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The EEF1AKMT4-ECE2 readthrough is a fusion protein resulting from the transcriptional readthrough of adjacent genes EEF1AKMT4 and ECE2, containing sequence identity and proposed enzymatic functions of both. The EEF1AKMT4-derived portion encodes a methyltransferase that specifically methylates lysine 36 of eukaryotic elongation factor 1A (eEF1A), influencing mRNA translation by modulating codon translation rates[1]. The ECE2-derived region contains a peptidase domain that hydrolyzes big endothelin-1 to produce endothelin-1, a vasoactive peptide important in cardiovascular physiology[2][3]. Evidence supporting the existence of the full-length fusion protein is limited, with most data supporting expression of individual protein domains but not the entire readthrough protein in vivo[1]. Therefore, "EEF1AKMT4-ECE2 readthrough" is not considered a canonical therapeutic target (receptor, enzyme, transporter) and its biological significance remains uncertain[1][2].
Not established for this readthrough protein; ECE2 region is a peptidase, EEF1AKMT4 region is a methyltransferase
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