PET100 encodes a small nuclear-encoded mitochondrial inner-membrane protein required for cytochrome c oxidase (respiratory complex IV) biogenesis. Pet100 acts after mitochondrial import as a complex IV assembly factor associated with a late assembly intermediate containing Cox7, Cox8, and Cox9, promoting productive incorporation of this module into the holoenzyme.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005743 mitochondrial inner membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inner-membrane localization is consistent with Pet100's experimentally supported site of complex IV assembly. Reason: Pet100 is an integral mitochondrial inner-membrane assembly factor and its conserved family context supports that localization. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002143768 · PTN002143768 SUPPORTS TRANSFER The current PTHR33968 PAINT file places mitochondrial inner membrane at this PET100-family node, seeded by yeast Pet100p and human PET100. Supporting Evidence: PMID:15507444 localized Pet100p to the inner mitochondrial membrane file:interpro/panther/PTHR33968/PTHR33968-metadata.yaml PROTEIN PET100 HOMOLOG, MITOCHONDRIAL |
| GO:0033617 mitochondrial respiratory chain complex IV assembly | IBA GO_REF:0000033 | ACCEPT | Summary: The family-based complex IV assembly annotation is strongly supported. Reason: Yeast Pet100 is experimentally required for cytochrome c oxidase assembly and the PANTHER family is specific to PET100 homologs. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002143768 · PTN002143768 SUPPORTS TRANSFER The current PTHR33968 PAINT file places mitochondrial respiratory chain complex IV assembly at this PET100-family node, seeded by yeast Pet100p itself. Supporting Evidence: PMID:11498004 required for the assembly of cytochrome c oxidase file:yeast/PET100/PET100-deep-research-falcon.md complex IV assembly factor/chaperone |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: The pinned GOA row carries a stale PAINT assertion to unfolded protein binding; current PTHR33968 no longer propagates GO:0051082, and Pet100 is better described as a COX-specific assembly factor. Reason: Current PAINT no longer places GO:0051082 at PTN002143768, replacing this old assertion with GO:0044183 protein folding chaperone. The underlying problem is the same: Pet100 facilitates incorporation of a specific Cox7/Cox8/Cox9 module into complex IV but is not shown to have a general unfolded-protein-binding or protein-folding activity. Keep the stale row as over-annotated rather than replacing it with another chaperone term; the core-function summary instead records the specific complex IV assembly process. Propagation Review Root cause: SOURCE STALE OR MISSING Failure modes: ROLE CONFLATION Sources checked: PANTHER:PTN002143768 · PTN002143768 SOURCE STALE OR MISSING The current PTHR33968 PAINT file contains GO:0044183 and GO:0051131 at this node, but no longer contains GO:0051082. Supporting Evidence: PMID:15507444 interaction with a subassembly that accumulates in a pet100 mutant |
| GO:0005739 mitochondrion | IEA GO_REF:0000002 | ACCEPT | Summary: Mitochondrial localization is correct for Pet100. Reason: Pet100 acts in mitochondrial complex IV assembly, with more precise inner-membrane annotations also present. Supporting Evidence: PMID:16823961 complete yeast mitochondrial proteome |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000044 | MODIFY | Summary: Mitochondrial membrane localization is correct but less precise than the experimentally supported inner membrane. Reason: Pet100 is an inner-membrane protein, so the broader mitochondrial membrane annotation should be replaced by the specific compartment. Proposed replacements: mitochondrial inner membrane Supporting Evidence: PMID:15507444 localized Pet100p to the inner mitochondrial membrane |
| GO:0033617 mitochondrial respiratory chain complex IV assembly | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro-derived complex IV assembly is correct. Reason: Experimental yeast studies show Pet100 is required for cytochrome c oxidase assembly and acts on a late complex IV subassembly. Supporting Evidence: PMID:15507444 A role for Pet100p in the assembly of yeast cytochrome c oxidase |
