Photomedin-1/OLFML2A is distinct from photomedin-2/OLFML2B and OLFM2. Mouse recombinant experiments establish secretion, disulfide-linked oligomerization, and binding to sulfated glycosaminoglycans. Human podocyte imaging supports a relevant glomerular protein pool. Matrix binding does not by itself demonstrate matrix assembly or a defined signaling receptor.
The selected horse model lacks the human1–27 signal-peptide region and an internal segment. Its olfactomedin domain is strongly conserved, but normal secretory entry and maturation are unresolved. Consequently extracellular localization, binding and organization are UNC for this exact model despite a reasonable extracellular family default.
The reproducible alignment, source paths and hashes are in the paired comparison. Current UniProt sequences have not been proven identical to the original ProtNLM input sequences. Sequence anomalies are therefore recorded as model/transfer limitations, not as proven wrong-input pipeline errors.
Check horse transcript starts and test secretory targeting. Trace the extracellular-matrix screen at gene/assay level before making a specific matrix-organization claim. Cancer-expression/knockdown associations in the Edison report are leads, not a demonstrated receptor mechanism.
Every seeded annotation receives a current assessment. UNDECIDED marks unresolved source-specific or biological evidence; these are initial reviews rather than a claim that every original experimental assay has been independently reproduced or verified. The human Edison report is retained as a research synthesis and source-finding aid; decisive YAML excerpts cite primary publications, source records or reproducible analysis. The validator advisory to cite the deep-research file is deliberately not satisfied by citing AI prose as biological proof.