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PROSITE documentation PDOC51281

TAP C-terminal (TAP-C) domain profile





Description

The NXF family of shuttling transport receptors for nuclear export of mRNA includes:

  • vertebrate mRNA export factor TAP or nuclear RNA export factor 1 (NXF1).
  • Caenorhabditis elegans nuclear RNA export factor 1 (nxf-1).
  • yeast mRNA export factor MEX67.

Members of the NXF family have a modular structure. A nuclear localization sequence and a noncanonical RNA recognition motif (RRM) (see <PDOC00030>) followed by four LRR repeats are located in its N-terminal half. The C-terminal half contains a NTF2 domain (see <PDOC50177>) followed by a second domain. This most C-terminal TAP-C domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling [1,2].

The Tap-C domain is made of four α helices packed against each other (see <PDB:1GO5>). 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 [1,2].

The profile we developed covers the entire TAP-C domain.

Last update:

December 2006 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

TAP_C, PS51281; TAP C-terminal (TAP-C) domain profile  (MATRIX)


References

1AuthorsSuyama M. Doerks T. Braun I.C. Sattler M. Izaurralde E. Bork P.
TitlePrediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins.
SourceEMBO Rep. 1:53-58(2000).
PubMed ID11256625
DOI10.1038/sj.embor.embor627

2AuthorsGrant R.P. Hurt E. Neuhaus D. Stewart M.
TitleStructure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.
SourceNat. Struct. Biol. 9:247-251(2002).
PubMed ID11875519
DOI10.1038/nsb773



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