Schlafen family member 14 (SLFN14)

Schlafen family member 14 (SLFN14) is an endoribonuclease and member of the Schlafen protein family implicated in RNA metabolism, immune defense, and human disease[1][2][3]. Structurally, SLFN14 consists of an RNase domain, a SWADL (Schlafen) domain, and a helicase-like C-terminal domain but lacks canonical helicase activity due to defective ATP binding[1]. SLFN14 binds and cleaves rRNA and ribosome-associated mRNAs, impacting protein translation[1][2][4]. Its normal function includes roles in the innate immune response and the development and secretion of platelets, explaining why mutations in SLFN14 cause inherited thrombocytopenia and bleeding disorders such as BDPLT20[1][2]. SLFN14 is also structurally related to other Schlafen proteins with important functions in cancer biology and immune defense, though its direct role as a therapeutic target is emerging primarily from genetic and structural studies rather than pharmacologic intervention[1][2][3][4].

Other names

Protein SLFN14C-terminally truncated SLFN14 endoribonucleaseSLFN14Schlafen family member 14BDPLT20