WAP-type 'four-disulfide core' domain
IPR008197
Definition
The four-disulfide core (4-DSC) or WAP domain comprises eight cysteine residues involved in disulfide bonds in a conserved arrangement PMID:6896234. The four disulphide core containing Whey Acidic Proteins (WAP) are the major whey proteins in the milk of many mammals and are considered to be the prototypic members of the family. However the WAP domain is not exclusive to WAP proteins, but it is found in many other proteins, a number of which have been shown to exhibit antiproteinase function [[cite:PMID:11965550], [cite:PMID:21936823], [cite:PMID:18676177]]. One or more of the WAP domains occur in the WDNM1 protein, which is involved in the metastatic potential of adenocarcinomas in rats PMID:3136918; Kallmann syndrome protein PMID:1913827; caltrin-like protein II from guinea pig PMID:2324101, which inhibits calcium transport into spermatozoa; elafin, a serine elastase inhibitor which belongs to MEROPS inhibitor family I17 PMID:2394696; and papilin, a metalloendopeptidase inhibitor which belongs to MEROPS inhibitor family I2 and is effective against procollagen N-proteinase PMID:11076767.
15 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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