OLFML2A (photomedin-1) is a secreted olfactomedin-domain glycoprotein associated with the extracellular matrix. Characterized mammalian photomedin-1 binds the glycosaminoglycans chondroitin sulfate E and heparin and forms disulfide-linked homodimers. Its extracellular interactions are better established than a specific role in matrix assembly or a defined signaling pathway.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: OLFML2A is a secreted extracellular protein. Reason: The mouse photomedin-1 secretion experiments support the manual ortholog transfer and the corresponding localization mapping. The PAINT extracellular-location inference agrees with the experimentally characterized family property. Supporting Evidence: PMID:15836428 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 PMID:15836428 We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins file:human/OLFML2A/OLFML2A-uniprot.txt DE AltName: Full=Photomedin-1; |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: OLFML2A is a secreted extracellular protein. Reason: The mouse photomedin-1 secretion experiments support the manual ortholog transfer and the corresponding localization mapping. The PAINT extracellular-location inference agrees with the experimentally characterized family property. Supporting Evidence: PMID:15836428 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 PMID:15836428 We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins file:human/OLFML2A/OLFML2A-uniprot.txt DE AltName: Full=Photomedin-1; |
| GO:0005576 extracellular region | ISS GO_REF:0000024 | ACCEPT | Summary: OLFML2A is a secreted extracellular protein. Reason: The mouse photomedin-1 secretion experiments support the manual ortholog transfer and the corresponding localization mapping. The PAINT extracellular-location inference agrees with the experimentally characterized family property. Supporting Evidence: PMID:15836428 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 PMID:15836428 We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins file:human/OLFML2A/OLFML2A-uniprot.txt DE AltName: Full=Photomedin-1; |
| GO:0007165 signal transduction | IBA GO_REF:0000033 | UNDECIDED | Summary: A specific signaling function for OLFML2A is not resolved by the photomedin experiments. Reason: The IBA represents a phylogenetic placement of signaling function, not a weak donor-count inference. The available OLFML2A-specific experiments demonstrate secretion, dimerization and glycosaminoglycan binding but do not establish the signaling mechanism inherited at this node. These data do not refute the IBA; retain uncertainty pending evidence connecting OLFML2A to that ancestral signaling role. Supporting Evidence: PMID:15836428 Among a panel of ECM components, including glycosaminoglycans, photomedins preferentially bound to chondroitin sulphate-E and heparin. PMID:15836428 We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | ACCEPT | Summary: Photomedin-1 associates with extracellular matrix components. Reason: The experimentally characterized mouse ortholog binds sulfated glycosaminoglycans and is found extracellularly in tissue. This supports ECM association and the electronic ortholog transfer, without inferring matrix structural activity. Supporting Evidence: PMID:15836428 Among a panel of ECM components, including glycosaminoglycans, photomedins preferentially bound to chondroitin sulphate-E and heparin. PMID:15836428 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 |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Photomedin-1 forms disulfide-linked homodimers. Reason: The mouse biochemical experiments directly distinguish dimeric photomedin-1 from multimeric photomedin-2. Conserved self-association supports this ortholog transfer, but it describes assembly state rather than the principal extracellular binding activity. Supporting Evidence: PMID:15836428 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 file:human/OLFML2A/OLFML2A-uniprot.txt DE AltName: Full=Photomedin-1; |
| GO:0050840 extracellular matrix binding | IEA GO_REF:0000107 | ACCEPT | Summary: Photomedin-1 binds extracellular glycosaminoglycans. Reason: The original mouse study tested a panel of ECM substrates and detected preferential binding to chondroitin sulfate E and heparin. This biochemical function supports transfer to human OLFML2A; it does not establish a matrix-assembly role. Supporting Evidence: PMID:15836428 Among a panel of ECM components, including glycosaminoglycans, photomedins preferentially bound to chondroitin sulphate-E and heparin. PMID:15836428 We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins |
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