Function and Biology Details
Reaction catalysed:
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S1A, chymotrypsin family
- Peptidase S1, PA clan, chymotrypsin-like fold
- Serine proteases, trypsin domain
- SRCR-like domain superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
- SRCR-like domain
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serine protease hepsin catalytic chain (preferred)
PDBe Complex ID:
PDB-CPX-138846 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease hepsin non-catalytic chain
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.52 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Hepsin, SRCR domain
Structure domains: SRCR-like domain
Length: 114 amino acids
Theoretical weight: 12.52 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P05981 (Residues: 46-159; Coverage: 27%)
Sequence domains: Hepsin, SRCR domain
Structure domains: SRCR-like domain
Serine protease hepsin catalytic chain
Molecule details ›
Chain: B
Length: 255 amino acids
Theoretical weight: 27.57 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 255 amino acids
Theoretical weight: 27.57 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical: P05981 (Residues: 163-417; Coverage: 61%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
