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WAP four-disulfide core domain protein 10A (WFDC10A) is a small, secreted protein characterized by a signature motif containing eight cysteines that form four disulfide bonds, providing structural stability. Primarily acting as a serine protease inhibitor, WFDC10A belongs to a family involved in tissue protection, immunomodulation, and host defense. The exact biological functions and disease associations of WFDC10A are less defined than for several other WFDC members, but its molecular structure and gene localization suggest roles in the immune system and antiprotease-mediated regulation of inflammation.
Inhibition of serine-type proteases; modulation of immune responses (based on family-wide function). Drug action mechanisms specific to WFDC10A are not established.
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