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carboxypeptidase D (metallocarboxypeptidase D, gp180, PEPD, CPD)
Function:
- releases C-terminal Arg & Lys from polypeptides
Cofactor: binds 2 Zn+2 per subunit (putative)
Kinetic parameters:
- Optimum pH is 6.0-6.5
Structure:
- carboxypeptidase-like domains
- only the 1st 2 domains seem to have catalytic activity
- belongs to the peptidase M14 family
Compartment: membrane
Expression:
- expressed in placenta, pancreas & hepatoma cells > skeletal muscle, heart & colon carcinoma & melanoma cell lines
General
carboxypeptidase
glycoprotein
phosphoprotein
Properties
SIZE: entity length = 1380 aa
MW = 153 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-31}
Carboxypeptidase-like 1 {32-493}
MOTIF: Zn+2-binding site
SITE: 139-139
Zn+2-binding site
SITE: 142-142
Cell attachment site {162-164}
N-glycosylation site {N172}
N-glycosylation site {N217}
Zn+2-binding site
SITE: 257-257
glutamate residue {E350}
N-glycosylation site {N399}
N-glycosylation site {N410}
N-glycosylation site {N429}
Carboxypeptidase-like 2 {494-897}
MOTIF: N-glycosylation site {N522}
Zn+2-binding site
SITE: 564-564
Zn+2-binding site
SITE: 567-567
N-glycosylation site {N626}
Zn+2-binding site
SITE: 671-671
glutamate residue {E762}
N-glycosylation site {N811}
N-glycosylation site {N855}
N-glycosylation site {N867}
N-glycosylation site {N879}
Carboxypeptidase-like 3 {898-1299}
MOTIF: N-glycosylation site {N955}
N-glycosylation site {N978}
N-glycosylation site {N1070}
N-glycosylation site {N1142}
transmembrane domain {1300-1320}
MOTIF: cysteine residue {C1317}
MODIFICATION: palmitate
COMPARTMENT: membrane
cysteine residue {C1321}
MODIFICATION: palmitate
COMPARTMENT: membrane
cysteine residue {C1323}
MODIFICATION: palmitate
COMPARTMENT: membrane
Thr phosphorylation site {T1368}
Thr phosphorylation site {T1370}
Database Correlations
OMIM 603102
UniProt O75976
Pfam PF00246
Entrez Gene 1362
Kegg hsa:1362
ENZYME 3.4.17.22
References
UniProt :accession O75976