Selected accession A0A9L0T4W6; 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 1996 cloning report states that recombinant IAR/PTPRN2 has phosphatase activity, but its abstract does not name the substrate. Later human cell work explicitly distinguishes lack of phosphoprotein-substrate activity from phosphoinositide phosphatase activity and tests the effect of a catalytic-domain mutant on migration and metastasis. Vesicle accumulation, insulin/neurotransmitter release, and membrane phosphoinositide regulation are not interchangeable with protein tyrosine dephosphorylation. Conversely, a biological-process annotation can describe regulation through another enzyme: losing intrinsic protein phosphatase activity alone does not refute all participation in protein dephosphorylation. The exact experimental annotation therefore remains unresolved while the inappropriate electronic intrinsic protein-phosphatase terms can be challenged.
Sources: PMID:8798755(https://pubmed.ncbi.nlm.nih.gov/8798755/), PMID:26620550(https://pubmed.ncbi.nlm.nih.gov/26620550/).