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U2 small nuclear RNA auxiliary factor 1-like 4 (U2AF1L4) is a multifaceted pre-mRNA splicing factor, homologous to the small U2AF subunit, that contributes to the recognition of 3′ splice sites and regulation of alternative splicing[1][2]. The protein contains zinc finger domains crucial for splicing activity, stability, and interactions with other spliceosomal proteins. U2AF1L4 regulates constitutive and enhancer-dependent splicing by binding to the AG dinucleotide at 3′ splice sites and enhances U2AF2 binding to weak polypyrimidine tracts[2]. Distinct isoforms of U2AF1L4 display differential subcellular localization, including shuttling between nucleus and cytoplasm, which may dictate availability for splicing or translation[1]. An evolutionarily conserved enhancer in its gene regulates transcription, and coordinated regulation of U2AF1L4 expression influences critical immune functions such as alternative splicing of CD45 receptor isoforms during T-cell activation[1]. U2AF1L4 is not associated with recognized drug modulation or disease, and is best classified as a core RNA-binding splicing factor within the spliceosomal machinery[1][2][3].
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