CPA1
CPA1 (carboxypeptidase A1, also known as CPA) is a secreted zinc metalloprotease of the M14 family that removes C-terminal amino acids from peptides and proteins. It is produced in the pancreas and acts on dietary proteins. Browse Assay Genie's current range of CPA1 research reagents below, or read on for the biology behind the target.
CPA1 is a carboxypeptidase that catalyses the release of a C-terminal amino acid from its substrates. It has little or no action when the C-terminal residue is aspartate, glutamate, arginine, lysine or proline. In the pancreas it preferentially cleaves C-terminal branched-chain and aromatic amino acids from dietary proteins. UniProt also records that CPA1 catalyses the conversion of leukotriene C4 to leukotriene F4 through hydrolysis of an amide bond.
The CPA1 gene encodes a member of the carboxypeptidase A family of zinc metalloproteases, and the protein belongs to the peptidase M14 family. HGNC places it in the M14 carboxypeptidases gene group. The enzyme is secreted, consistent with its role as a digestive enzyme produced in the pancreas. Mouse and rat each have a corresponding Cpa1 ortholog. The gene sits in a cluster on chromosome 7 together with several other family members, including CPA2, CPA4 and CPA5.
CPA1 was formerly listed as carboxypeptidase A1 (pancreatic), and CPA is a previous symbol. RefSeq notes that mutations in the gene may be linked to chronic pancreatitis, while elevated CPA1 protein levels may be associated with pancreatic cancer. This makes the protein a point of interest for researchers studying pancreatic physiology and disease.
Mutations in the CPA1 gene may be linked to chronic pancreatitis, making it relevant to studies of pancreatic injury and inflammation.
Elevated CPA1 protein levels may be associated with pancreatic cancer, so the enzyme is examined in work on tumour biology.
CPA1 is produced in the pancreas and cleaves C-terminal branched-chain and aromatic residues from dietary proteins.
CPA1 converts leukotriene C4 to leukotriene F4 by hydrolysing an amide bond, linking it to lipid mediator processing.
CPA1 is a zinc metalloprotease that releases C-terminal amino acids, with little or no action on aspartate, glutamate, arginine, lysine or proline. In the pancreas it preferentially cleaves branched-chain and aromatic residues from dietary proteins. It also converts leukotriene C4 to leukotriene F4.
The HGNC name is carboxypeptidase A1, and UniProt uses the same protein name. CPA is a previous symbol, and the earlier name was carboxypeptidase A1 (pancreatic). It carries the EC number 3.4.17.1 and sits in the M14 carboxypeptidases gene group.
RefSeq reports that CPA1 mutations may be linked to chronic pancreatitis and that elevated protein levels may be associated with pancreatic cancer. Mouse and rat both have a Cpa1 ortholog; check the datasheet of any product for its validated reactivity.
Other members of the carboxypeptidase A family encoded in the same chromosome 7 gene cluster.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P15085; product specifications from Assay Genie datasheets.