651524 The brain-specific carnitine palmitoyltransferase-1c regulat... | ACCEPT | Summary: Experimental comparison showing that CPT1A (liver) catalyzes acyl transfer from fatty acyl-CoAs to carnitine, in contrast to the catalytically inactive brain isoform CPT1C. Reason: Directly supports CPT1A's carnitine O-palmitoyltransferase activity as its core molecular function. Supporting Evidence: PMID:16651524 CPT1a and CPT1b catalyze acyl transfer from various fatty |
| GO:0005741 mitochondrial outer membrane | EXP PMID:11350182 Molecular and enzymatic characterization of a unique carniti... | ACCEPT | Summary: Experimental determination of CPT1A subcellular location at the mitochondrial outer membrane (variant characterization also assessed mitochondrial targeting). Reason: The mitochondrial outer membrane is the specific, correct compartment for CPT1A, consistent with the UniProt SUBCELLULAR LOCATION statement and the two-transmembrane-helix outer-membrane topology. Supporting Evidence: PMID:11350182 alters neither mitochondrial targeting nor stability of the CPT1A |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | KEEP AS NON CORE | Summary: High-throughput mitochondrial proteome study detecting CPT1A in the mitochondrion. Correct but less specific than the outer-membrane localization. Reason: Supports mitochondrial localization at low specificity; the informative compartment is the mitochondrial outer membrane. Retained as non-core parent. |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:38016475 CPT1A induction following epigenetic perturbation promotes M... | ACCEPT | Summary: CPT1A acts as an adaptor/scaffold that recruits the ER-localized palmitoyl transferase ZDHHC4 to MAVS, promoting MAVS Cys79-palmitoylation; a catalytically-dead H473A mutant retains this scaffolding activity, showing it is independent of the acyltransferase activity. Reason: Directly demonstrated adaptor/scaffold function bridging ZDHHC4 and MAVS. This is a genuine but non-core (moonlighting) molecular function, distinct from the canonical carnitine O-palmitoyltransferase activity. Supporting Evidence: PMID:38016475 CPT1A recruits the endoplasmic |
| GO:0045089 positive regulation of innate immune response | IDA PMID:38016475 CPT1A induction following epigenetic perturbation promotes M... | ACCEPT | Summary: By recruiting ZDHHC4 to palmitoylate and stabilize MAVS, CPT1A sustains a double-stranded-RNA-activated type I interferon response and potentiates antitumor immunity. Reason: Experimentally supported role in positively regulating the innate (type I IFN) immune response via MAVS stabilization; a real but non-core process for this metabolic enzyme. Supporting Evidence: PMID:38016475 sustains, a double-stranded |
| GO:0004095 carnitine O-palmitoyltransferase activity | IMP PMID:14517221 Functional and structural basis of carnitine palmitoyltransf... | ACCEPT | Summary: Mutant-phenotype evidence in which disease-causing missense variants (G709E, G710E) abolish CPT1A carnitine O-palmitoyltransferase activity, demonstrating the wild-type enzyme carries out this reaction. Reason: Supports the core catalytic function through loss-of-function variant analysis; consistent with the EXP annotation from the same study. Supporting Evidence: PMID:14517221 mutations G709E and G710E, which abolish |
| GO:0004095 carnitine O-palmitoyltransferase activity | IMP PMID:9691089 Molecular basis of hepatic carnitine palmitoyltransferase I ... | ACCEPT | Summary: Mutant-phenotype evidence in which the disease-causing D454G variant expressed in yeast retained only ~2% of wild-type activity, establishing CPT1A's carnitine O-palmitoyltransferase activity. Reason: Loss-of-function variant confirms the core catalytic function of CPT1A. Supporting Evidence: PMID:9691089 D454G mutation is the disease-causing mutation |
| GO:0005741 mitochondrial outer membrane | IMP PMID:14517221 Functional and structural basis of carnitine palmitoyltransf... | ACCEPT | Summary: Variant/expression analysis consistent with CPT1A residing at the mitochondrial outer membrane. Reason: Supports the specific, correct mitochondrial outer membrane localization, concordant with the EXP and ISS annotations to the same term. Supporting Evidence: PMID:16651524 an outer mitochondrial membrane enzyme |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MARK AS OVER ANNOTATED | Summary: High-throughput membrane-proteome detection of CPT1A in an NK-like cell line. Correct at a very general level (CPT1A is a membrane protein) but off-context and uninformative. Reason: CPT1A is indeed a membrane protein, but membrane is a very general term and this detection comes from an unrelated NK-cell membrane proteomics screen; the informative localization is the mitochondrial outer membrane. |
| GO:0004095 carnitine O-palmitoyltransferase activity | IDA PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I: ... | ACCEPT | Summary: Characterization of the cloned human liver CPT I cDNA/enzyme, establishing it as a carnitine palmitoyltransferase (EC 2.3.1.21) distinct from CPT II. Reason: Foundational characterization supporting the core carnitine O-palmitoyltransferase activity of human CPT1A. Supporting Evidence: PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I |
