TFP1 curation notes

Family and PAINT

TFP1 encodes C. albicans Q5AJB1, a 617 aa V-type proton ATPase catalytic subunit
A. PANTHER places it in PTHR43607:SF1, "H(+)-TRANSPORTING TWO-SECTOR ATPASE",
alongside S. cerevisiae VMA1, S. pombe vma1, and N. crassa vma-1.

For PTHR43607, the IBA rows in the seeded review correspond to three PAINT node
assertions:

All three PAINT placements match Tfp1 biology. Tfp1 has no apparent
lineage-specific loss or retargeting relative to these nodes, and the C.
albicans experimental record is one of the fungal-node sources rather than a
circular defect.

Local and web literature check

just fetch-pmid 25220074 initially hit an NCBI 429 during seeding; I retried
it once and cached the PubMed record successfully. The publication is still
abstract-only locally (full_text_available: false), so exact YAML quotes from
Jia et al. 2014 are limited to the PubMed abstract rather than the full
ScienceDirect article. The abstract identifies Tfp1 as a putative V-ATPase
subunit and states that "Tfp1 played an essential role in vacuolar acidification
and endocytic trafficking" PMID:25220074.

I also searched for later TFP1-focused work and cached two abstract-only
follow-ups from the same group. Jia et al. 2015 found that TFP1 deletion
perturbed iron, copper, calcium, fluconazole, and GlcNAc physiology, including
"generation of an iron starvation signal and reduced total iron content" that
the authors connected to copper-dependent Fet34p mislocalization
PMID:26255859. Jia et al. 2018 used a tfp1 background to examine PMC1 and
reported that deleting the vacuolar calcium pump in the tfp1 mutant "led to
more severe dysregulation of calcium homeostasis" PMID:29086141.

Annotation decisions

The core retained activity is ATP hydrolysis by Tfp1 in the peripheral V1
sector, contributing to the V-ATPase holoenzyme's rotary proton-pumping activity
at the fungal vacuole membrane. I accepted the PAINT root/eukaryotic/fungal node
assertions because they place conserved functions at the right depth: rotary
proton pump contribution and proton transport are ancestral to PTHR43607, the V1
sector is eukaryotic, and fungal-type vacuole membrane is a fungal
specialization.

The generic GO:0033180 V-type ATPase V1-domain row should be refined to the
vacuolar V1 term GO:0000221, and the generic GO:0005774 vacuolar membrane
rows should be refined to GO:0000329. The InterPro GO:0046961 row shares the
same term as the accepted PAINT row and should be kept consistently; the PAINT
contributes_to row is the one that precisely scopes Tfp1 as the
ATP-hydrolyzing A subunit that contributes to the proton-transporting ATPase
activity of the complete V1-V0 pump.

The GO:0006897 endocytosis and GO:0034599 cellular response to oxidative
stress IMP rows from Jia et al. 2014 look phenotype-driven. Endocytosis was
marked over-annotated because the abstract supports it as a readout of failed
vacuolar/endosomal acidification rather than a direct V1 A-subunit process.
Cellular response to oxidative stress was kept as non-core because both CGD and
Swiss-Prot curate Tfp1-dependent oxidative-stress physiology from the full Jia
et al. paper, but this remains downstream of the core V-ATPase function.