TFP1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain	IBA GO_REF:0000033	ACCEPT	Summary: Accept the PAINT placement of Tfp1 in the vacuolar V-ATPase V1 domain. Reason: PTN000389802 is the eukaryotic PTHR43607 node for membership in the vacuolar proton-transporting V-type ATPase V1 domain. Tfp1 is an intact fungal V-ATPase catalytic subunit A in this clade, and Jia et al. identify it as a putative C. albicans V-ATPase subunit required for vacuolar acidification, so the inherited V1-domain membership is biologically appropriate. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000389802 SUPPORTS TRANSFER Eukaryotic PAINT node for V-ATPase V1-domain membership; the PTHR43607 review places C. albicans Tfp1 inside this inherited clade. Supporting Evidence: PMID:25220074 In this study, we identified C. albicans Tfp1 as a putative subunit of V-ATPase, and explored its importance in multiple cellular processes.
GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain	ISS GO_REF:0000024	ACCEPT	Summary: Accept orthology-based V1-domain membership. Reason: The vacuolar V-ATPase V1-domain claim is consistent with the PAINT eukaryotic node and with experimental characterization of C. albicans Tfp1 as a V-ATPase subunit required for vacuolar acidification. The row should be retained, but the UniProt ISS donor P16140 is the S. cerevisiae VMA2/subunit B record rather than the VMA1/subunit A ortholog P17255. Supporting Evidence: PMID:25220074 In this study, we identified C. albicans Tfp1 as a putative subunit of V-ATPase, and explored its importance in multiple cellular processes.
GO:0000329 fungal-type vacuole membrane	IBA GO_REF:0000033	ACCEPT	Summary: Accept the fungal PAINT placement at the vacuolar membrane. Reason: PTN001032540 is the fungal PTHR43607 node for activity at the fungal-type vacuole membrane, seeded by the C. albicans and S. cerevisiae VMA1/TFP1 annotations. The target's own experimental localization is part of the PAINT support, and there is no evidence for loss or retargeting in Tfp1. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001032540 SUPPORTS TRANSFER Fungal PAINT node for fungal-type vacuole membrane activity, seeded by CGD and SGD V-ATPase A-subunit annotations. Supporting Evidence: PMID:25220074
GO:0000329 fungal-type vacuole membrane	IDA PMID:25220074 Role of TFP1 in vacuolar acidification, oxidative stress and...	ACCEPT	Summary: Accept the direct CGD localization to the fungal-type vacuole membrane. Reason: The cached record for Jia et al. is abstract-only, but CGD curated this localization from the full text and both PAINT and electronic annotations independently place Tfp1 at the fungal vacuolar membrane. Supporting Evidence: PMID:25220074
GO:0000329 fungal-type vacuole membrane	IEA GO_REF:0000117	ACCEPT	Summary: Accept the ARBA fungal-type vacuole membrane localization. Reason: The fungal-type vacuole membrane is the specific compartment supported by the C. albicans IDA row and by the PAINT fungal node, so the ARBA electronic localization is consistent with the reviewed biology of Tfp1.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: Accept ATP binding as a domain-supported activity of the V-ATPase A subunit. Reason: Tfp1 carries the conserved F1/V1/A1 alpha/beta nucleotide-binding and active-site signatures expected for a V1 A subunit, so ATP binding is a valid molecular function even though ATP hydrolysis and contribution to the V-ATPase proton pump are more informative.
GO:0005774 vacuolar membrane	IEA GO_REF:0000044	MODIFY	Summary: Refine the generic vacuolar membrane term to fungal-type vacuole membrane. Reason: Vacuolar membrane is true but the fungal-type vacuole membrane is a more precise descendant that is already supported directly and by the fungal PAINT node for this C. albicans protein. Proposed replacements: fungal-type vacuole membrane
GO:0005774 vacuolar membrane	ISS GO_REF:0000024	MODIFY	Summary: Refine the orthology-based vacuolar membrane annotation to the fungal-type vacuole membrane. Reason: The transfer from S. cerevisiae Vma1 is directionally correct, but Tfp1 acts at the fungal-type vacuole membrane; replacing GO:0005774 with GO:0000329 captures the organism-specific compartment already present in the CGD and PAINT rows. Proposed replacements: fungal-type vacuole membrane
GO:0005829 cytosol	IDA PMID:25220074 Role of TFP1 in vacuolar acidification, oxidative stress and...	KEEP AS NON CORE	Summary: Keep the cytosol localization as a non-core distribution of the peripheral V1 subunit. Reason: CGD curated cytosolic Tfp1 from the Jia et al. full text, but the productive V-ATPase activity reviewed here occurs when the V1 sector is assembled on the vacuolar membrane, not as free cytosolic subunit. Supporting Evidence: PMID:25220074
GO:0006897 endocytosis	IMP PMID:25220074 Role of TFP1 in vacuolar acidification, oxidative stress and...	MARK AS OVER ANNOTATED	Summary: Mark endocytosis as a phenotype-derived over-annotation. Reason: The abstract reports that Tfp1 is essential for endocytic trafficking, but this follows from loss of V-ATPase-dependent organelle acidification rather than evidence that the V1 A subunit performs a trafficking step. Vacuolar acidification is the direct process to retain for Tfp1. Supporting Evidence: PMID:25220074 Our results revealed that Tfp1 played an essential role in vacuolar acidification and endocytic trafficking.
GO:0007035 vacuolar acidification	IEA GO_REF:0000117	ACCEPT	Summary: Accept ARBA-inferred involvement in vacuolar acidification. Reason: Vacuolar acidification is the immediate biological outcome of the V-ATPase proton pump in the fungal vacuole, and the same process is directly supported by the C. albicans tfp1 mutant phenotype in Jia et al. Supporting Evidence: PMID:25220074 Our results revealed that Tfp1 played an essential role in vacuolar acidification and endocytic trafficking.
