SMART: CRM1_C domain annotation

CRM1_C CRM1 C terminal

SMART accession number:	SM01102
Description:	CRM1 (also known as Exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This region forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat (PUBMED:15574331).
Interpro abstract (IPR014877):	CRM1 (also known as exportin1) mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES). CRM1 forms a complex with the NES containing protein and the small GTPase Ran. This entry represents the C-terminal domain of CRM1. It forms an alpha helical structure formed by six helical hairpin motifs that are structurally similar to the HEAT repeat, but share little sequence similarity to the HEAT repeat [(PUBMED:15574331)].
Family alignment:	View or

There are 189 CRM1_C domains in 189 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a CRM1_C domain in a specific node, click on it.

This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CRM1_C domain is also avaliable.

Useful shortcuts: Expand all nodes or Collapse tree
Go to specific node: Anopheles gambiae, Arabidopsis thaliana, 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.
- Petosa C et al.
- Architecture of CRM1/Exportin1 suggests how cooperativity is achievedduring formation of a nuclear export complex.
- Mol Cell. 2004; 16: 761-75
- Display abstract
- CRM1/Exportin1 mediates the nuclear export of proteins bearing aleucine-rich nuclear export signal (NES) by forming a cooperative ternarycomplex with the NES-bearing substrate and the small GTPase Ran. Wepresent a structural model of human CRM1 based on a combination of X-raycrystallography, homology modeling, and electron microscopy. Thearchitecture of CRM1 resembles that of the import receptor transportin1,with 19 HEAT repeats and a large loop implicated in Ran binding. Residuescritical for NES recognition are identified adjacent to the cysteineresidue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. Wepresent evidence that a conformational change of the Ran binding loopaccounts for the cooperativity of Ran- and substrate binding and for theselective enhancement of CRM1-mediated export by the cofactor RanBP3. Ourfindings indicate that a single architectural and mechanistic frameworkcan explain the divergent effects of RanGTP on substrate binding by manyimport and export receptors.
Structure (3D structures containing this domain)

Links (links to other resources describing this domain)
PFAM CRM1_C
INTERPRO IPR014877

PDB code	Main view	Title
1w9c		Proteolytic fragment of crm1 spanning six c-terminal heat repeats
3gb8		Crystal structure of crm1/snurportin-1 complex
3gjx		Crystal structure of the nuclear export complex crm1- snurportin1-rangtp

PFAM	CRM1_C
INTERPRO	IPR014877

CRM1_C

3D Structures of CRM1_C domains in PDB