PXA2 (also PAT1) encodes one of the two peroxisomal ABC half-transporters of S. cerevisiae. Pxa1p and Pxa2p are the two half ATP-binding-cassette transporters of the ABCD (ALDP/PMP70) family in the S. cerevisiae peroxisomal membrane; they heterodimerise to form a full transporter that imports long-chain and very long-chain acyl groups from the cytosolic acyl-CoA pool into the peroxisome, the only site of fatty acid beta-oxidation in yeast. The complex hydrolyses the acyl-CoA during transport and translocates the fatty acid moiety, which is re-esterified to CoA on the luminal side by the acyl-CoA synthetases Faa2p and/or Fat1p; medium-chain fatty acids instead enter as free acids and are activated by Faa2p. pxa mutants fail to oxidise oleate and other long-chain fatty acids and grow poorly on oleate, but have normal peroxisomes. The pxa1 pxa2 defect is partly complemented by human ABCD1 or ABCD2 acting as homodimers. Pxa1p-Pxa2p also mediates unidirectional ATP uptake into peroxisomes, alongside the Ant1p and Aac2p nucleotide carriers. The C-terminal region of Pxa2p is required for its interaction with Pxa1p.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005324 long-chain fatty acid transmembrane transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for long-chain fatty acid transmembrane transporter activity (ABCD1/ABCD2 clade, yeast PXA1/PXA2 among sources). Consistent with the mechanism in which the Pxa1p-Pxa2p complex hydrolyses (very) long-chain acyl-CoA and translocates the fatty acid moiety. Supporting Evidence: PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes PMID:8670886 long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via Pat1p and Pat2p, peroxisomal membrane proteins belonging to the ATP binding cassette transporter superfamily. |
| GO:0005324 long-chain fatty acid transmembrane transporter activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (IPR005283, ABCD family) mapping to long-chain fatty acid transmembrane transporter activity. Correct for the yeast heterodimer. Supporting Evidence: PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes |
| GO:0005324 long-chain fatty acid transmembrane transporter activity | IGI PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | ACCEPT | Summary: The pxa1/pxa2 deletion phenotype is partially rescued by human ABCD1 (with/from), and the yeast heterodimer handles a spectrum of acyl-CoA esters. Supports long-chain fatty acyl import; whether the translocated species is acyl-CoA or free fatty acid was later resolved in favour of hydrolysis followed by fatty acid transport (PMID:22493507). Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. PMID:18757502 the mutant phenotype of the pxa1/pxa2Delta mutant can be rescued, at least partially, by the sole expression of the human ABCD1 cDNA PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes |
| GO:0005515 protein binding | IPI PMID:23831759 Mapping the functional yeast ABC transporter interactome. | REMOVE | Summary: Membrane yeast two-hybrid (MYTH) interactome screen of yeast ABC transporters reported PXA2p interactions with unrelated soluble proteins (e.g. Arf1p and others). 'Protein binding' is uninformative and these high-throughput hits have no established functional significance for the transporter. Reason: Uninformative 'protein binding' from a high-throughput MYTH screen with no functional follow-up; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:23831759 Mapping the functional yeast ABC transporter interactome. | REMOVE | Summary: Membrane yeast two-hybrid (MYTH) interactome screen of yeast ABC transporters reported PXA2p interactions with unrelated soluble proteins (e.g. Arf1p and others). 'Protein binding' is uninformative and these high-throughput hits have no established functional significance for the transporter. Reason: Uninformative 'protein binding' from a high-throughput MYTH screen with no functional follow-up; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:23831759 Mapping the functional yeast ABC transporter interactome. | REMOVE | Summary: Membrane yeast two-hybrid (MYTH) interactome screen of yeast ABC transporters reported PXA2p interactions with unrelated soluble proteins (e.g. Arf1p and others). 