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| PROSITE documentation PDOC51281 |
TAP C-terminal (TAP-C) domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Suyama M. Doerks T. Braun I.C. Sattler M. Izaurralde E. Bork P. |
| Title | Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins. | |
| Source | EMBO Rep. 1:53-58(2000). | |
| PubMed ID | 11256625 | |
| DOI | 10.1038/sj.embor.embor627 |
| 2 | Authors | Grant R.P. Hurt E. Neuhaus D. Stewart M. |
| Title | Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. | |
| Source | Nat. Struct. Biol. 9:247-251(2002). | |
| PubMed ID | 11875519 | |
| DOI | 10.1038/nsb773 |
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