Cloned (Comment) | Organism |
---|---|
determination of polyadenylation of endogenous furin transcripts | Xenopus laevis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | furin antisense expression leading to furin depletionin oocytes is accompanied by a corresponding decrease in the levels of both the fully cleaved prodomain and mature BMP4 | Xenopus laevis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
alpha1-AT | a naturally occurring serpin and a potent inhibitor of furin | Xenopus laevis | |
alpha1-PDX | a furin- and PC6-selective inhibitor, blocks cleavage of furin minimal consensus motifs, and of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase | Xenopus laevis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-BMP4 + H2O | Xenopus laevis | pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4 | BMP4 + propeptide of BMP4 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xenopus laevis | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | - |
Xenopus laevis | - |
oocyte | - |
Xenopus laevis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-BMP4 + H2O | pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4 | Xenopus laevis | BMP4 + propeptide of BMP4 | - |
? | |
pro-BMP4 + H2O | i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin | Xenopus laevis | BMP4 + propeptide of BMP4 | - |
? |
General Information | Comment | Organism |
---|---|---|
additional information | alpha1-PDX blocks cleavage of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase, probably PC7, overview | Xenopus laevis |
physiological function | bone morphogenetic proteins, BMPs, require proteolytic activation by members of the proprotein convertase family | Xenopus laevis |