Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of P3H2-null mice, the mutants are embryonic-lethal by embryonic day 8.5. The mechanism of the unexpectedly early lethality involves the interaction of non-3-hydroxylated embryonic type IV collagen with the maternal platelet-specific glycoprotein VI (GPVI). This interaction results in maternal platelet aggregation, thrombosis of the maternal blood, and death of the embryo. The phenotype is completely rescued by producing double KOs of P3H2 and GPVI. Double nulls are viable and fertile. Epigenetic silencing of P3H2 in breast cancers implies that the interaction between GPVI and nonย3-hydroxylated type IV collagen might also play a role in the progression of malignant tumors and metastasis | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[procollagen]-L-proline + 2-oxoglutarate + O2 | Mus musculus | type IV collagen | [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q8CG71 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[procollagen]-L-proline + 2-oxoglutarate + O2 | type IV collagen | Mus musculus | [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Leprel1 | - |
Mus musculus |
P3H2 | - |
Mus musculus |
prolyl 3-hydroxylase-2 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | P3H2-null mice are embryonic-lethal by embryonic day 8.5. The mechanism of the unexpectedly early lethality involves the interaction of non-3-hydroxylated embryonic type IV collagen with the maternal platelet-specific glycoprotein VI (GPVI). This interaction results in maternal platelet aggregation, thrombosis of the maternal blood, and death of the embryo. The phenotype is completely rescued by producing double knockouts of P3H2 and GPVI. Double nulls are viable and fertile. Epigenetic silencing of P3H2 in breast cancers implies that the interaction between GPVI and nonย3-hydroxylated type IV collagen might also play a role in the progression of malignant tumors and metastasis | Mus musculus |
physiological function | role of prolyl 3-hydroxylation in type IV collagen. Subendothelial collagens bear platelet-specific glycoprotein VI, GPVI, binding sites that initiate platelet aggregation upon blood exposure during injuries. In type IV collagen, these sites are normally 3-hydroxylated. Prolyl 3-hydroxylation of type IV collagen has an important function preventing maternal platelet aggregation in response to the early developing embryo. 3-Hydroxylation of type IV collagen is indispensable for embryonic development in mice | Mus musculus |