id: A0A9L0SKW1 gene_symbol: OLFML2A taxon: id: NCBITaxon:9796 label: Equus caballus status: COMPLETE description: The conserved photomedin family supports extracellular glycosaminoglycan binding and dimerization, but the selected horse model lacks the canonical signal-peptide segment. All four sequence-specific predictions remain unresolved; matrix organization additionally lacks direct mechanistic support. source_documents: - projects/PROTNLM_EVALUATION/mammal-benchmark/horse40-predictions.csv - projects/PROTNLM_EVALUATION/mammal-benchmark/predictions.jsonl.gz - projects/PROTNLM_EVALUATION/mammal-benchmark/paired-sequences/OLFML2A.json - genes/HORSE/OLFML2A/OLFML2A-hypotheses/horse40-extracellular-matrix-localization/openscientist.md references: - id: PMID:15836428 title: 'Identification and characterization of photomedins: novel olfactomedin-domain-containing proteins with chondroitin sulphate-E-binding activity.' full_text_unavailable: true findings: [] - id: file:HORSE/OLFML2A/OLFML2A-uniprot.txt title: HORSE/OLFML2A/OLFML2A-uniprot.txt findings: [] - id: file:HORSE/OLFML2A/OLFML2A-bioinformatics/RESULTS.md title: HORSE/OLFML2A/OLFML2A-bioinformatics/RESULTS.md findings: [] - id: file:human/OLFML2A/OLFML2A-uniprot.txt title: human/OLFML2A/OLFML2A-uniprot.txt findings: [] - id: file:HORSE/OLFML2A/OLFML2A-hypotheses/horse40-extracellular-matrix-localization/openscientist.md title: 'OpenScientist hypothesis run: OLFML2A extracellular matrix localization' publication_type: DEEP_RESEARCH reference_review: relevance: HIGH review_notes: Substantive computational synthesis directly addressing the selected horse accession's missing signal peptide and the extracellular-matrix localization prediction. The photomedin-family identity is independently corroborated by cached PANTHER and sequence-comparison evidence, but the live Ensembl/RefSeq isoform-resolution claims should be treated as curator-verification leads. findings: - statement: OpenScientist reported that the selected A0A9L0SKW1 accession is an N-terminally truncated product and that the horse OLFML2A locus has secretion-competent isoforms. supporting_text: Isoform resolution shows this is one **alternative product** of the locus predictions: - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0030198 label: extracellular matrix organization predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: 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. supported_by: - &id006 reference_id: PMID:15836428 supporting_text: 'Among a panel of ECM components, including glycosaminoglycans, photomedins preferentially bound to chondroitin sulphate-E and heparin.' - &id001 reference_id: PMID:15836428 supporting_text: 'These proteins, named photomedin-1 and photomedin-2, were secreted as disulphide-bonded dimers (photomedin-1) or oligomers/multimers (photomedin-2) with O-linked carbohydrate chains' - &id002 reference_id: file:HORSE/OLFML2A/OLFML2A-uniprot.txt supporting_text: DR PANTHER; PTHR23192:SF29; OLFACTOMEDIN-LIKE PROTEIN 2A; 1. - &id003 reference_id: file:HORSE/OLFML2A/OLFML2A-bioinformatics/RESULTS.md supporting_text: share 91.3% identity among 598 paired residues. - &id004 reference_id: file:HORSE/OLFML2A/OLFML2A-bioinformatics/RESULTS.md supporting_text: Human UniProt annotates residues 1–27 as the signal peptide; the horse sequence starts `MDSQVFGDMDQVRMTSEGSDCRCKCIMRPLSKDA`, without the hydrophobic human leader. - &id005 reference_id: file:human/OLFML2A/OLFML2A-uniprot.txt supporting_text: FT SIGNAL 1..27 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0042802 label: identical protein binding predicted_term_type: GO_MF review: assessment: UNC confidence_score: 1 summary: 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. supported_by: - *id001 - reference_id: file:human/OLFML2A/OLFML2A-uniprot.txt supporting_text: 'DE AltName: Full=Photomedin-1;' - *id002 - *id003 - *id004 - *id005 - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0031012 label: extracellular matrix predicted_term_type: GO_CC review: assessment: UNC confidence_score: 1 summary: 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. supported_by: - *id001 - *id006 - &id007 reference_id: PMID:15836428 supporting_text: 'We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins' - *id002 - *id003 - *id004 - *id005 - reference_id: file:HORSE/OLFML2A/OLFML2A-hypotheses/horse40-extracellular-matrix-localization/openscientist.md supporting_text: GO:0031012 is defensible as an ISS/ISO annotation with the signal-peptide-truncation caveat noted - source_method: ProtNLM2 source_version: UniProt API snapshot 2026-09-08 predicted_term: id: GO:0050840 label: extracellular matrix binding predicted_term_type: GO_MF review: assessment: UNC confidence_score: 1 summary: 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. supported_by: - *id006 - *id007 - *id002 - *id003 - *id004 - *id005