WAP four-disulfide core domain
IPR050514
Definition
The WAP four-disulfide core domain family encompasses a group of proteins characterized by a conserved WAP-type four-disulfide core domain. Members of this family are involved in a variety of biological functions, primarily acting as protease inhibitors. They exhibit a broad range of inhibitory activities against proteases such as trypsin, chymotrypsin, elastase, and cathepsin G. Some family members are implicated in modulating inflammatory and immune responses, particularly following bacterial infections or in response to intracellular parasites like L.major. They may also play roles in tissue remodeling, wound healing, and possibly in sperm maturation. Additionally, certain proteins within this family, particularly those classified as venom waprins, have been shown to damage bacterial membranes and exhibit antibacterial activity, although they do not display hemolytic or toxic effects in mammals. The diversity of functions within this family reflects the versatility of the WAP-type domain in providing protective roles in various biological contexts.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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