'Protein binding' is uninformative and these high-throughput hits have no established functional significance for the transporter. Reason: Uninformative 'protein binding' from a high-throughput MYTH screen with no functional follow-up; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:23831759 Mapping the functional yeast ABC transporter interactome. | REMOVE | Summary: Membrane yeast two-hybrid (MYTH) interactome screen of yeast ABC transporters reported PXA2p interactions with unrelated soluble proteins (e.g. Arf1p and others). 'Protein binding' is uninformative and these high-throughput hits have no established functional significance for the transporter. Reason: Uninformative 'protein binding' from a high-throughput MYTH screen with no functional follow-up; removal does not imply the interaction is false. |
| GO:0005515 protein binding | IPI PMID:8876235 A Saccharomyces cerevisiae homolog of the human adrenoleukod... | MODIFY | Summary: Co-immunoprecipitation of Pxa1p with Pxa2p: the two half-transporters form the functional heterodimeric ABC transporter. The interaction is real and important, but is better represented by membership of the ABC transporter complex (GO:0043190, also annotated) than by 'protein binding'. Reason: Biologically meaningful heterodimerisation with PXA1; 'protein binding' itself is uninformative, and the complex annotation captures it. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:8876235 Finally, we find that Pxa1p and Pxa2p coimmuno-precipitate. PMID:8876235 These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. |
| GO:0005524 ATP binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT IBA for ATP binding by the nucleotide-binding domain. Correct, but part of the transporter's ATPase cycle rather than a separate function. Reason: Implicit in ATP-driven transport. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt Belongs to the ABC transporter superfamily. ABCD family. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro2GO (ABC transporter-like/ABCD) mapping to ATP binding. Correct but implicit in transporter activity. Reason: Implicit in ATP-driven transport. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt Belongs to the ABC transporter superfamily. ABCD family. |
| GO:0005777 peroxisome | IDA PMID:27663510 Characterization of proteome dynamics during growth in oleat... | ACCEPT | Summary: High-content localisation screens during oleate growth visualised GFP-Pxa2 in peroxisomes. Supporting Evidence: PMID:27663510 the constitutively expressed GFP-Pxa2 could be visualized in peroxisomes in both conditions |
| GO:0005777 peroxisome | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA/InterPro) mapping to peroxisome. Correct; the more specific peroxisomal membrane is also annotated. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. |
| GO:0005778 peroxisomal membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for peroxisomal-membrane activity of the ABCD family. Correct; Pxa2p is an integral peroxisomal-membrane half-transporter. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. PMID:8670886 long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via Pat1p and Pat2p, peroxisomal membrane proteins belonging to the ATP binding cassette transporter superfamily. |
| GO:0005778 peroxisomal membrane | IDA PMID:35127709 Peroxisomal ATP Uptake Is Provided by Two Adenine Nucleotide... | ACCEPT | Summary: Peroxisomal-membrane proteoliposome and reporter experiments place Pxa1p/Pxa2p activity in the peroxisomal membrane. Supporting Evidence: PMID:35127709 the ABC transporter protein complex Pxa1p/Pxa2p, which mediates both uni-directional acyl-CoA and ATP uptake |
| GO:0005778 peroxisomal membrane | IDA PMID:9395310 Transport of activated fatty acids by the peroxisomal ATP-bi... | ACCEPT | Summary: Semi-intact cell assays show Pxa2p-dependent import of C18:1-CoA into peroxisomes, consistent with Pxa2p in the peroxisomal membrane. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. |
| GO:0005778 peroxisomal membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping to peroxisomal membrane. Correct. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. |
