| 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. WFDC6 (WAP four-disulfide core domain protein 6), also known as WAP6, is a 131 amino acid secreted protein that contains one WAP domain and one BPTI/Kunitz inhibitor domain. WFDC6 is ubiquitously expressed, however highest levels are found in testis, trachea and epididymis. A cluster of WAP genes, including WFDC6, exist on chromosome 20, suggesting they evolved by repeated duplications. There are two isoforms of WFDC6 that are produced as a result of alternative splicing events. |
