Schlafen family member 13 (SLFN13)

Schlafen family member 13 (SLFN13) is a human protein that belongs to the Schlafen (SLFN) gene family, which encodes proteins sharing an N-terminal endoribonuclease domain, a central SWAVDL motif, and, in the case of group III SLFNs such as SLFN13, a C-terminal helicase/ATPase domain[1][2]. SLFN13 acts as a cytoplasmically localized endoribonuclease that specifically cleaves tRNA and rRNA, making a cut 11 nucleotides from the 3' terminus of tRNAs at the acceptor stem, thereby inhibiting protein synthesis in human cells[3][7]. SLFN13 can restrict the replication of HIV-1 by direct RNase activity and is considered part of the innate immune antiviral response, while other putative roles include involvement in monocyte differentiation[4][5][6]. Expression of SLFN13 appears to be tightly regulated, and the full-length protein is difficult to express stably in cells, likely due to toxicity resulting from its global inhibition of translation[4][6]. There are currently no known direct drugs targeting SLFN13 nor is it utilized as a clinical biomarker or therapeutic target, but ongoing research into the function and structure of Schlafen proteins continues to clarify their roles in immunity and stress responses[1][3][7].

Other names

SLFN13hSLFN13FLJ31952Schlafen-13SLFN10schlafen family member 13schlafen-13

No drugs known to target SLFN13 directly. SLFN13's restriction of HIV-1 is via its endoribonuclease activity on tRNAs/rRNAs, inhibiting protein synthesis.