Description
Product Characteristics:
Prenylation and methylation are two forms of protein modification, both of which are important for a variety of functions, including membrane attachment, protein-protein interactions and signaling events. NARF (nuclear prelamin A recognition factor), also known as IOP2, is a 456 amino acid nuclear protein that belongs to the NARF family. Expressed ubiquitously with highest expression in heart, skeletal muscle and brain, NARF binds to the C-terminal end of prenylated prelamin A and may be a member of a prelamin A-containing endoprotease complex. Additionally, via its association with prelamin A, NARF may be involved in heterochromatin organization. NARF is expressed as three isoforms due to alternative splicing events and, upon DNA damage, may be phosphorylated by ATM or ATR.
Subcellular location: Nucleus
Synonyms: DKFZp434G0420, FLJ10067, GC17P078009, IOP2, Iron only hydrogenase like protein 2, Nuclear prelamin A recognition factor, Prenyl dependent prelamin A binding NARF_HUMAN.
Target Information: Several proteins have been found to be prenylated and 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 protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the 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 hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing. [provided by RefSeq, Jul 2008]