Splicing factor, suppressor of white-apricot homolog (SFSWAP)

Splicing factor, suppressor of white-apricot homolog (SFSWAP) is a human protein encoded by the SFSWAP gene, functioning as a splicing factor originally characterized as the human homolog of the Drosophila splicing regulatory protein SWAP[1][2][3][7]. SFSWAP regulates alternative mRNA splicing by controlling exon inclusion/skipping and retained intron splicing in various transcripts, including fibronectin, CD45, MAPT/Tau, and itself through autoregulation[1][2][3][7]. Structurally, SFSWAP contains two SURP domains—which mediate protein-protein interactions—as well as an RS (arginine/serine-rich) domain, but it lacks canonical RNA binding domains[2]. It is a global negative regulator of splicing, facilitating detained intron formation and exon skipping by modulating spliceosome assembly, often in coordination with other splicing factors such as SF1 and SRSF1[2]. No approved drugs or clinical modulators for SFSWAP are known, and it is currently not considered a direct therapeutic target. Mutations or altered functions in SFSWAP have been associated with rare Mendelian diseases such as autosomal dominant deafness (type 41) and pulmonary subvalvular stenosis[3]. No specific small-molecule safety issues, drugs, or biomarker roles for SFSWAP have been reported to date.

Other names

SFRS8SWAPSplicing factor SWAPSuppressor of white apricot protein homologSplicing factor, arginine/serine-rich 8Splicing factor, suppressor of white-apricot family