词条 | NXF1 |
释义 |
FunctionThis 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] InteractionsNXF1 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] Tap proteinIn molecular biology, another name for the protein NXF1 is TAP. In particular this entry focuses on the C-terminal domain, which also contains the UBA(protein domain). {{Infobox protein family| Symbol = TAP_C | Name = TAP_C | image = PDB 1oai EBI.jpg | width = | caption = complex between tap uba domain and fxfg nucleoporin peptide | Pfam = PF03943 | Pfam_clan = CL0214 | InterPro = IPR005637 | SMART = | PROSITE = | MEROPS = | SCOP = 1go5 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} This entry contains the NXF family of shuttling transport receptors for nuclear export of mRNA, which include:
The Tap-C domain is made of four alpha helices packed against each other. The arrangement of helices 1, 2 and 3 is similar to that seen in a UBA fold. and is joined to the next module by flexible 12-residue Pro-rich linker.[14][15] FunctionNuclear export of mRNAs is mediated by the Tap protein. StructureTap can form a multimeric complex with itself and with other members of the NXF family. Three functional domains of Tap have been well characterized: the RNA-binding domain, the Nuclear Transport Factor 2 (NTF2)-like domain, and the ubiquitin-associated (UBA) domain. References1. ^{{cite journal |vauthors=Yoon DW, Lee H, Seol W, DeMaria M, Rosenzweig M, Jung JU | title = Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation | journal = Immunity | volume = 6 | issue = 5 | pages = 571–82 |date=May 1997 | pmid = 9175835 | doi = 10.1016/S1074-7613(00)80345-3 | url = }} {{PDB_Gallery|geneid=10482}}2. ^1 {{cite journal |vauthors=Grüter P, Tabernero C, von Kobbe C, etal | title = TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus | journal = Mol. Cell | volume = 1 | issue = 5 | pages = 649–59 |date=April 1998 | pmid = 9660949 | doi = 10.1016/S1097-2765(00)80065-9 | url = }} 3. ^{{cite journal |vauthors=Katahira J, Strässer K, Podtelejnikov A, Mann M, Jung JU, Hurt E | title = The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human | journal = EMBO J. | volume = 18 | issue = 9 | pages = 2593–609 |date=May 1999 | pmid = 10228171 | pmc = 1171339 | doi = 10.1093/emboj/18.9.2593 | url = | issn = }} 4. ^{{cite web | title = Entrez Gene: NXF1 nuclear RNA export factor 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10482| accessdate = }} 5. ^{{cite journal |vauthors=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 | title = A natural allele of Nxf1 suppresses retrovirus insertional mutations | journal = Nat. Genet. | volume = 35 | issue = 3 | pages = 221–8 |date=November 2003 | pmid = 14517553 | doi = 10.1038/ng1247 | url = | pmc = 2756099 }} 6. ^{{cite journal | vauthors = Concepcion D, Flores-García L, Hamilton BA | title = Multipotent genetic suppression of retrotransposon-induced mutations by Nxf1 through fine-tuning of alternative splicing | journal = PLoS Genetics | volume = 5 | issue = 5 | pages = e1000484 | date = May 2009 | pmid = 19436707 | pmc = 2674570 | doi = 10.1371/journal.pgen.1000484}} 7. ^{{cite journal |last=Shamsher |first=Monee K |authorlink= |author2=Ploski Jonathan |author3=Radu Aurelian |date=October 2002 |title=Karyopherin beta 2B participates in mRNA export from the nucleus |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue=22 |pages=14195–9 | issn = 0027-8424| pmid = 12384575 |doi = 10.1073/pnas.212518199 | bibcode =2002PNAS...9914195S | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=137860 }} 8. ^{{cite journal |last=Kataoka |first=N |authorlink= |author2=Diem M D |author3=Kim V N |author4=Yong J |author5=Dreyfuss G |date=November 2001 |title=Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex |journal=EMBO J. |volume=20 |issue=22 |pages=6424–33 | issn = 0261-4189| pmid = 11707413 |doi = 10.1093/emboj/20.22.6424 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=125744 }} 9. ^{{cite journal |last=Zolotukhin |first=Andrei S |authorlink= |author2=Tan Wei |author3=Bear Jenifer |author4=Smulevitch Sergey |author5=Felber Barbara K |date=February 2002 |title=U2AF participates in the binding of TAP (NXF1) to mRNA |journal=J. Biol. Chem. |volume=277 |issue=6 |pages=3935–42 | issn = 0021-9258| pmid = 11724776 |doi = 10.1074/jbc.M107598200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }} 10. ^{{cite journal |last=Tang |first=H |authorlink= |author2=Wong-Staal F |date=October 2000 |title=Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus |journal=J. Biol. Chem. |volume=275 |issue=42 |pages=32694–700 | issn = 0021-9258| pmid = 10924507 |doi = 10.1074/jbc.M003933200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }} 11. ^{{cite journal |last=Saito |first=Kuniaki |authorlink= |author2=Fujiwara Toshinobu |author3=Katahira Jun |author4=Inoue Kunio |author5=Sakamoto Hiroshi |date=August 2004 |title=TAP/NXF1, the primary mRNA export receptor, specifically interacts with a neuronal RNA-binding protein HuD |journal=Biochem. Biophys. Res. Commun. |volume=321 |issue=2 |pages=291–7 | issn = 0006-291X| pmid = 15358174 |doi = 10.1016/j.bbrc.2004.06.140 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }} 12. ^{{cite journal |last=Herold |first=A |authorlink= |author2=Suyama M |author3=Rodrigues J P |author4=Braun I C |author5=Kutay U |author6=Carmo-Fonseca M |author7=Bork P |author8=Izaurralde E |date=December 2000 |title=TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture |journal=Mol. Cell. Biol. |volume=20 |issue=23 |pages=8996–9008 | issn = 0270-7306| pmid = 11073998 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1128/MCB.20.23.8996-9008.2000 |pmc=86553 }} 13. ^{{cite journal |last=Schmitt |first=I |authorlink= |author2=Gerace L |date=November 2001 |title=In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap |journal=J. Biol. Chem. |volume=276 |issue=45 |pages=42355–63 | issn = 0021-9258| pmid = 11551912 |doi = 10.1074/jbc.M103916200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }} 14. ^1 {{cite journal |vauthors=Grant RP, Hurt E, Neuhaus D, Stewart M | title = Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1 | journal = Nat. Struct. Biol. | volume = 9 | issue = 4 | pages = 247–51 |date=April 2002 | pmid = 11875519 | doi = 10.1038/nsb773 | url = }} 15. ^1 {{cite journal |vauthors=Suyama M, Doerks T, Braun IC, Sattler M, Izaurralde E, Bork P | title = Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins | journal = EMBO Rep. | volume = 1 | issue = 1 | pages = 53–8 |date=July 2000 | pmid = 11256625 | pmc = 1083685 | doi = 10.1038/sj.embor.embor627 | url = | doi-broken-date = 2019-02-22 }} |
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