| Post Translational Modifications | N-glycosylated. Proteolytic cleavage produces a CUB-containing C-terminal fragment that retains the ability to bind to TGFBR2. This reaction is catalyzed in vitro by MMP2 and, to a lesser extent, by MMP9. |
| Function | Is a positive regulator of the BMP signaling pathway, required for proper chondrogenesis, osteogenesis and skeletal development. It acts as a coreceptor for BMP ligands, particularly BMP2 and BMP4, facilitating their interactions with BMP type I receptors. It is required for ligand-induced recruitment of BMP receptors to lipid rafts. Binds to TGFBR2 and activates TGFB signaling. In lung cancer cells, could serve as an endogenous autocrine and paracrine ligand of TGFBR2, which could regulate TGFBR2 signaling and hence modulate epithelial-mesenchymal transition and cancer progression. |
| Protein Name | Signal Peptide - Cub And Egf-Like Domain-Containing Protein 3 |
| Database Links | Reactome: R-HSA-1474228 |
| Cellular Localisation | SecretedCell Surface |
| Alternative Protein Names | Signal Peptide - Cub And Egf-Like Domain-Containing Protein 3 proteinSCUBE3 proteinCEGF3 protein |
Information sourced from Uniprot.org
