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LUC7 like 3 pre-mRNA splicing factor (LUC7L3) is a nuclear RNA-binding protein involved in the regulation of pre-mRNA splicing. The protein contains an N-terminal region with cysteine/histidine motifs and leucine zipper-like repeats, and a C-terminal region rich in arginine-glutamate (RE domain) and arginine-serine (RS domain). It is a component of the spliceosome, particularly associated with the U1 small nuclear ribonucleoprotein (U1 snRNP) complex, and influences 5′ splice site recognition and alternative splicing outcomes. LUC7L3 exerts its regulatory function through direct RNA binding and interaction with other splicing factors; its loss or dysfunction can shift splicing patterns, affecting gene expression in a context-dependent manner. Disease associations include altered splicing in cancer and possible roles in cardiac disease via interaction with key splicing regulators such as RBM25. Two major isoforms result from alternative splicing of its transcript, but both are believed to encode the same protein.
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