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Literature summary for 3.4.24.82 extracted from
- Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4 (2010), J. Biol. Chem., 285, 5868-5877.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hevin + H2O | digestion of hevin by ADAMTS4 in vitro produces fragments similar to those present in brain lysates. The proteolysis liberates a hevin peptide, termed SPARC-like fragment, with significant homology to SPARC (secreted protein acidic and rich in cysteine) | Mus musculus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADAMTS4 | - |
Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the lack of hevin cleavage, as seen in ADAMTS4-null mice results in altered Purkinje-cell morphology and a reactive gliosis phenotype in the brain of these adult animals | Mus musculus |
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Release 2023.1 (January 2023)
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