Summary: Importin-beta N-terminal domain
This is the Wikipedia entry entitled "Importin". More...
Does Pfam agree with the content of the Wikipedia entry ?
Editing Wikipedia articles
Before you edit for the first time
You should take a few minutes to view the following pages:
How your contribution will be recorded
Importin Edit Wikipedia article
|Importin beta binding domain|
|mouse importin alpha-nucleoplasmin nls peptide complex|
|Importin-beta N-terminal domain|
|structure of the karyopherin beta2-ran gppnhp nuclear transport complex|
Importin is a type of protein that moves other protein molecules into the nucleus by binding to a specific recognition sequence, called the nuclear localization signal (NLS). Importin is classified as a karyopherin.
Importin has two subunits, importin α and importin β. Members of the importin-beta family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. The NLS-Importin α-Importin β trimer dissociates after binding to Ran GTP inside the nucleus. Proteins can contain one (monopartite) or two (bipartite) NLS motifs. Importin-alpha contains several armadillo (ARM) repeats, which produce a curving structure with two NLS-binding sites, a major one close to the N terminus and a minor one close to the C terminus. Importin alpha also contains an N-terminal importin beta binding domain that contains an auto-regulatory region. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins, which is important for importin-beta mediated transport.
Ran GTPase helps to control the unidirectional transfer of cargo. The cytoplasm contains primarily RanGDP and the nucleus RanGTP through the actions of RanGAP and RanGEF, respectively. In the nucleus, RanGTP binds to importin-beta within the importin/cargo complex, causing a conformational change in importin-beta that releases it from importin-alpha-bound cargo. The N-terminal importin-beta-binding (IBB) domain of importin-alpha contains an auto-regulatory region that mimics the NLS motif. The release of importin-beta frees the auto-regulatory region on importin-alpha to loop back and bind to the major NLS-binding site, causing the cargo to be released.
 Human importin genes
- Importin: IPO4, IPO7, IPO8, IPO9, IPO11, IPO13
- Karyopherin-α: KPNA1, KPNA2, KPNA3, KPNA4, KPNA5, KPNA6
- Karyopherin-β: KPNB1
- Görlich D, Prehn S, Laskey RA, Hartmann E (1994). "Isolation of a protein that is essential for the first step of nuclear protein import". Cell 79 (5): 767–78. doi:10.1016/0092-8674(94)90067-1. PMID 8001116.
- Mattaj IW, Englmeier L (1998). "Nucleocytoplasmic transport: the soluble phase". Annu. Rev. Biochem. 67: 265–306. doi:10.1146/annurev.biochem.67.1.265. PMID 9759490.
- Moroianu J, Blobel G, Radu A (1996). "The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence.". Proc Natl Acad Sci U S A 93 (13): 6572–6. doi:10.1073/pnas.93.13.6572. PMC 39066. PMID 8692858. //www.ncbi.nlm.nih.gov/pmc/articles/PMC39066/.
- Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M (December 2002). "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta". J. Biol. Chem. 277 (52): 50597–606. doi:10.1074/jbc.M209037200. PMID 12372823.
- Isgro TA, Schulten K (February 2007). "Association of nuclear pore FG-repeat domains to NTF2 import and export complexes". J. Mol. Biol. 366 (1): 330–45. doi:10.1016/j.jmb.2006.11.048. PMID 17161424.
- Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, Corbett AH (February 2007). "Classical nuclear localization signals: definition, function, and interaction with importin alpha". J. Biol. Chem. 282 (8): 5101–5. doi:10.1074/jbc.R600026200. PMID 17170104.
|This protein-related article is a stub. You can help Wikipedia by expanding it.|
Importin-beta N-terminal domain Provide feedback
No Pfam abstract.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001494
Karyopherins are a group of proteins involved in transporting molecules through the pores of the nuclear envelope. Karyopherins, which may act as importins or exportins, are part of the Importin-beta super-family, which all share a similar three-dimensional structure.
Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins [PUBMED:12372823, PUBMED:17161424], which is important for importin-beta mediated transport.
Ran GTPase helps to control the unidirectional transfer of cargo. The cytoplasm contains primarily RanGDP and the nucleus RanGTP through the actions of RanGAP and RanGEF, respectively. In the nucleus, RanGTP binds to importin-beta within the importin/cargo complex, causing a conformational change in importin-beta that releases it from importin-alpha-bound cargo. As a result, the N-terminal auto-inhibitory region on importin-alpha is free to loop back and bind to the major NLS-binding site, causing the cargo to be released [PUBMED:17170104]. There are additional release factors as well.
This entry represents the N-terminal domain of karyopherins that is important for the binding of the Ran protein [PUBMED:10367892].
More information about these proteins can be found at Protein of the Month: Importins [PUBMED:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||protein transporter activity (GO:0008565)|
|Biological process||intracellular protein transport (GO:0006886)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Loading domain graphics...
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
If you find these logos useful in your own work, please consider citing the following article:
Note: You can also download the data file for the tree.
Curation and family details
|Number in seed:||52|
|Number in full:||2930|
|Average length of the domain:||72.40 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||7.63 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
There are 4 interactions for this family. More...
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IBN_N domain has been found. There are 59 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...