| Modification Notes |
Peptidases are enzymes that are responsible for hydrolyzing peptide bonds of polypeptide chains during protein catabolism. Protease inhibitors are important peptidase regulators which halt enzymatic function. The WAP (whey acidic protein) domain, also referred to as the WAP-type four-disulfide core domain, is a signature protein motif that contains eight cysteine residues which form disulfide bonds and may exhibit protease inhibitor activity. WAP domain-containing proteins are thought to function in the immune defense by cleaving microbial proteolytic enzymes in order to prevent tissue penetration and infection. WFDC9 (WAP four-disulfide core domain protein 9), also known as WAP9, is a 89 amino acid secreted protein that that doesn’t contain a classical WAP domain, however the gene encoding WFDC9 resides within a cluster of WAP genes on chromosome 20. WFDC9 contains a 23 amino acid N-terminal signal peptide that is cleaved to result in a secreted mature form. |
