Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
TreeGrafter-generated GO annotations
Identification and characterization of photomedins: novel olfactomedin-domain-containing proteins with chondroitin sulphate-E-binding activity.
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Full-length mouse photomedin-1 (OLFML2A) has tandem N-terminal CXCXCX9C motifs, a coiled coil and a C-terminal olfactomedin domain. It is secreted as a disulfide-bonded dimer and binds chondroitin sulfate E and heparin.
"characterized by the presence of tandem CXCXCX9C motifs in the N-terminal region, a coiled-coil domain and an olfactomedin domain in the C-terminal region"
A0A8C9H4D2 gene-model comparison against human OLFML2A and the same-gene full-length product
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A0A8C9H4D2 is the counterpart of human isoform 3 (Q68BL7-3) and matches it over its full length (97.3% identity). It lacks the region equivalent to human residues 1-222, which contains the signal peptide, both CXCXCX9C motifs and the coiled coil. The full-length product of the same gene is A0A8C9H9A8 (655 aa).
"A0A8C9H4D2 (XP_023072933.1, isoform X2) is the short alternative-first-exon isoform of Piliocolobus OLFML2A, the counterpart of human isoform 3."
UniProt record A0A8C9H4D2
Falcon deep research for A0A8C9H4D2 (OLFML2A)