Function and Biology Details
Reaction catalysed:
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135987 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain
Length: 196 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P50281 (Residues: 316-511; Coverage: 35%)
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain
Truncated apolipoprotein A-I
Molecule details ›
Chains: B, C
Length: 211 amino acids
Theoretical weight: 24.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Apolipoprotein A1/A4/E domain
Length: 211 amino acids
Theoretical weight: 24.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P02647 (Residues: 79-122, 123-267; Coverage: 76%)
Sequence domains: Apolipoprotein A1/A4/E domain