| GO:0030855 epithelial cell differentiation | IEP PMID:21492153 Analysis of proteomic changes induced upon cellular differen... | MARK AS OVER ANNOTATED | Summary: Expression-pattern evidence in which CPT1A was among lipid-metabolism proteins up-regulated during differentiation of the Caco-2 intestinal cell line. This is a correlative association, not a demonstrated role in differentiation. Reason: The IEP annotation reflects a correlative change in CPT1A abundance during Caco-2 differentiation, not evidence that CPT1A drives epithelial cell differentiation; likely over-annotation. Supporting Evidence: PMID:21492153 proteins involved in xenobiotic and drug metabolism as well as in lipid metabolism were upregulated upon cellular differentiation |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-200406 | ACCEPT | Summary: Reactome traceable-author-statement placing CPT1A at the mitochondrial outer membrane, where it transfers palmitoyl to carnitine. Reason: Concordant with the experimentally established mitochondrial outer membrane localization; correct and specific. Supporting Evidence: PMID:16651524 an outer mitochondrial membrane enzyme |
| GO:0001676 long-chain fatty acid metabolic process | IDA PMID:11350182 Molecular and enzymatic characterization of a unique carniti... | ACCEPT | Summary: Direct-assay evidence of CPT1A's role in long-chain fatty acid metabolism, consistent with its substrate specificity for long-chain acyl-CoAs. Reason: Correct, specific process term supported by direct experimental characterization of the enzyme. Supporting Evidence: PMID:11350182 a rare disorder |
| GO:0004095 carnitine O-palmitoyltransferase activity | IDA PMID:11350182 Molecular and enzymatic characterization of a unique carniti... | ACCEPT | Summary: Direct kinetic characterization of CPT1A carnitine O-palmitoyltransferase activity (KM/Vmax for carnitine and palmitoyl-CoA), with the G710E variant shown to be catalytically inactive. Reason: Direct experimental support for the core catalytic function of CPT1A. Supporting Evidence: PMID:11350182 CPT1A is totally inactive |
| GO:0005739 mitochondrion | IDA PMID:11350182 Molecular and enzymatic characterization of a unique carniti... | KEEP AS NON CORE | Summary: Direct evidence that CPT1A localizes to the mitochondrion (mitochondrial targeting assessed for the G710E variant). Correct but less specific than the outer membrane. Reason: Supports mitochondrial localization; the informative compartment is the mitochondrial outer membrane (GO:0005741). Retained as non-core parent. Supporting Evidence: PMID:11350182 alters neither mitochondrial targeting nor stability of the CPT1A |
| GO:0005741 mitochondrial outer membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer (from rat Cpt1a, P32198) of the mitochondrial outer membrane localization, consistent with the human experimental data. Reason: Correct, specific compartment concordant with the human EXP/IMP annotations. Supporting Evidence: PMID:16651524 an outer mitochondrial membrane enzyme |
| GO:0009437 carnitine metabolic process | IDA PMID:11350182 Molecular and enzymatic characterization of a unique carniti... | ACCEPT | Summary: Direct-assay evidence for CPT1A's role in carnitine metabolism, consistent with its use of L-carnitine as the acyl acceptor. Reason: Correct process term supported by direct experimental characterization. Supporting Evidence: PMID:11350182 a rare disorder |
| GO:0004095 carnitine O-palmitoyltransferase activity | TAS PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I: ... | ACCEPT | Summary: Traceable-author-statement citing characterization of the human liver CPT I enzyme (EC 2.3.1.21). Reason: Supports the core carnitine O-palmitoyltransferase activity of CPT1A. Supporting Evidence: PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I |
| GO:0005739 mitochondrion | TAS PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I: ... | KEEP AS NON CORE | Summary: Traceable-author-statement for mitochondrial localization of the human liver CPT I. Correct but general. Reason: Supports mitochondrial localization at low specificity; outer membrane is the informative compartment. Retained as non-core parent. Supporting Evidence: PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I |
| GO:0006635 fatty acid beta-oxidation | TAS PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I: ... | ACCEPT | Summary: Traceable-author-statement placing human liver CPT I in mitochondrial fatty acid beta-oxidation, where it catalyzes the committed import step. Reason: Correct, central process term consistent with CPT1A biology and corroborated by IEA/ISS annotations. Supporting Evidence: PMID:7892212 Human liver mitochondrial carnitine palmitoyltransferase I |
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