NARF

From Wikipedia, the free encyclopedia

Nuclear prelamin A recognition factor

Identifiers

NARF; DKFZp434G0420; FLJ10067; IOP2

External IDs

OMIM: 605349 MGI: 1914858 HomoloGene: 57048

Gene ontology
Molecular Function:	• iron ion binding • protein binding • lamin binding • ferredoxin hydrogenase activity • electron carrier activity
Cellular Component:	• lamin filament • nuclear lamina • nuclear lumen • periplasmic space
Biological Process:	• electron transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001038618 (mRNA)
NP_001033707 (protein)

NM_026272 (mRNA)
NP_080548 (protein)

Location

Chr 17: 78.01 - 78.04 Mb

Chr 11: 121.05 - 121.07 Mb

Pubmed search

[1]

[2]

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Nuclear prelamin A recognition factor, also known as NARF, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: NARF nuclear prelamin A recognition factor.

[edit] Further reading

Maltese WA (1991). "Posttranslational modification of proteins by isoprenoids in mammalian cells.". FASEB J. 4 (15): 3319–28. PMID 2123808.
Barton RM, Worman HJ (1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein.". J. Biol. Chem. 274 (42): 30008–18. PMID 10514485.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Hackstein JH (2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochem. Soc. Trans. 33 (Pt 1): 47–50. doi:10.1042/BST0330047. PMID 15667261.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Yamada M, Ohnishi J, Ohkawara B, et al. (2006). "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF).". J. Biol. Chem. 281 (30): 20749–60. doi:10.1074/jbc.M602089200. PMID 16714285.
Lev-Maor G, Sorek R, Levanon EY, et al. (2007). "RNA-editing-mediated exon evolution.". Genome Biol. 8 (2): R29. doi:10.1186/gb-2007-8-2-r29. PMID 17326827.