| GO:0005778 peroxisomal membrane | NAS PMID:22493507 Peroxisomal fatty acid uptake mechanism in Saccharomyces cer... | ACCEPT | Summary: Statement in van Roermund et al. 2012 about the Pxa1p-Pxa2p complex in the peroxisomal membrane. Correct and corroborated by experimental data. Supporting Evidence: PMID:22493507 The Pxa1p-Pxa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner surface of the peroxisomal membrane file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. |
| GO:0006635 fatty acid beta-oxidation | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for fatty acid beta-oxidation. The transporter delivers long-chain acyl substrates into the peroxisome, the exclusive site of beta-oxidation in yeast; pxa mutants are deficient in oleate oxidation. Accepted as the pathway the transport step serves. Supporting Evidence: PMID:8876235 These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. PMID:21145416 the phenotype of the pxa1/pxa2Ξ yeast mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, cannot only be partially rescued by human ABCD1, but also by human ABCD2 (ALDRP) |
| GO:0006635 fatty acid beta-oxidation | IGI PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | ACCEPT | Summary: Genetic interaction data (with FAA2 and the partner half-transporter) linking Pxa1p/Pxa2p-mediated uptake to peroxisomal beta-oxidation of long-chain substrates. Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. |
| GO:0007031 peroxisome organization | IBA GO_REF:0000033 | REMOVE | Summary: PAINT IBA for peroxisome organization, seeded from human ABCD1/ABCD3. For yeast, Shani & Valle showed Pxa1p and Pxa2p are associated with peroxisomes but not required for their assembly; the transporter acts on substrate import, not organelle biogenesis. Reason: Contradicted for the yeast proteins: neither PXA1 nor PXA2 is required for peroxisome assembly. Over-propagation from mammalian ABCD members. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: UniProtKB:P28288 Β· ABCD3 (PMP70), human SUPPORTS SOURCE BUT NOT TARGET Mammalian ABCD source; the yeast Pxa1p/Pxa2p half-transporters are not required for peroxisome assembly (PMID:8876235). UniProtKB:P33897 Β· ABCD1 (ALDP), human SUPPORTS SOURCE BUT NOT TARGET Mammalian ABCD source; organelle-biogenesis role not transferable to the yeast heterodimer. Supporting Evidence: PMID:8876235 is associated with peroxisomes but not required for their assembly. |
| GO:0015867 ATP transport | IDA PMID:35127709 Peroxisomal ATP Uptake Is Provided by Two Adenine Nucleotide... | KEEP AS NON CORE | Summary: van Roermund et al. 2022 found that, besides Ant1p and Aac2p, the Pxa1p/Pxa2p complex mediates unidirectional ATP uptake into peroxisomes (proteoliposome assays and peroxisomal ATP sensors). A genuine but secondary activity relative to acyl-CoA import. Reason: Experimentally supported secondary transport activity; acyl import is the primary function. Supporting Evidence: PMID:35127709 These findings pointed to a novel, unanticipated role for the ABC transporter protein complex Pxa1p/Pxa2p in peroxisomal ATP uptake in addition to its established role in the peroxisomal import of fatty acyl-CoAs. |
| GO:0015910 long-chain fatty acid import into peroxisome | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for long-chain fatty acid import into peroxisome. This is the core process of Pxa1p-Pxa2p. Supporting Evidence: PMID:8670886 long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via Pat1p and Pat2p, peroxisomal membrane proteins belonging to the ATP binding cassette transporter superfamily. PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes |
| GO:0015910 long-chain fatty acid import into peroxisome | IDA PMID:25118695 Involvement of the carboxyl-terminal region of the yeast per... | ACCEPT | Summary: Chuang et al. showed that the Pxa2p C-terminal region mediates interaction with Pxa1p and is required for transporter function, assayed by growth on oleate. Supports the role of the heterodimer in long-chain fatty acid import. Supporting Evidence: PMID:25118695 The oleate plate functional assay clearly demonstrated that the CT2 of Pxa2p is required for transporter function, suggesting that the interactions identified here are functionally related. |
| GO:0015910 long-chain fatty acid import into peroxisome | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO (ABCD family) mapping to long-chain fatty acid import into peroxisome. Correct. Supporting Evidence: PMID:8670886 long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via Pat1p and Pat2p, peroxisomal membrane proteins belonging to the ATP binding cassette transporter superfamily. |
