Selected accession A0A9L0SQG9; ordinary UniProt record is TrEMBL and cites genome sequencing/submission rather than a gene-specific functional experiment. Human evidence is summarized in the paired human investigation. Sequence comparison records the exact target gaps and transfer limits. The targeted Europe PMC search found no decisive gene-specific horse functional assay warranting a separate horse Edison investigation; general omics/association hits were not counted as mechanistic validation.
The heme-containing membrane oxidase/dehydrogenase machinery transfers reducing equivalents from NADPH through FAD and hemes to oxygen. The extracellular peroxidase-like domain is a different structural region. Direct biochemical work finds that the isolated human peroxidase-like domain lacks heme binding and intrinsic peroxidase activity; the C. elegans homolog behaves differently. The human NOT-peroxidase annotation is therefore supported, without negating the heme required by the membrane oxidase. High- and low-calcium structures of DUOX1–DUOXA1 establish EF-hand-dependent conformational regulation. The selected horse deletion removes major elements of that regulatory region, making exact-sequence transfer much less secure than ordinary family identification. Hormone synthesis requires coupling peroxide production to separate peroxidases and the appropriate tissue context.
Sources: PMID:19460756(https://pubmed.ncbi.nlm.nih.gov/19460756/), PMID:33420071(https://pubmed.ncbi.nlm.nih.gov/33420071/), PMID:25761904(https://pubmed.ncbi.nlm.nih.gov/25761904/).