Home News About DMDM Database Statistics Research Publications Contact  

  Domain Name: M14_CP_A-B_like_1
Peptidase M14 carboxypeptidase subfamily A/B-like; uncharacterized subgroup. The Peptidase M14 Carboxypeptidase A/B-like subfamily is one of two main M14 carboxypeptidase subfamilies, defined by sequence and structural homology, the other being N/E. Carboxypeptidases (CPs) hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Majority of the proteins in this subfamily have not been characterized as yet. The A/B enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; the proenzymes are called procarboxypeptidases. These enzymes exhibit distinct substrate specificity pattern; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4, detected in hormone-regulated tissues, is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 19
Total Disease Mutations Found: 2
This domain occurred 14 times on human genes (17 proteins).


 If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position.

 The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.

 Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.

Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  

Feature Name:Total Found:
Zn binding site
putative active site

Weblogos are Copyright (c) 2002 Regents of the University of California

Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

   |   1000 Hilltop Circle, Baltimore, MD 21250   |   Department of Biological Sciences   |   Phone: 410-455-2258