Literature summary extracted from
Hata, S.; Abe, M.; Suzuki, H.; Kitamura, F.; Toyama-Sorimachi, N.; Abe, K.; Sakimura, K.; Sorimachi, H.
Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense (2010), PLoS Genet., 6, e1001040.
Protein Variants
| EC Number |
Protein Variants |
Comment |
Organism |
|---|
| 3.4.22.B28 |
additional information |
generation of Capn8-/- mice, that are fertile and whose gastric mucosae appears normal. However, the mutant mice are susceptible to gastric mucosal injury induced by ethanol administration, and the Capn8-/- stomach shows significant decreases in both calpains 9 and 8, and the same was true for Capn9-/-. Effects of calpain 8 deficiency on mucous granule formation and secretion, overview |
Mus musculus |
Localization
| EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
|---|
| 3.4.22.B28 |
cytosol |
- |
Mus musculus |
5829 |
- |
Metals/Ions
| EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
|---|
| 3.4.22.B28 |
Ca2+ |
dependent on |
Mus musculus |
|
Natural Substrates/ Products (Substrates)
| EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
|---|
| 3.4.22.B28 |
additional information |
Mus musculus |
calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, in which both molecules are essential for activity, and that is involved in gastric mucosal defense. Calpains 8 and 9 are regulated differently from each other and from conventional calpains and, thus, have potentially important, specific functions in the gastrointestinal tract. Calpains 8 and 9 are molecular chaperones for each other, overview |
? |
- |
? |
|
Organism
| EC Number |
Organism |
UniProt |
Comment |
Textmining |
|---|
| 3.4.22.B28 |
Mus musculus |
Q91VA3 |
- |
- |
Source Tissue
| EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
|---|
| 3.4.22.B28 |
mucosa |
gastric |
Mus musculus |
- |
| 3.4.22.B28 |
stomach |
calpain 8/nCL-2 is predominantly expressed in the gastrointestinal tract and is restricted to the gastric surface mucus cells in the stomach |
Mus musculus |
- |
Substrates and Products (Substrate)
| EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
|---|
| 3.4.22.B28 |
additional information |
calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, in which both molecules are essential for activity, and that is involved in gastric mucosal defense. Calpains 8 and 9 are regulated differently from each other and from conventional calpains and, thus, have potentially important, specific functions in the gastrointestinal tract. Calpains 8 and 9 are molecular chaperones for each other, overview |
Mus musculus |
? |
- |
? |
|
Subunits
| EC Number |
Subunits |
Comment |
Organism |
|---|
| 3.4.22.B28 |
additional information |
enzyme domain structure with prodomain, protease domain, C2-like domain, and 5EF-hand domain |
Mus musculus |
Synonyms
| EC Number |
Synonyms |
Comment |
Organism |
|---|
| 3.4.22.B28 |
calpain 8/nCL-2 |
- |
Mus musculus |
| 3.4.22.B28 |
additional information |
calpains constitute a superfamily of Ca2+-dependent cysteine proteases |
Mus musculus |
General Information
| EC Number |
General Information |
Comment |
Organism |
|---|
| 3.4.22.B28 |
physiological function |
calpain 8 is involved in vesicle trafficking between endoplasmic reticulum and Golgi. Calpain 8/nCL-2 is also involved in the mucosal defense against stress-induced gastropathies |
Mus musculus |