Nuclear prelamin A recognition factor

Nuclear prelamin A recognition factor, also known as NARF, is a is_associated_with::protein which in humans is encoded by the NARF is_associated_with::gene.

Function
Several proteins have been found to be is_associated_with::prenylated and is_associated_with::methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in is_associated_with::protein-protein interactions. The only is_associated_with::nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type is_associated_with::lamins. Prelamin A is farnesylated and carboxymethylated on the is_associated_with::cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial is_associated_with::hydrogenases. Alternatively spliced transcript variants encoding different is_associated_with::isoforms have been identified for this gene, including one with a novel is_associated_with::exon that is generated by RNA editing.

Interactions
NARF has been shown to interact with is_associated_with::LMNA.