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WD repeat and coiled-coil-containing protein (WDCP) is a nuclear and possibly cytoplasmic protein encoded by the human WDCP gene (also known as C2orf44, MMAP, PP384). Its structure consists of two WD-repeat domains at the N-terminus and a coiled-coil region at the C-terminus, as well as a proline-rich motif that specifically binds to the SH3 domain of the Src-family kinase HCK, leading to tyrosine phosphorylation of WDCP. WDCP tends to form oligomers in cells and lacks transmembrane regions, which supports its subcellular localization to the nucleus and nucleolus, though cytoplasmic presence has been observed in some contexts. Its molecular function appears related to protein-protein interactions, including with kinases (e.g., HCK) and AAA ATPases; however, its cellular roles remain largely undefined. WDCP is notably implicated in oncogenic processes through gene fusion events, such as ALK-C2orf44 in colorectal cancer, where the fusion protein promotes constitutive kinase activation, aberrant signaling, and possibly tumorigenesis. No drugs, mechanism of action, or safety issues are known for WDCP itself; clinical and biomarker relevance primarily arise in the context of disease-linked fusion proteins.
Not applicable for WDCP alone. In fusion proteins (such as ALK-C2orf44), it may promote kinase activation and signaling by oligomerization; Src tyrosine kinase may phosphorylate the protein.
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