CTR1
S. cerevisiae
high-affinity Cu transporter CTR1
What the model saw
Gene: CTR1 Organism: Saccharomyces cerevisiae Known functions: high-affinity Cu transporter CTR1. copper ion transmembrane transporter activity.
View unredacted entry
high-affinity Cu transporter CTR1. copper ion transmembrane transporter activity.
Solver output
CTR1 encodes the high-affinity copper importer in S. cerevisiae, responsible for uptake of Cu(I) across the plasma membrane. Copper is an essential cofactor for cytochrome c oxidase (Complex IV of the mitochondrial electron transport chain) and for Cu/Zn superoxide dismutase (Sod1), both of which are critical for mitochondrial respiration and antioxidant defense. Loss of CTR1 leads to copper deficiency, impairing Complex IV assembly and reducing respiratory capacity, as well as diminishing Sod1 activity and increasing oxidative stress. Adequate copper import via CTR1 is therefore necessary to maintain mitochondrial function and proteostasis under oxidative conditions. Because copper sufficiency supports both respiratory efficiency and ROS detoxification, CTR1's normal function is expected to promote longevity rather than oppose it.
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 pro_longevity for CTR1 in S. cerevisiae. The mechanistic reasoning is sound: CTR1 imports copper needed for cytochrome c oxidase (Complex IV) and Cu/Zn SOD (Sod1), so loss of CTR1 impairs mitochondrial respiration and antioxidant defense. The mechanism_class of "mitochondrial_dysfunction" is a reasonable categorization, though the antioxidant/ROS defense angle is equally important. The reasoning is well-articulated and biologically accurate. Confidence of 0.62 is appropriately moderate given the indirect nature of the evidence.
Raw API responses
solver
{
"reasoning": "CTR1 encodes the high-affinity copper importer in S. cerevisiae, responsible for uptake of Cu(I) across the plasma membrane. Copper is an essential cofactor for cytochrome c oxidase (Complex IV of the mitochondrial electron transport chain) and for Cu/Zn superoxide dismutase (Sod1), both of which are critical for mitochondrial respiration and antioxidant defense. Loss of CTR1 leads to copper deficiency, impairing Complex IV assembly and reducing respiratory capacity, as well as diminishing Sod1 activity and increasing oxidative stress. Adequate copper import via CTR1 is therefore necessary to maintain mitochondrial function and proteostasis under oxidative conditions. Because copper sufficiency supports both respiratory efficiency and ROS detoxification, CTR1's normal function is expected to promote longevity rather than oppose it.",
"confidence": 0.62,
"key_pathways": [
"mitochondrial electron transport chain (cytochrome c oxidase/Complex IV)",
"Cu/Zn superoxide dismutase (Sod1) antioxidant defense",
"copper ion homeostasis and transmembrane transport"
],
"mechanism_class": "mitochondrial_dysfunction",
"longevity_influence": "pro_longevity"
}advisor
{
"notes": "The model correctly predicted pro_longevity for CTR1 in S. cerevisiae. The mechanistic reasoning is sound: CTR1 imports copper needed for cytochrome c oxidase (Complex IV) and Cu/Zn SOD (Sod1), so loss of CTR1 impairs mitochondrial respiration and antioxidant defense. The mechanism_class of \"mitochondrial_dysfunction\" is a reasonable categorization, though the antioxidant/ROS defense angle is equally important. The reasoning is well-articulated and biologically accurate. Confidence of 0.62 is appropriately moderate given the indirect nature of the evidence.",
"failure_mode": "correct",
"answer_correct": true,
"mechanism_correct": true,
"reasoning_quality": 4,
"ground_truth_questionable": false
}