Finding: Supported conserved deubiquitinase function.
Target: A0A9L0T7K6, Equus caballus. The exact source is the frozen ProtNLM API response dated 2026-09-08, retained in projects/PROTNLM_EVALUATION/mammal-benchmark/predictions.jsonl.gz.
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes
Supported. Recombinant and immunoprecipitated human UBPY/USP8 cleave linear and isopeptide-linked ubiquitin chains (PMID:9628861). The selected horse protein retains the USP8 catalytic architecture with 91.82% paired sequence identity across 99.46% of the human reference.
Supported at this broad level. Human studies connect USP8 to endosomal sorting, EGFR trafficking and substrate stability. This broad wording does not assert a particular horse-specific substrate or disease phenotype.
Existing horse GOA already includes cysteine-type deubiquitinase activity and protein deubiquitination. Deubiquitination can participate in ubiquitin-dependent catabolism by controlling cargo sorting; a deubiquitinase label alone does not refute the accompanying catabolic-process GO prediction. Training membership is unknown.
The reproducible paired sequence comparison records residue-level findings and sequence hashes. The human UniProt source distinguishes experimental supporting papers from inferred statements. ARBA assertions and generated review prose are not used as validating evidence.