WAP four-disulfide core domain protein 13 (WFDC13)

WAP four-disulfide core domain protein 13 (WFDC13) is a member of the WFDC (whey acidic protein four-disulfide core) domain family, characterized by a 40–50 amino acid domain that contains eight conserved cysteine residues forming four intramolecular disulfide bonds. The WFDC domain is primarily a structural protein motif with probable function as a protease inhibitor, especially antiprotease activity against serine proteases, although direct biochemical function for WFDC13 has not been fully established and remains putative. Most genes in the WFDC family are clustered on human chromosome 20q12-q13, with WFDC13 located in the telomeric cluster. WFDC proteins in general are implicated in host defense, immune regulation, and inhibition of various proteases, potentially relevant to tissue protection, inflammation, and antimicrobial activity, but no direct links for WFDC13 with specific diseases, biomarkers, or drug interactions are established in current public databases or literature. WFDC13 is referenced as a putative acid-stable proteinase inhibitor, but its precise biological function, disease association, and value as a therapeutic target are unconfirmed. Key contextual notes: - No evidence WFDC13 is currently a direct therapeutic target, receptor, or enzyme of drug interest. - No approved drugs or ligands, no direct safety concerns, and no established role in disease have been assigned in searched biomedical resources. - The structural domain is well described, but specific molecular and clinical relevance remains under-characterized in the literature.

Other names

C20orf138WAP13dJ601O1.3protein WFDC13protease inhibitor WAP13