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presequence protease, mitochondrial (hPreP, pitrilysin metalloproteinase 1, metalloprotease 1, hMP1, PITRM1, KIAA1104, MP1)
Function:
1) ATP-independent protease
2) degrades mitochondrial transit peptides after their cleavage
3) also degrades other unstructured peptides
4) specific for peptides in the range of 10-65 residues
5) able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion
6) preference for cleavage after small polar residues & before basic residues, without any positional preference
Cofactor: binds 1 Zn+2 per subunit
Structure:
- homodimer
- disulfide bond may lock the enzyme in a closed conformation under oxidized conditions, i.e. redox regulation of enzyme
- belongs to the peptidase M16 family, PreP subfamily
Compartment: mitochondrial matrix
Alternative splicing: named isoforms=2
Expression:
- widely expressed
- expressed in muscle & heart > brain, pancreas, liver, lung & placenta
General
metalloprotease
mitochondrial protein
Properties
SIZE: MW = 117 kD
entity length = 1037 aa
COMPARTMENT: mitochondrial matrix
MOTIF: Zn+2-binding site
SITE: 104-104
glutamate residue {E107}
Zn+2-binding site
SITE: 108-108
cysteine residue {C119}
MODIFICATION: cysteine residue {C556}
Zn+2-binding site
SITE: 205-205
cysteine residue {C556}
MODIFICATION: cysteine residue {C119}
Database Correlations
UniProt Q5JRX3
PFAM correlations
References
UniProt :accession Q5JRX3