Nuclear prelamin A recognition factor

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Technical|date=April 2008}}

{{Infobox_gene}}

Nuclear prelamin A recognition factor, also known as NARF, is a protein which in humans is encoded by the NARF gene.{{cite web | title = Entrez Gene: NARF nuclear prelamin A recognition factor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26502| accessdate = }}{{cite journal | vauthors = Barton RM, Worman HJ | title = Prenylated prelamin A interacts with Narf, a novel nuclear protein | journal = The Journal of Biological Chemistry | volume = 274 | issue = 42 | pages = 30008–18 | date = Oct 1999 | pmid = 10514485 | doi = 10.1074/jbc.274.42.30008 | doi-access = free }}{{cite journal | vauthors = Hackstein JH | title = Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions? | journal = Biochemical Society Transactions | volume = 33 | issue = Pt 1 | pages = 47–50 | date = Feb 2005 | pmid = 15667261 | doi = 10.1042/BST0330047 }}

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.

Interactions

NARF has been shown to interact with LMNA.

References

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Further reading

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  • {{cite journal | vauthors = Maltese WA | title = Posttranslational modification of proteins by isoprenoids in mammalian cells | journal = FASEB Journal | volume = 4 | issue = 15 | pages = 3319–28 | date = Dec 1990 | pmid = 2123808 | doi = 10.1096/fasebj.4.15.2123808| doi-access = free | s2cid = 17511637 }}
  • {{cite journal | vauthors = Barton RM, Worman HJ | title = Prenylated prelamin A interacts with Narf, a novel nuclear protein | journal = The Journal of Biological Chemistry | volume = 274 | issue = 42 | pages = 30008–18 | date = Oct 1999 | pmid = 10514485 | doi = 10.1074/jbc.274.42.30008 | doi-access = free }}
  • {{cite journal | vauthors = Hackstein JH | title = Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions? | journal = Biochemical Society Transactions | volume = 33 | issue = Pt 1 | pages = 47–50 | date = Feb 2005 | pmid = 15667261 | doi = 10.1042/BST0330047 }}
  • {{cite journal | vauthors = 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 | title = Towards a proteome-scale map of the human protein–protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}
  • {{cite journal | vauthors = 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 | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = Jan 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
  • {{cite journal | vauthors = Yamada M, Ohnishi J, Ohkawara B, Iemura S, Satoh K, Hyodo-Miura J, Kawachi K, Natsume T, Shibuya H | title = NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF) | journal = The Journal of Biological Chemistry | volume = 281 | issue = 30 | pages = 20749–60 | date = Jul 2006 | pmid = 16714285 | doi = 10.1074/jbc.M602089200 | doi-access = free }}
  • {{cite journal | vauthors = Lev-Maor G, Sorek R, Levanon EY, Paz N, Eisenberg E, Ast G | title = RNA-editing-mediated exon evolution | journal = Genome Biology | volume = 8 | issue = 2 | pages = R29 | year = 2007 | pmid = 17326827 | pmc = 1852406 | doi = 10.1186/gb-2007-8-2-r29 | doi-access = free }}

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Category:Human proteins

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