Nuclear prelamin A recognition factor

Nuclear prelamin A recognition factor, also known as NARF, is a protein which in humans is encoded by the NARF gene.[5][6][7]

NARF
Identifiers
Aliases	NARF, IOP2, nuclear prelamin A recognition factor
External IDs	OMIM: 605349 MGI: 1914858 HomoloGene: 57048 GeneCards: NARF
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q25.3 Start 82,458,180 bp[1] End 82,490,537 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 E2 Start 121,237,253 bp[2] End 121,255,856 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • lamin binding • NADH dehydrogenase activity • iron-sulfur cluster binding Cellular component • nuclear lamina • nuclear lumen • lamin filament • cell nucleus • nucleolus Biological process • oxidation-reduction process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	26502	67608
Ensembl	ENSG00000141562	ENSMUSG00000000056
UniProt	Q9UHQ1	Q9CYQ7
RefSeq (mRNA)	NM_001038618 NM_001083608 NM_012336 NM_031968	NM_026272
RefSeq (protein)	NP_001033707 NP_001077077 NP_036468 NP_114174	NP_080548
Location (UCSC)	Chr 17: 82.46 – 82.49 Mb	Chr 11: 121.24 – 121.26 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[5]

Interactions

NARF has been shown to interact with LMNA.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000141562 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000056 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: NARF nuclear prelamin A recognition factor".
6. Barton RM, Worman HJ (Oct 1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". The Journal of Biological Chemistry. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.
7. Hackstein JH (Feb 2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochemical Society Transactions. 33 (Pt 1): 47–50. doi:10.1042/BST0330047. PMID 15667261.

Further reading

• Maltese WA (Dec 1990). "Posttranslational modification of proteins by isoprenoids in mammalian cells". FASEB Journal. 4 (15): 3319–28. doi:10.1096/fasebj.4.15.2123808. PMID 2123808. S2CID 17511637.
• Barton RM, Worman HJ (Oct 1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". The Journal of Biological Chemistry. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.
• Hackstein JH (Feb 2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochemical Society Transactions. 33 (Pt 1): 47–50. doi:10.1042/BST0330047. PMID 15667261.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein–protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Yamada M, Ohnishi J, Ohkawara B, Iemura S, Satoh K, Hyodo-Miura J, Kawachi K, Natsume T, Shibuya H (Jul 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)". The Journal of Biological Chemistry. 281 (30): 20749–60. doi:10.1074/jbc.M602089200. PMID 16714285.
• Lev-Maor G, Sorek R, Levanon EY, Paz N, Eisenberg E, Ast G (2007). "RNA-editing-mediated exon evolution". Genome Biology. 8 (2): R29. doi:10.1186/gb-2007-8-2-r29. PMC 1852406. PMID 17326827.