AFAP1L2

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The primary human airway-cell experiment reports reduced IL-6 after XB130 siRNA. Conservation of the signaling adaptor supports this general regulatory participation; it does not establish identical effect size or expression across horse tissues. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human XB130 enhances Src-dependent SRE/AP-1 transcription. This supports conserved upstream positive regulation, without implying that AFAP1L2 is a DNA-binding transcription factor. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. XB130 knockdown alters human epithelial cell-cycle progression downstream of growth-factor signaling. This supports a conserved regulatory contribution, not intrinsic cell-cycle catalysis. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human protein activates Src and depletion reduces endogenous Src activity. Conserved adaptor architecture supports kinase-activator activity rather than kinase activity. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human airway-cell knockdown lowers IL-8 production. The horse inference concerns a conserved signaling contribution to cytokine output and remains tissue/context dependent. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human N-terminal motif-rich region supports SH2-mediated interaction and Src signaling. Retention of the human-length sequence and adaptor architecture supports transfer, rather than assigning an SH2 domain to AFAP1L2. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. The human N-terminal SH3-binding region mediates signaling interactions. This molecular binding role is consistent with the conserved horse adaptor. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Primary human cytokine-response experiments establish a contribution to inflammatory signaling. This is a broad, context-dependent biological process, not a claim of universal proinflammatory action. The claim is new relative to the frozen horse GOA; the model training membership is unknown.

Review rationale: The selected horse AFAP1L2 aligns across all 818 human residues with 88.6% identity among paired positions and retains its AFAP-family architecture. Human depletion reduces EGF-induced Akt/GSK3beta phosphorylation, supporting a conserved positive contribution to EGFR downstream signaling through the adaptor. The claim is new relative to the frozen horse GOA; the model training membership is unknown.