WAP four-disulfide core domain protein 10B (WFDC10B)

WAP four-disulfide core domain protein 10B (WFDC10B) is a member of the WFDC domain-containing protein family, which is characterized by a conserved domain structure containing eight cysteine residues forming four disulfide bonds at its core[1][2]. This domain, also known as the WAP signature motif, is commonly found in a class of small secretory proteins and typically confers protease inhibitor activity. The human WFDC gene cluster, including WFDC10B, is located on chromosome 20q12-q13 and is divided into centromeric and telomeric clusters, with WFDC10B in the telomeric cluster[1][2]. WFDC family members are involved in diverse biological processes, particularly protease inhibition and host defense, exhibiting antiprotease, antimicrobial, and immunomodulatory activities. Aberrant expression of these proteins, including WFDC10B, has been associated with human diseases such as inflammation and cancer[2]. However, there is limited evidence that WFDC10B itself is a validated or established therapeutic target, and there are currently no drugs known to interact with it specifically[2][3].

Other names

Protein WFDC10BWAP12protease inhibitor WAP12protein WFDC10BWFDC10B