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alpha-Man-Ia

D. melanogaster

alpha-Mannosidase class I a

What the model saw

Gene: alpha-Man-Ia
Organism: Drosophila melanogaster
Known functions: alpha-Mannosidase class I a. calcium ion binding. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity.
View unredacted entry
alpha-Mannosidase class I a. calcium ion binding. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity.

Solver output

Predicted influence
Pro-longevity
Confidence
62%
Mechanism
Loss of proteostasis
Reasoning

alpha-Man-Ia encodes a class I alpha-mannosidase that catalyzes the trimming of mannose residues from N-linked oligosaccharides (Man9GlcNAc2 → Man5-8GlcNAc2) in the endoplasmic reticulum. This trimming step is essential for proper N-glycan maturation and is a prerequisite for glycoprotein quality control: misfolded glycoproteins that fail to achieve native structure are targeted for ER-associated degradation (ERAD) via mannose trimming signals recognized by OS-9/XTP3-B lectins. By facilitating correct N-glycosylation processing and ERAD-mediated clearance of misfolded proteins, alpha-Man-Ia supports proteostasis. Loss of this activity would impair glycoprotein folding fidelity and ERAD efficiency, leading to accumulation of aberrant proteins — a hallmark of aging. Calcium ion binding is consistent with the known calcium dependence of class I mannosidases, supporting catalytic function in the ER lumen.

Key pathways
N-glycan processing / ER quality controlER-associated degradation (ERAD)Unfolded protein response (UPR)
Longevity influence
Anti-longevity
Lifespan effect
Increase

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

Answer
Incorrect
Mechanism
Incorrect
Reasoning quality
3/5
Failure mode
Confident wrong
Notes

The model predicted pro_longevity but the ground truth is anti_longevity. The model's reasoning about alpha-Man-Ia's role in N-glycan processing and ERAD is biochemically plausible and well-articulated, but it led to the wrong conclusion. The model assumed that supporting proteostasis via ERAD would make this gene pro-longevity, but in reality alpha-Man-Ia is anti-longevity in Drosophila. This could mean that loss of alpha-Man-Ia actually extends lifespan (making it anti-longevity), perhaps because excessive ERAD or mannose trimming is detrimental, or because the gene promotes aging through some other mechanism. The mechanistic reasoning, while coherent, does not align with the actual experimental outcome. The confidence of 0.62 is moderate but still wrong.

Raw API responses

solver

{
  "reasoning": "alpha-Man-Ia encodes a class I alpha-mannosidase that catalyzes the trimming of mannose residues from N-linked oligosaccharides (Man9GlcNAc2 → Man5-8GlcNAc2) in the endoplasmic reticulum. This trimming step is essential for proper N-glycan maturation and is a prerequisite for glycoprotein quality control: misfolded glycoproteins that fail to achieve native structure are targeted for ER-associated degradation (ERAD) via mannose trimming signals recognized by OS-9/XTP3-B lectins. By facilitating correct N-glycosylation processing and ERAD-mediated clearance of misfolded proteins, alpha-Man-Ia supports proteostasis. Loss of this activity would impair glycoprotein folding fidelity and ERAD efficiency, leading to accumulation of aberrant proteins — a hallmark of aging. Calcium ion binding is consistent with the known calcium dependence of class I mannosidases, supporting catalytic function in the ER lumen.",
  "confidence": 0.62,
  "key_pathways": [
    "N-glycan processing / ER quality control",
    "ER-associated degradation (ERAD)",
    "Unfolded protein response (UPR)"
  ],
  "mechanism_class": "loss_of_proteostasis",
  "longevity_influence": "pro_longevity"
}

advisor

{
  "notes": "The model predicted pro_longevity but the ground truth is anti_longevity. The model's reasoning about alpha-Man-Ia's role in N-glycan processing and ERAD is biochemically plausible and well-articulated, but it led to the wrong conclusion. The model assumed that supporting proteostasis via ERAD would make this gene pro-longevity, but in reality alpha-Man-Ia is anti-longevity in Drosophila. This could mean that loss of alpha-Man-Ia actually extends lifespan (making it anti-longevity), perhaps because excessive ERAD or mannose trimming is detrimental, or because the gene promotes aging through some other mechanism. The mechanistic reasoning, while coherent, does not align with the actual experimental outcome. The confidence of 0.62 is moderate but still wrong.",
  "failure_mode": "confident_wrong",
  "answer_correct": false,
  "mechanism_correct": false,
  "reasoning_quality": 3,
  "ground_truth_questionable": false
}