NXF1

Nuclear RNA export factor 1
Rendering of 1FO1
Available structures PDB 1FO1, 1FT8, 1JKG, 1JN5, 1KOH, 1KOO, 1OAI, 2Z5K, 2Z5M
Identifiers
Symbols	NXF1; DKFZp667O0311; MEX67; TAP
External IDs	OMIM: 602647 MGI: 1858330 HomoloGene: 38176 GeneCards: NXF1 Gene
Gene Ontology Molecular function • nucleotide binding • mRNA binding • nucleocytoplasmic transporter activity • protein binding Cellular component • intracellular • nucleus • nuclear pore • nucleoplasm • cytoplasm • cytosol • nuclear speck • nuclear inclusion body Biological process • mRNA export from nucleus • mRNA export from nucleus • transport • gene expression • poly(A)+ mRNA export from nucleus • interspecies interaction between organisms Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10482	53319
Ensembl	ENSG00000162231	ENSMUSG00000010097
UniProt	Q9UBU9	Q3TJA5
RefSeq (mRNA)	NM_001081491.1	NM_016813.2
RefSeq (protein)	NP_001074960.1	NP_058093.2
Location (UCSC)	Chr 11: 62.56 – 62.57 Mb	Chr 19: 8.83 – 8.85 Mb
PubMed search	[1]	[2]

Nuclear RNA export factor 1, also known as NXF1, is a protein which in humans is encoded by the NXF1 gene.^[1][2]

Function

This gene is one member of a family of nuclear RNA export factor genes. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. Alternative splicing results in transcript variants. The LRRs and NTF2-like domains are required for export activity. The encoded protein of this gene shuttles between the nucleus and the cytoplasm and binds in vivo to poly(A)+ RNA. It is the vertebrate homologue of the yeast protein Mex67p.^[2][3] The encoded protein overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses.^[4] A variant allele of the homologous Nxf1 gene in mice suppresses a class of mutations caused by integration of an endogenous retrovirus (intracisternal A particle) into an intron.^[5][6]

Interactions

NXF1 has been shown to interact with TNPO2,^[7] MAGOH,^[8] U2 small nuclear RNA auxiliary factor 1,^[9] DHX9,^[10] HuD^[11] and NUP214.^[12][13]

References

1. ^ Yoon DW, Lee H, Seol W, DeMaria M, Rosenzweig M, Jung JU (May 1997). "Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation". Immunity 6 (5): 571–82. doi:10.1016/S1074-7613(00)80345-3. PMID 9175835. 
2. ^ ^{a b} Grüter P, Tabernero C, von Kobbe C, et al. (April 1998). "TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus". Mol. Cell 1 (5): 649–59. doi:10.1016/S1097-2765(00)80065-9. PMID 9660949. 
3. ^ Katahira J, Strässer K, Podtelejnikov A, Mann M, Jung JU, Hurt E (May 1999). "The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human". EMBO J. 18 (9): 2593–609. doi:10.1093/emboj/18.9.2593. PMC 1171339. PMID 10228171. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171339. 
4. ^ "Entrez Gene: NXF1 nuclear RNA export factor 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10482. 
5. ^ Floyd JA, Gold DA, Concepcion D, Poon TH, Wang X, Keithley E, Chen D, Ward EJ, Chinn SB, Friedman RA, Yu HT, Moriwaki K, Shiroishi T, Hamilton BA (November 2003). "A natural allele of Nxf1 suppresses retrovirus insertional mutations". Nat. Genet. 35 (3): 221–8. doi:10.1038/ng1247. PMC 2756099. PMID 14517553. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2756099. 
6. ^ Concepcion D, Flores-García L, Hamilton BA (May 2009). Frankel, Wayne N.. ed. "Multipotent genetic suppression of retrotransposon-induced mutations by Nxf1 through fine-tuning of alternative splicing". PLoS Genet. 5 (5): e1000484. doi:10.1371/journal.pgen.1000484. PMC 2674570. PMID 19436707. http://www.plosgenetics.org/article/info%3Adoi%2F10.1371%2Fjournal.pgen.1000484. 
7. ^ Shamsher, Monee K; Ploski Jonathan, Radu Aurelian (Oct. 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (22): 14195–9. doi:10.1073/pnas.212518199. ISSN 0027-8424. PMC 137860. PMID 12384575. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=137860. 
8. ^ Kataoka, N; Diem M D, Kim V N, Yong J, Dreyfuss G (Nov. 2001). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". EMBO J. (England) 20 (22): 6424–33. doi:10.1093/emboj/20.22.6424. ISSN 0261-4189. PMC 125744. PMID 11707413. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125744. 
9. ^ Zolotukhin, Andrei S; Tan Wei, Bear Jenifer, Smulevitch Sergey, Felber Barbara K (Feb. 2002). "U2AF participates in the binding of TAP (NXF1) to mRNA". J. Biol. Chem. (United States) 277 (6): 3935–42. doi:10.1074/jbc.M107598200. ISSN 0021-9258. PMID 11724776. 
10. ^ Tang, H; Wong-Staal F (Oct. 2000). "Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus". J. Biol. Chem. (UNITED STATES) 275 (42): 32694–700. doi:10.1074/jbc.M003933200. ISSN 0021-9258. PMID 10924507. 
11. ^ Saito, Kuniaki; Fujiwara Toshinobu, Katahira Jun, Inoue Kunio, Sakamoto Hiroshi (Aug. 2004). "TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD". Biochem. Biophys. Res. Commun. (United States) 321 (2): 291–7. doi:10.1016/j.bbrc.2004.06.140. ISSN 0006-291X. PMID 15358174. 
12. ^ Herold, A; Suyama M, Rodrigues J P, Braun I C, Kutay U, Carmo-Fonseca M, Bork P, Izaurralde E (Dec. 2000). "TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture". Mol. Cell. Biol. (UNITED STATES) 20 (23): 8996–9008. doi:10.1128/MCB.20.23.8996-9008.2000. ISSN 0270-7306. PMC 86553. PMID 11073998. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86553. 
13. ^ Schmitt, I; Gerace L (Nov. 2001). "In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap". J. Biol. Chem. (United States) 276 (45): 42355–63. doi:10.1074/jbc.M103916200. ISSN 0021-9258. PMID 11551912.