Function and Biology Details
Reaction catalysed:
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152975 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Disintegrin and metalloproteinase domain-containing protein 17
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 28.95 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
Sequence domains: Metallo-peptidase family M12B Reprolysin-like
Structure domains: Collagenase (Catalytic Domain)
Length: 256 amino acids
Theoretical weight: 28.95 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
- Canonical:
P78536 (Residues: 219-474; Coverage: 32%)
Sequence domains: Metallo-peptidase family M12B Reprolysin-like
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 3
Molecule details ›
Chain: B
Length: 121 amino acids
Theoretical weight: 13.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 121 amino acids
Theoretical weight: 13.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P35625 (Residues: 24-144; Coverage: 64%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
