SMART: TAP_C domain annotation

TAP_C C-terminal domain of vertebrate Tap protein

SMART accession number:	SM00804
Description:	The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for the nuclear export of mRNA. Its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate shuttling. This domain forms a compact four-helix fold related to that of a UBA domain.
Interpro abstract (IPR005637):	The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling [(PUBMED:11875519)]. The structure of the C-terminal domain is composed of four helices [(PUBMED:11875519)]. The structure is related to the UBA domain.
GO process:	mRNA transport (GO:0051028)
GO component:	nucleus (GO:0005634)
Family alignment:	View or

There are 190 TAP_C domains in 190 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with TAP_C domain is also avaliable.

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Go to specific node: Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: transport
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Grant RP, Hurt E, Neuhaus D, Stewart M
- Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.
- Nat Struct Biol. 2002; 9: 247-51
- Display abstract
- The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four alpha-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.
Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM TAP_C
INTERPRO IPR005637

PDB code	Main view	Title
1go5		Structure of the c-terminal fg-binding domain of human tap
1jkg		Structural basis for the recognition of a nucleoporin fg- repeat by the ntf2-like domain of tap-p15 mrna nuclear export factor
1jn5		Structural basis for the recognition of a nucleoporin fg- repeat by the ntf2-like domain of tap-p15 mrna export factor
1oai		Complex between tap uba domain and fxfg nucleoporin peptide
2jp7		Nmr structure of the mex67 uba domain
2khh		Structural requirements for the uba domain of the mrna export factor mex67 to bind its specific targets, the transcription elongation tho complex component hpr1 and nucleoporin fxfg repeats

PFAM	TAP_C
INTERPRO	IPR005637

TAP_C

3D Structures of TAP_C domains in PDB