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) ].
GO function:	nuclear export signal receptor activity (GO:0005049)
Family alignment:	View or

There are 1759 CRM1_C domains in 1757 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CRM1_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CRM1_C domain is also avaliable.

Click on the protein counts, or double click on taxonomic names to display all proteins containing CRM1_C domain in the selected taxonomic class.
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)

3D Structures of CRM1_C domains in PDB

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
3m1i		Crystal structure of yeast CRM1 (Xpo1p) in complex with yeast RanBP1 (Yrb1p) and yeast RanGTP (Gsp1pGTP)
3nby		Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex
3nbz		Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal I)
3nc0		Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II)
3nc1		Crystal structure of the CRM1-RanGTP complex
3vyc		Crystal structure of unliganded Saccharomyces cerevisiae CRM1 (Xpo1p)
3wyf		3WYF
3wyg		3WYG
4bsm		Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.5A
4bsn		Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1A
4fgv		Crystal structure of free CRM1 (crystal form 1)
4gmx		Crystal structure of KPT185 in complex with CRM1-Ran-RanBP1
4gpt		Crystal structure of KPT251 in complex with CRM1-Ran-RanBP1
4hat		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
4hau		Crystal structure of CRM1 inhibitor Ratjadone A in complex with CRM1-Ran-RanBP1
4hav		Crystal structure of CRM1 inhibitor Anguinomycin A in complex with CRM1-Ran-RanBP1
4haw		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K548A)-Ran-RanBP1
4hax		Crystal structure of CRM1 inhibitor Ratjadone A in complex with CRM1(K579A)-Ran-RanBP1
4hay		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K548E,K579Q)-Ran-RanBP1
4haz		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(R543S,K548E,K579Q)-Ran-RanBP1
4hb0		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(K541Q,K542Q,R543S,K545Q,K548Q,K579Q)-Ran-RanBP1
4hb2		Crystal structure of CRM1-Ran-RanBP1
4hb3		Crystal structure of CRM1(T539S)-Ran-RanBP1 with weakly bound unmodeled Leptomycin B
4hb4		Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1(537DLTVK541/GLCEQ)-Ran-RanBP1
4hzk		Crystal structure of free CRM1 (crystal form 2)
4wvf		4WVF
5dh9		5DH9
5dha		5DHA
5dhf		5DHF
5di9		5DI9
5dif		5DIF
5dis		5DIS
5jlj		5JLJ

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

PFAM	CRM1_C
INTERPRO	IPR014877

CRM1_C

Taxonomic distribution of proteins containing CRM1_C domain.

3D Structures of CRM1_C domains in PDB