NARF
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Official Full Name
nuclear prelamin A recognition factor -
Overview
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. -
Synonyms
NARF;nuclear prelamin A recognition factor;DKFZp434G0420;FLJ10067;IOP2;iron only hydrogenase like protein 2;iron-only hydrogenase-like protein 2;prenyl-dependent prelamin A binding protein
Recombinant Proteins
- Mouse
- Human
- Rat
- Zebrafish
- Mammalian Cells
- E.coli
- HEK293
- His
- Non
- Myc&DDK
- His&Fc&Avi
Involved Pathway
NARF involved in several pathways and played different roles in them. We selected most pathways NARF participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with NARF were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
NARF has several biochemical functions, for example, NOT NADH dehydrogenase activity,NOT iron-sulfur cluster binding,lamin binding. Some of the functions are cooperated with other proteins, some of the functions could acted by NARF itself. We selected most functions NARF had, and list some proteins which have the same functions with NARF. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| lamin binding | SUN2,SUN1,TMEM201,IFI27,PLCB1,LBR,TOR1AIP1,PPP4C,BNIP3L,TMPO |
Interacting Protein
NARF has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with NARF here. Most of them are supplied by our site. Hope this information will be useful for your research of NARF.
SFRP4;q7ard3_yerpe;PRPF4;PTBP3;Nedd1;CBX5;Espl1;Ppp4c;TOR1AIP1;Vangl1;ENTHD2;Rab11fip1;Ranbp2;ACTR5;Mtmr2
Resources
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References
- Song, DS; Lee, FS; et al. Mouse Knock-out of IOP1 Protein Reveals Its Essential Role in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis. JOURNAL OF BIOLOGICAL CHEMISTRY 286:-(2011).
- Song, DS; Tu, Z; et al. Human ISCA1 Interacts with IOP1/NARFL and Functions in Both Cytosolic and Mitochondrial Iron-Sulfur Protein Biogenesis. JOURNAL OF BIOLOGICAL CHEMISTRY 284:35297-35307(2009).
