IPT1
S. cerevisiae
inositolphosphotransferase
What the model saw
Gene: IPT1 Organism: Saccharomyces cerevisiae Known functions: inositolphosphotransferase. transferase activity, transferring phosphorus-containing groups.
View unredacted entry
inositolphosphotransferase. transferase activity, transferring phosphorus-containing groups.
Solver output
IPT1 encodes inositolphosphotransferase, the enzyme catalyzing the final step in the biosynthesis of mannose-(inositol-P)2-ceramide (M(IP)2C), the most abundant complex sphingolipid in S. cerevisiae. Complex sphingolipids, particularly M(IP)2C, are known to sequester and inhibit the TORC2-Ypk1 signaling axis and modulate membrane microdomain organization. Elevated M(IP)2C levels have been linked to reduced chronological lifespan, and deletion of IPT1 (which abolishes M(IP)2C synthesis) extends both chronological and replicative lifespan in yeast. This places IPT1's normal function in opposition to longevity, as its product promotes pro-aging sphingolipid signaling that intersects with TOR pathway regulation and ceramide-mediated stress responses. The phosphoinositol transfer activity of IPT1 thus feeds into a lipid-signaling network that dampens stress resistance and accelerates aging.
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 IPT1 as anti_longevity. The mechanistic reasoning is detailed and accurate: IPT1 encodes inositolphosphotransferase that catalyzes the final step in M(IP)2C (mannose-(inositol-P)2-ceramide) synthesis, the most abundant complex sphingolipid in yeast. The model correctly identifies that deletion of IPT1 extends lifespan by abolishing M(IP)2C synthesis, and correctly links this to TORC2-Ypk1 signaling and ceramide-mediated stress responses. The confidence level of 0.62 is appropriately calibrated for a less commonly discussed gene. Overall, this is an excellent prediction with solid mechanistic reasoning.
Raw API responses
solver
{
"reasoning": "IPT1 encodes inositolphosphotransferase, the enzyme catalyzing the final step in the biosynthesis of mannose-(inositol-P)2-ceramide (M(IP)2C), the most abundant complex sphingolipid in S. cerevisiae. Complex sphingolipids, particularly M(IP)2C, are known to sequester and inhibit the TORC2-Ypk1 signaling axis and modulate membrane microdomain organization. Elevated M(IP)2C levels have been linked to reduced chronological lifespan, and deletion of IPT1 (which abolishes M(IP)2C synthesis) extends both chronological and replicative lifespan in yeast. This places IPT1's normal function in opposition to longevity, as its product promotes pro-aging sphingolipid signaling that intersects with TOR pathway regulation and ceramide-mediated stress responses. The phosphoinositol transfer activity of IPT1 thus feeds into a lipid-signaling network that dampens stress resistance and accelerates aging.",
"confidence": 0.62,
"key_pathways": [
"sphingolipid biosynthesis (M(IP)2C synthesis)",
"TORC2-Ypk1 signaling",
"ceramide-mediated stress response"
],
"mechanism_class": "deregulated_nutrient_sensing",
"longevity_influence": "anti_longevity"
}advisor
{
"notes": "The model correctly predicted IPT1 as anti_longevity. The mechanistic reasoning is detailed and accurate: IPT1 encodes inositolphosphotransferase that catalyzes the final step in M(IP)2C (mannose-(inositol-P)2-ceramide) synthesis, the most abundant complex sphingolipid in yeast. The model correctly identifies that deletion of IPT1 extends lifespan by abolishing M(IP)2C synthesis, and correctly links this to TORC2-Ypk1 signaling and ceramide-mediated stress responses. The confidence level of 0.62 is appropriately calibrated for a less commonly discussed gene. 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
}