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carboxypeptidase A1 (CPA1, CPA)
Function:
- release of a C-terminal amino acid
- little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
- may form a complex with proelastase 2
Cofactor: binds 1 Zn+2 per subunit
Structure:
- monomer
- belongs to the peptidase M14 family
Compartment: secreted
General
carboxypeptidase-A
Properties
SIZE: entity length = 419 aa
MW = 47 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-16}
Substrate binding {179-182}
MOTIF: Zn+2-binding site
SITE: 179-179
Zn+2-binding site
SITE: 182-182
binding site
SITE: 237-237
FOR-BINDING-OF: Substrate
cysteine residue {C248}
MODIFICATION: cysteine residue {C271}
Substrate binding {254-255}
cysteine residue {C271}
MODIFICATION: cysteine residue {C248}
Zn+2-binding site
SITE: 306-306
Substrate binding {307-308}
glutamate residue {E380}
Database Correlations
OMIM 114850
UniProt P15085
PFAM correlations
Entrez Gene 1357
Kegg hsa:1357
ENZYME 3.4.17.1
References
UniProt :accession P15085