WAP four-disulfide core domain 9 (WFDC9)

WAP four-disulfide core domain 9 is a secreted protein in humans encoded by the WFDC9 gene, which is part of the WFDC protein family. These proteins are characterized by the presence of one or more WFDC domains, which consist of 40–50 amino acids with eight conserved cysteine residues forming four disulfide bonds. WFDC family members are known for their antiprotease, antibacterial, and immunomodulatory functions, and are expressed in a variety of tissues throughout the body. Aberrant expression of WFDC family proteins has been related to pathological conditions such as cancer and inflammatory diseases. Although well-studied family members like SLPI and elafin have established roles in immunity and inflammation, the specific biological roles of WFDC9 are less well-defined but presumed similar in terms of potential protease inhibition and involvement in host defense. The WFDC9 gene is located in a gene cluster on human chromosome 20. WFDC proteins contain a distinctive four-disulfide core domain implicated in protease inhibition, antimicrobial activity, and immunomodulation. The WFDC9 gene is clustered with other WFDC domain-containing genes, suggesting evolutionary adaptations related to reproduction and immunity. No experimentally validated protein-protein interactions or functional studies on WFDC9 alone are currently available. Aliases for WFDC9 include several alternative names, but the canonical name for structured data purposes is "WAP four-disulfide core domain 9" (WFDC9). While the overall WFDC family is a topic of drug development and biomarker research, no drugs or clinical utility are attributed specifically to WFDC9 at present.

Other names

WFDC9WAP9dJ688G8.2Protein WFDC9