pept-1
C. elegans
Peptide transporter family 1
What the model saw
Gene: pept-1 Organism: Caenorhabditis elegans Known functions: Peptide transporter family 1. dipeptide transmembrane transporter activity. oligopeptide transmembrane transporter activity. transmembrane transporter activity.
View unredacted entry
Peptide transporter family 1. dipeptide transmembrane transporter activity. oligopeptide transmembrane transporter activity. transmembrane transporter activity.
Solver output
PEPT-1 is the major intestinal di/oligopeptide transporter in C. elegans (homolog of mammalian PepT1/SLC15A1), responsible for absorbing dietary peptides derived from protein digestion. By facilitating nutrient uptake, PEPT-1 activity feeds into amino acid and nitrogen sensing pathways, including TOR (Target of Rapamycin) signaling. Elevated TOR activity driven by amino acid availability is a well-established pro-aging signal in C. elegans. Consistent with this, loss-of-function mutations in pept-1 have been shown to extend lifespan in C. elegans, likely by reducing amino acid/peptide import and thereby dampening TOR-mediated nutrient sensing. Thus, the normal (wild-type) function of PEPT-1 — promoting peptide absorption — acts to sustain nutrient signaling that opposes longevity.
GenAge curators classify each gene's normal function as promoting (Pro-Longevity) or opposing (Anti-Longevity) longevity, based on synthesis across studies. Loss-of-function effects can vary from this depending on the manipulation.
Advisor judgment
The model correctly predicted anti_longevity for pept-1 in C. elegans. The mechanistic reasoning is well-grounded: PEPT-1 is the intestinal di/oligopeptide transporter, and its loss-of-function extends lifespan, likely through reduced nutrient/amino acid import dampening TOR signaling. The model correctly identifies the dietary restriction mimicry angle and TOR pathway involvement. Confidence of 0.72 is appropriate given the specificity of the claim. Overall, this is an excellent prediction with solid mechanistic reasoning.
Raw API responses
solver
{
"reasoning": "PEPT-1 is the major intestinal di/oligopeptide transporter in C. elegans (homolog of mammalian PepT1/SLC15A1), responsible for absorbing dietary peptides derived from protein digestion. By facilitating nutrient uptake, PEPT-1 activity feeds into amino acid and nitrogen sensing pathways, including TOR (Target of Rapamycin) signaling. Elevated TOR activity driven by amino acid availability is a well-established pro-aging signal in C. elegans. Consistent with this, loss-of-function mutations in pept-1 have been shown to extend lifespan in C. elegans, likely by reducing amino acid/peptide import and thereby dampening TOR-mediated nutrient sensing. Thus, the normal (wild-type) function of PEPT-1 — promoting peptide absorption — acts to sustain nutrient signaling that opposes longevity.",
"confidence": 0.72,
"key_pathways": [
"TOR (Target of Rapamycin) nutrient sensing",
"intestinal peptide/amino acid absorption",
"dietary restriction mimicry"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted anti_longevity for pept-1 in C. elegans. The mechanistic reasoning is well-grounded: PEPT-1 is the intestinal di/oligopeptide transporter, and its loss-of-function extends lifespan, likely through reduced nutrient/amino acid import dampening TOR signaling. The model correctly identifies the dietary restriction mimicry angle and TOR pathway involvement. Confidence of 0.72 is appropriate given the specificity of the claim. Overall, this is an excellent prediction with solid mechanistic reasoning.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 5,
"ground_truth_questionable": false
}