OLFML2A

Review rationale: The primate target and mouse photomedin-1 (Olfml2a; Q8BHP7) share the OLFML2A PANTHER subfamily PTHR23192:SF29. Mouse photomedin-1 was experimentally secreted as a disulfide-bonded dimer; the photomedins bound chondroitin sulphate-E and heparin, supporting association with extracellular glycosaminoglycans (PMID:15836428). This supports an inferred matrix-associated location for the OLFML2A gene product rather than transferring a generic olfactomedin-domain property. The 439-residue primate record lacks an annotated signal peptide, so secretion of that deposited sequence is not demonstrated; the assignment relies on conserved ortholog biology, not on an observed targeting signal in this record. Matrix association is absent from the cached target annotations, making COR appropriate for this explicitly inferred localization. Matrix organization is assessed separately using the mouse experimental process annotation.

Review rationale: Mouse photomedin-1 (Olfml2a; Q8BHP7) has an MGI IDA annotation to extracellular matrix organization, with the relation acts_upstream_of_or_within. The QuickGO record identifies PMID:18757743 as its source: a study that includes functional ECM-assembly assays. This is distinct from the secretion and glycosaminoglycan-binding evidence in PMID:15836428. The experimentally grounded curated process annotation, together with the matching OLFML2A PANTHER subfamily PTHR23192:SF29, supports transfer of a broad involvement in matrix organization to the primate gene product. COR denotes this ortholog-based inference, not a demonstrated matrix-remodeling mechanism or an assay of the deposited 439-residue sequence. The process is absent from the cached target annotations.