Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli XL1-Blue cells | Haliotis diversicolor supertexta |
PC1, DNA and amino acid sequence determination and analysis, phylogenetic tree | Haliotis diversicolor supertexta |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Haliotis diversicolor supertexta |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Haliotis diversicolor supertexta | the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haliotis diversicolor supertexta | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
digestive gland | - |
Haliotis diversicolor supertexta | - |
digestive gland | in the digestive gland the PC1 activity of pre-breeding stage is 1.17fold and 1.55fold as that of the during-breeding and the post-breeding stages, respectively | Haliotis diversicolor supertexta | - |
gonad | - |
Haliotis diversicolor supertexta | - |
gonad | relative activity of PC1 in gonad is 10% of that in the digestive gland. In male, the PC1 activity in digestive gland is slightly lower than in female | Haliotis diversicolor supertexta | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-pGlu-L-Arg-L-Thr-L-Lys-Arg-7-amido-4-methylcoumarin + H2O | - |
Haliotis diversicolor supertexta | L-pGlu-L-Arg-L-Thr-L-Lys-Arg + 7-amino-4-methylcoumarin | - |
? | |
additional information | the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97 | Haliotis diversicolor supertexta | ? | - |
? | |
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O | - |
Haliotis diversicolor supertexta | pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | also cf. EC 3.4.21.75. Prohormone convertases are calcium-dependent serine endoproteases of the subtilisin family | Haliotis diversicolor supertexta |
PC1 | - |
Haliotis diversicolor supertexta |
prohormone convertase 1 | - |
Haliotis diversicolor supertexta |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
asay at | Haliotis diversicolor supertexta |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Haliotis diversicolor supertexta |
Organism | Comment | Expression |
---|---|---|
Haliotis diversicolor supertexta | in female digestive gland the PC1 activity of pre-breeding stage is 1.17 and 1.55fold as that of the during-breeding and the post-breeding stages, respectively. The level of PC1 in male individual does not exhibit a significant difference in various reproduction stages | up |
General Information | Comment | Organism |
---|---|---|
evolution | PC members are paralogous genes derived from a common ancestor, which represents independent lineages by gene replication in evolution. Abalone PC1 is located in PC1 clade which is orthologous genes in different species. The potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97 | Haliotis diversicolor supertexta |
physiological function | PC1 is a potential prohormone processing enzyme and plays a critical role in abalone physiological processes related to reproduction | Haliotis diversicolor supertexta |
physiological function | the enzyme plays a key role in the posttranslational processing of precursors for bioactive peptides | Haliotis diversicolor supertexta |