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THAP domain-containing protein 4 (THAP4) is a human heme-binding protein that displays peroxynitrite isomerase activity, meaning it scavenges peroxynitrite and protects against peroxynitrite-mediated nitration by converting peroxynitrite to nitrate. The protein contains a DNA-binding THAP domain at its N-terminus and a C-terminal nitrobindin heme-binding domain, making it unique among human THAP proteins for its ability to bind a cofactor. Structurally, THAP4 may function as a nitric oxide (NO) sensor, modulating the activity of the DNA-binding domain and possibly controlling NO-regulated transcription or apoptosis. While expression is fairly ubiquitous, it is upregulated under heat shock and in certain malignancies such as lymphoma. Although some functional similarity to other THAP family members (such as transcriptional regulation and apoptosis mediation) is predicted, THAP4’s exact physiological and pathological roles remain incompletely characterized. No known drugs or established therapeutic mechanisms are associated with THAP4.
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