Nuclear prelamin A recognition factor

NARF
Identifiers
AliasesNARF, IOP2, nuclear prelamin A recognition factor
External IDsMGI: 1914858 HomoloGene: 57048 GeneCards: NARF
Gene location (Human)
Chr.Chromosome 17 (human)[1]
BandNo data availableStart82,458,180 bp[1]
End82,490,537 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 17: 121.24 – 121.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000141562 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000056 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: NARF nuclear prelamin A recognition factor".
  6. 1 2 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. PMID 10514485. doi:10.1074/jbc.274.42.30008.
  7. Hackstein JH (Feb 2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochemical Society Transactions. 33 (Pt 1): 47–50. PMID 15667261. doi:10.1042/BST0330047.

Further reading

  • Maltese WA (Dec 1990). "Posttranslational modification of proteins by isoprenoids in mammalian cells". FASEB Journal. 4 (15): 3319–28. PMID 2123808. 
  • 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. PMID 10514485. doi:10.1074/jbc.274.42.30008. 
  • Hackstein JH (Feb 2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochemical Society Transactions. 33 (Pt 1): 47–50. PMID 15667261. doi:10.1042/BST0330047. 
  • 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. PMID 16189514. doi:10.1038/nature04209. 
  • 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. PMC 1356129Freely accessible. PMID 16344560. doi:10.1101/gr.4039406. 
  • 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. PMID 16714285. doi:10.1074/jbc.M602089200. 
  • Lev-Maor G, Sorek R, Levanon EY, Paz N, Eisenberg E, Ast G (2007). "RNA-editing-mediated exon evolution". Genome Biology. 8 (2): R29. PMC 1852406Freely accessible. PMID 17326827. doi:10.1186/gb-2007-8-2-r29. 


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