OLFML2A

Review rationale: Secretion, ECM residence, glycosaminoglycan binding and self-association are supported by mouse photomedin experiments and conserved horse sequence. These properties make a role in ECM organization plausible but do not demonstrate creation, rearrangement or disassembly of matrix, so a perturbation or reconstitution result linking OLFML2A to matrix organization is still needed. The OpenScientist report resolved the missing signal peptide as a caveat on the selected N-terminally truncated accession, not evidence for loss of secretion by the horse OLFML2A locus.

Review rationale: Mouse photomedin-1 experiments support disulfide-linked homodimerization. The selected horse protein retains strong OLFML2A family similarity, and the OpenScientist report resolved its missing signal peptide as a caveat on this N-terminally truncated product rather than a loss from the horse locus. Because A0A9L0SKW1 itself still lacks the leader, secretory maturation and access to extracellular homodimerization partners remain unresolved for this exact model.

Review rationale: Mouse photomedin-1 experiments support extracellular-matrix association. The OpenScientist report resolved the missing signal peptide at the locus level by identifying secretion-competent horse OLFML2A isoforms, but the selected A0A9L0SKW1 accession remains N-terminally truncated and should carry an accession-specific secretion caveat. GO:0031012 is therefore plausible by ISS/ISO for the locus while unresolved for direct assignment to this exact protein product.

Review rationale: Mouse photomedin-1 experiments support binding to sulfated extracellular glycosaminoglycans, and conserved horse OLFML2A isoforms can plausibly reach extracellular partners. The OpenScientist report resolved the signal-peptide gap as specific to the selected N-terminally truncated accession rather than to the locus, but that leaves access to extracellular binding partners unresolved for the A0A9L0SKW1 product itself.