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Based on its amino acid sequence, KEAP1 has five distinct domains: (i) an N-terminal region (NTR, amino acids 1–49), (ii) a Broad complex, Tramtrack, and Bric à brac (BTB) domain (amino acids 50–179), through which KEAP1 forms a homodimer and also interacts with Cullin3, (iii) an intervening region (IVR, also known as BACK domain, amino acids 180–314), which is especially cysteine-rich and contains 8 cysteine residues among its 134 amino acids, (iv) a Kelch domain, comprising six Kelch motifs (amino acids 315–359, 361–410, 412–457, 459–504, 506–551, and 553–598), through which KEAP1 binds to its substrates, and (v) a C-terminal region (CTR, amino acids 599–624)
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Discussion Cataract is a major ophthalmic disease causing severe visual impairment and even blindness in patients (1,2)