| GO:0005743 mitochondrial inner membrane | IDA PMID:15507444 A role for Pet100p in the assembly of yeast cytochrome c oxi... | ACCEPT | Summary: Direct inner-membrane localization is well supported. Reason: Pet100's membrane localization is required for its role in assembling membrane-embedded complex IV. Supporting Evidence: PMID:15507444 localized Pet100p to the inner mitochondrial membrane |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: High-throughput mitochondrial proteomics localization is consistent with Pet100 biology. Reason: Pet100 functions in mitochondrial respiratory-chain assembly; more precise inner-membrane annotations are available separately. Supporting Evidence: PMID:16823961 Toward the complete yeast mitochondrial proteome |
| GO:0005743 mitochondrial inner membrane | IDA PMID:11498004 Structure and function of Pet100p, a molecular chaperone req... | ACCEPT | Summary: Experimental work supports mitochondrial inner-membrane localization. Reason: Pet100 is a membrane-associated complex IV assembly factor and inner-membrane localization is consistent across the literature. Supporting Evidence: PMID:11498004 molecular chaperone required for the assembly of cytochrome c oxidase |
| GO:0033617 mitochondrial respiratory chain complex IV assembly | IMP PMID:11498004 Structure and function of Pet100p, a molecular chaperone req... | ACCEPT | Summary: Mutant evidence directly supports a requirement for complex IV assembly. Reason: Loss of PET100 causes failure to assemble functional cytochrome c oxidase and respiratory deficiency. Supporting Evidence: PMID:11498004 required for the assembly of cytochrome c oxidase |
| GO:0033617 mitochondrial respiratory chain complex IV assembly | IMP PMID:15507444 A role for Pet100p in the assembly of yeast cytochrome c oxi... | ACCEPT | Summary: Subassembly evidence directly supports Pet100's role in complex IV assembly. Reason: Pet100 interacts with a Cox7/Cox8/Cox9-containing assembly intermediate and promotes its productive use in holoenzyme assembly. Supporting Evidence: PMID:15507444 interaction with a subassembly that accumulates in a pet100 mutant |
| GO:0051082 unfolded protein binding | IDA PMID:11498004 Structure and function of Pet100p, a molecular chaperone req... | MARK AS OVER ANNOTATED | Summary: The experiment supports a COX-specific assembly-facilitator role rather than general unfolded protein binding. Reason: Pet100's supported activity is not general binding to unfolded proteins: it facilitates specific complex IV subassembly interactions. The generic and now-obsolete GO:0051082 term overstates that activity in the same way as the stale IBA row; the core-function summary instead records the specific complex IV assembly process. Supporting Evidence: PMID:15507444 Pet100p does not interact with the same subunits after they have been assembled into the holoenzyme |
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Download this section (compressed HTML)Q: What is the direct Pet100 binding interface on the Cox7/Cox8/Cox9 assembly module and on later complex IV intermediates?
Suggested experts: mitochondrial respiratory-chain assembly experts, structural biologists
Q: Does Pet100 function primarily as a scaffold for subassembly docking, a stabilizer of an otherwise unstable module, or both?
Suggested experts: yeast mitochondrial biochemists
Experiment: Map Pet100 contacts in wild-type and pet100 mutant-rescue strains during respiratory growth, focusing on Cox7, Cox8, Cox9, and later complex IV assembly intermediates.
Hypothesis: Pet100 makes specific contacts with the Cox7/Cox8/Cox9 module and a downstream complex IV intermediate, explaining its adaptor-like assembly role.
Type: crosslinking mass spectrometry
Experiment: Follow newly synthesized complex IV subunits after acute Pet100 depletion or allele replacement and quantify accumulation or loss of defined Cox7/Cox8/Cox9-containing intermediates.
Hypothesis: Pet100 loss blocks conversion of a late subassembly into holo-complex IV rather than causing a general mitochondrial protein-import defect.
Type: blue-native PAGE pulse-chase assembly assay
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Download this section (compressed HTML)Chaperone that facilitates the assembly of cytochrome c oxidase; integral to the mitochondrial inner membrane; interacts with a subcomplex of subunits VII, VIIa, and VIII (Cox7p, Cox9p, and Cox8p) but not with the holoenzyme
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