| GO:0015910 long-chain fatty acid import into peroxisome | IGI PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | ACCEPT | Summary: Rescue of pxa1/pxa2 deletion by human ABCD1 supports the conserved role in import of long-chain acyl groups into peroxisomes. Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. PMID:18757502 the mutant phenotype of the pxa1/pxa2Delta mutant can be rescued, at least partially, by the sole expression of the human ABCD1 cDNA |
| GO:0015916 fatty-acyl-CoA transport | IGI PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | KEEP AS NON CORE | Summary: van Roermund et al. 2008 concluded that the heterodimer transports acyl-CoA esters. The same group later showed the acyl-CoA is hydrolysed by the complex and only the fatty acid moiety is translocated, so 'fatty-acyl-CoA transport' describes the substrate taken up from the cytosol but not the translocated species. Reason: Accurately reflects acyl-CoA as the cytosolic substrate, but the mechanistic picture (PMID:22493507) favours fatty acid translocation; the core process is GO:0015910. Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes |
| GO:0016020 membrane | IEA GO_REF:0000120 | TOO GENERAL | Summary: Generic 'membrane' from combined IEA. Correct but uninformative; the specific location is the peroxisomal membrane. Reason: Generic ancestor of GO:0005778. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro2GO (ABC transporter-like) mapping to ATP hydrolysis activity. The NBDs hydrolyse ATP to drive transport; this is a component of the transporter activity rather than a stand-alone function. Reason: Part of the ATPase-coupled transport mechanism. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. |
| GO:0042626 ATPase-coupled transmembrane transporter activity | IBA GO_REF:0000033 | TOO GENERAL | Summary: PAINT IBA for ATPase-coupled transmembrane transporter activity of ABCD transporters. Correct but generic; PXA2, as half of the Pxa1p-Pxa2p heterodimer, mediates ATP-dependent import of long-chain acyl groups. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. PMID:8876235 These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. |
| GO:0042626 ATPase-coupled transmembrane transporter activity | IDA PMID:35127709 Peroxisomal ATP Uptake Is Provided by Two Adenine Nucleotide... | TOO GENERAL | Summary: ATP-dependent transport by Pxa1p/Pxa2p shown in proteoliposomes from peroxisomal membranes. Correct, if generic. Supporting Evidence: PMID:35127709 the ABC transporter protein complex Pxa1p/Pxa2p, which mediates both uni-directional acyl-CoA and ATP uptake |
| GO:0042626 ATPase-coupled transmembrane transporter activity | IDA PMID:9395310 Transport of activated fatty acids by the peroxisomal ATP-bi... | TOO GENERAL | Summary: In digitonin-permeabilised cells C18:1-CoA enters peroxisomes via Pxa2p in an ATP-dependent manner: direct support for ATP-coupled transport. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. |
| GO:0042626 ATPase-coupled transmembrane transporter activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO (ABCD family) mapping to ATPase-coupled transmembrane transporter activity. Correct but generic. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. |
| GO:0042758 long-chain fatty acid catabolic process | IMP PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | ACCEPT | Summary: pxa mutants are deficient in oxidation of long-chain fatty acids such as oleate. The transporter supplies substrate to peroxisomal beta-oxidation. Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. PMID:21145416 the phenotype of the pxa1/pxa2Ξ yeast mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, cannot only be partially rescued by human ABCD1, but also by human ABCD2 (ALDRP) |
| GO:0042760 very long-chain fatty acid catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for very long-chain fatty acid catabolic process (ABCD1/ABCD2 clade). Consistent with Pxa1p-Pxa2p handling very long-chain acyl-CoA esters. Supporting Evidence: PMID:22493507 very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes |
