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carboxypeptidase Z (CPZ)
Function:
1) cleaves substrates with C-terminal arginine residues
3) modulates Wnt signaling pathway, by cleaving some undetermined protein (probable)
3) role in cleavage during prohormone processing.
Cofactor: bind 1 Zn+2 per subunit
Inhibition:
- 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid (MGTA)
- guanidinoethylmercaptosuccinic acid (GEMSA)
- chelating agents, including EDTA & EGTA
Kinetic parameters:
- KM=2 mM for dansyl-Phe-Ala-Arg;
- KM=2 mM for dansyl-Pro-Ala-Arg;
- Optimum pH is 7.8
Structure:
1) belongs to the peptidase M14 family
2) contains 1 FZ (frizzled) domain
Compartment: secreted protein, extracellular matrix
Alternative splicing: named isoforms=2
Expression:
- widely expressed
- placenta, present within invasive trophoblasts & in surrounding extracellular space
- present in amnion cells
- present in pituitary
General
carboxypeptidase
glycoprotein
matrix protein
metalloprotein
Properties
SIZE: MW = 74 kD
entity length = 652 aa
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-18}
frizzled domain {27-160}
MOTIF: cysteine residue {C43}
MODIFICATION: cysteine residue {C109}
cysteine residue {C51}
MODIFICATION: cysteine residue {C102}
cysteine residue {C93}
MODIFICATION: cysteine residue {C129}
cysteine residue {C102}
MODIFICATION: cysteine residue {C51}
cysteine residue {C109}
MODIFICATION: cysteine residue {C43}
cysteine residue {C118}
MODIFICATION: cysteine residue {C157}
cysteine residue {C122}
MODIFICATION: cysteine residue {C146}
cysteine residue {C129}
MODIFICATION: cysteine residue {C93}
cysteine residue {C146}
MODIFICATION: cysteine residue {C122}
cysteine residue {C157}
MODIFICATION: cysteine residue {C118}
Zn+2-binding site
SITE: 248-248
Zn+2-binding site
SITE: 251-251
N-glycosylation site {N281}
Zn+2-binding site
SITE: 380-380
tyrosine residue {Y450}
glutamate residue {E472}
Database Correlations
OMIM 603105
UniProt Q66K79
PFAM correlations
Entrez Gene 8532
References
UniProt :accession Q66K79