GO:0007035 vacuolar acidification	IMP PMID:25220074 Role of TFP1 in vacuolar acidification, oxidative stress and...	ACCEPT	Summary: Accept the TFP1 mutant evidence for vacuolar acidification. Reason: Tfp1 is the V1 catalytic A subunit; loss of this subunit directly compromises vacuolar proton pumping, and Jia et al. report that Tfp1 is essential for vacuolar acidification. Supporting Evidence: PMID:25220074 Our results revealed that Tfp1 played an essential role in vacuolar acidification and endocytic trafficking.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000002	ACCEPT	Summary: Accept ATP hydrolysis activity for the catalytic A subunit. Reason: InterPro identifies Tfp1 as a V-ATPase V1-complex A subunit, the catalytic ATP-hydrolyzing subunit that powers the rotary proton pump. This term captures the subunit's direct enzymatic activity without assigning the complete proton-pumping activity to isolated Tfp1.
GO:0033180 proton-transporting V-type ATPase, V1 domain	IEA GO_REF:0000002	MODIFY	Summary: Refine the generic V1-domain annotation to the vacuolar V-ATPase V1 domain. Reason: The InterPro V1 A-subunit signature correctly places Tfp1 in a proton-transporting V-type ATPase V1 domain, but the fungal protein is specifically part of the vacuolar proton-transporting V-type ATPase V1 domain already asserted by PAINT. Proposed replacements: vacuolar proton-transporting V-type ATPase, V1 domain
GO:0034599 cellular response to oxidative stress	IMP PMID:25220074 Role of TFP1 in vacuolar acidification, oxidative stress and...	KEEP AS NON CORE	Summary: Keep the oxidative-stress response term as a downstream non-core phenotype. Reason: TFP1 deletion perturbs ROS levels and Cap1 expression after peroxide treatment, and both CGD and UniProt curate an oxidative-stress response from Jia et al. Tfp1's core activity is V-ATPase ATP hydrolysis and vacuolar acidification, but the oxidative-stress row is still a curator-supported downstream cellular response rather than an over-propagated claim. Supporting Evidence: PMID:25220074 Western blotting analysis showed that deletion of TFP1 significantly reduced the expression of Cap1 under H2O2 treatment, which contributes to the regulation of genes involved in the oxidative stress response.
GO:0046034 ATP metabolic process	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: Mark the ATP metabolic-process annotation as an over-general consequence of ATPase domain detection. Reason: Tfp1 hydrolyzes ATP as part of V-ATPase proton pumping, but the BP term ATP metabolic process adds only a generic consequence of ATPase chemistry. ATP hydrolysis activity and vacuolar proton transport describe the core function more directly.
GO:0046961 proton-transporting ATPase activity, rotational mechanism	IBA GO_REF:0000033	ACCEPT	Summary: Accept the family-root PAINT assertion that Tfp1 contributes to rotary proton-transporting ATPase activity. Reason: PTN000389800 is the PTHR43607 family-root node for rotary proton-transporting ATPase activity. Tfp1 is a conserved V1 A subunit that hydrolyzes ATP in the V-ATPase complex, so the contributes_to qualifier accurately scopes its role in the holoenzyme activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000389800 SUPPORTS TRANSFER PTHR43607 root node for the conserved rotary proton-transporting ATPase activity of A/V-type ATPase catalytic subunit A proteins. Supporting Evidence: PMID:25220074 The vacuolar-type H(+)-ATPase (V-ATPase) is a multiprotein complex consisting of the V0 and V1 sectors, and is required for vacuolar acidification and virulence in the opportunistic fungal pathogen Candida albicans.
GO:0046961 proton-transporting ATPase activity, rotational mechanism	IEA GO_REF:0000002	ACCEPT	Summary: Accept InterPro-inferred proton-transporting ATPase activity as corroborating the PAINT term. Reason: InterPro correctly recognizes a V1 A subunit in the rotary proton pump family. The PAINT row captures the exact contributes_to qualifier for this term, while the InterPro row corroborates that Tfp1 is part of the V-ATPase machinery that couples ATP hydrolysis to proton transport.
GO:1902600 proton transmembrane transport	IBA GO_REF:0000033	ACCEPT	Summary: Accept the family-root PAINT assertion for proton transmembrane transport. Reason: The PTHR43607 root node PTN000389800 carries both the rotary proton-ATPase activity and the coupled proton transmembrane transport BP, and Tfp1 is a conserved catalytic subunit of this proton-pumping complex. Its direct C. albicans mutant phenotype in vacuolar acidification supports retention of the inherited transport process. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000389800 SUPPORTS TRANSFER PTHR43607 root node for the conserved proton transmembrane transport driven by A/V-type ATPase rotary pumps. Supporting Evidence: PMID:25220074 The vacuolar-type H(+)-ATPase (V-ATPase) is a multiprotein complex consisting of the V0 and V1 sectors, and is required for vacuolar acidification and virulence in the opportunistic fungal pathogen Candida albicans.
GO:1902600 proton transmembrane transport	IEA GO_REF:0000002	ACCEPT	Summary: Accept InterPro-inferred proton transmembrane transport. Reason: The V1 A subunit provides the ATP hydrolysis that drives the V-ATPase rotary proton pump. The broad proton transmembrane transport term is therefore valid for Tfp1 and is independently supported by the family-root PAINT assertion.

Gene Description

Existing Annotations Review

Core Functions

Hydrolyzes ATP in the peripheral V1 sector of the fungal vacuolar V-ATPase to drive rotary proton translocation and acidify the vacuole.

References

📚 Additional Documentation

Notes

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