| GO:0042760 very long-chain fatty acid catabolic process | IGI PMID:21145416 Differential substrate specificities of human ABCD1 and ABCD... | ACCEPT | Summary: Very long-chain fatty acid oxidation in the pxa1/pxa2 double mutant depends on Pxa1p-Pxa2p and is restored by human ABCD1/ABCD2 (with/from: PXA1). Supporting Evidence: PMID:21145416 the phenotype of the pxa1/pxa2Ξ yeast mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, cannot only be partially rescued by human ABCD1, but also by human ABCD2 (ALDRP) PMID:21145416 full rescue of beta-oxidation activity in cells expressing human ABCD2 was observed with C22:0 and different unsaturated very long-chain fatty acids including C24:6 and especially C22:6 whereas in cells expressing HsABCD1 rescue of beta-oxidation activity was best with C24:0 and C26:0 as substrates. |
| GO:0042760 very long-chain fatty acid catabolic process | IMP PMID:18757502 The human peroxisomal ABC half transporter ALDP functions as... | ACCEPT | Summary: pxa mutants have defective handling of very long-chain acyl-CoAs; consistent with the ABCD-family role in VLCFA delivery to peroxisomal beta-oxidation. Supporting Evidence: PMID:18757502 we show that the Pxa1p/Pxa2p heterodimer is involved in the transport of a spectrum of acyl-CoA esters. |
| GO:0043190 ATP-binding cassette (ABC) transporter complex | IPI PMID:25118695 Involvement of the carboxyl-terminal region of the yeast per... | ACCEPT | Summary: Two-hybrid mapping of the Pxa1p-Pxa2p interaction (Pxa2p C-terminus required) supports Pxa1p and Pxa2p forming a heterodimeric ABC transporter complex. Supporting Evidence: PMID:25118695 Using a yeast two-hybrid assay, we found that the carboxyl-terminal region (CT) of Pxa2p, but not of Pxa1p, is required for their interaction. PMID:8876235 These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. |
| GO:0055085 transmembrane transport | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO (ABC transmembrane domain) mapping to generic transmembrane transport. Correct but uninformative; the specific process is long-chain fatty acid import into peroxisome. Reason: Generic ancestor of GO:0015910. Supporting Evidence: PMID:8670886 long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via Pat1p and Pat2p, peroxisomal membrane proteins belonging to the ATP binding cassette transporter superfamily. |
| GO:0140359 ABC-type transporter activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO mapping to ABC-type transporter activity. Correct description of the transporter class. Supporting Evidence: file:yeast/PXA2/PXA2-uniprot.txt Belongs to the ABC transporter superfamily. ABCD family. PMID:8876235 These genetic and physical data suggest that Pxa1p and Pxa2p heterodimerize to form a complete peroxisomal ABC transporter involved in fatty acid beta-oxidation. |
| GO:1902001 fatty acid transmembrane transport | IDA PMID:9395310 Transport of activated fatty acids by the peroxisomal ATP-bi... | ACCEPT | Summary: Pxa2p-dependent, ATP-dependent uptake of long-chain (C18:1) but not medium-chain acyl-CoA into peroxisomes. Correct; GO:0015910 is the more specific peroxisomal term. Supporting Evidence: PMID:9395310 we show that C18:1-CoA, but not C8:0-CoA, enters the peroxisome via Pxa2p, in an ATP-dependent fashion. |
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Download this section (compressed HTML)Q: Is the acyl-CoA thioesterase step intrinsic to the Pxa1p-Pxa2p transporter (as in PMID:22493507), and should GO describe the activity as fatty-acyl-CoA transport (GO:0015607) or as fatty acid transport coupled to acyl-CoA hydrolysis?
Experiment: Reconstitute purified Pxa1p-Pxa2p in proteoliposomes with labelled acyl-CoA (CoA and acyl moieties separately labelled) to determine which moiety is translocated and whether ATP hydrolysis is coupled to thioester cleavage.
Subunit of heterodimeric peroxisomal ABC transport complex, with Pxa1p; required for import of long-chain fatty acids into peroxisomes; similar to human adrenoleukodystrophy transportesr ABCD1 and ABCD2, and ALD-related proteins; mutations in ABCD1 cause X-linked adrenoleukodystrophy (X-ALD), a peroxisomal disorder; human ABCD1 and ABCD2 can each partially complement yeast pxa1 pxa2 double null mutant
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