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41  structures 301  species 0  interactions 914  sequences 16  architectures

Family: IBB (PF01749)

Summary: Importin beta binding domain

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This is the Wikipedia entry entitled "Importin". More...

Importin Edit Wikipedia article

Importin beta binding domain
PDB 1ejy EBI.jpg
mouse importin alpha-nucleoplasmin nls peptide complex
Identifiers
Symbol IBB
Pfam PF01749
Pfam clan CL0020
InterPro IPR002652
SCOP 1bk5
SUPERFAMILY 1bk5
Importin-beta N-terminal domain
PDB 1qbk EBI.jpg
structure of the karyopherin beta2-ran gppnhp nuclear transport complex
Identifiers
Symbol IBN_N
Pfam PF03810
Pfam clan CL0020
InterPro IPR001494
SCOP 1qbk
SUPERFAMILY 1qbk

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.[1][2]

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.[3] 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.[4] 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.[5][6]

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.[4] 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.[7]

Human importin genes[edit]

References[edit]

  1. ^ http://big.mcw.edu/display.php/1053.html
  2. ^ 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. 
  3. ^ 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. 
  4. ^ a b 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR002652 This article incorporates text from the public domain Pfam and InterPro IPR001494

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Importin beta binding domain Provide feedback

This family consists of the importin alpha (karyopherin alpha), importin beta (karyopherin beta) binding domain. The domain mediates formation of the importin alpha beta complex; required for classical NLS import of proteins into the nucleus, through the nuclear pore complex and across the nuclear envelope. Also in the alignment is the NLS of importin alpha which overlaps with the IBB domain [4].

Literature references

  1. Conti E, Uy M, Leighton L, Blobel G, Kuriyan J; , Cell 1998;94:193-204.: Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. PUBMED:9695948 EPMC:9695948

  2. Weis K; , Trends Biochem Sci 1998;23:185-189.: Importins and exportins: how to get in and out of the nucleus [published erratum appears in Trends Biochem Sci 1998 Jul;23(7):235] PUBMED:9612083 EPMC:9612083

  3. Gorlich D; , EMBO J 1998;17:2721-2727.: Transport into and out of the cell nucleus. PUBMED:9582265 EPMC:9582265

  4. Moroianu J, Blobel G, Radu A; , Proc Natl Acad Sci U S A 1996;93:6572-6576.: The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. PUBMED:8692858 EPMC:8692858

  5. Gorlich D, Henklein P, Laskey RA, Hartmann E; , EMBO J 1996;15:1810-1817.: A 41 amino acid motif in importin-alpha confers binding to importin- beta and hence transit into the nucleus. PUBMED:8617226 EPMC:8617226


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002652

The exchange of macromolecules between the nucleus and cytoplasm takes place through nuclear pore complexes within the nuclear membrane. Active transport of large molecules through these pore complexes require carrier proteins, called karyopherins (importins and exportins), which shuttle between the two compartments.

Members of the importin-alpha (karyopherin-alpha) family can form heterodimers with importin-beta. 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. 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.

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 [PUBMED:8692858]. 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 [PUBMED:17170104].

This entry represents the N-terminal IBB domain of importin-alpha that contains the auto-regulatory region.

More information about these proteins can be found at Protein of the Month: Importins [PUBMED:].

Gene Ontology

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Domain organisation

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Alignments

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(18)
Full
(914)
Representative proteomes NCBI
(813)
Meta
(4)
RP15
(157)
RP35
(244)
RP55
(397)
RP75
(568)
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Format an alignment

  Seed
(18)
Full
(914)
Representative proteomes NCBI
(813)
Meta
(4)
RP15
(157)
RP35
(244)
RP55
(397)
RP75
(568)
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  Seed
(18)
Full
(914)
Representative proteomes NCBI
(813)
Meta
(4)
RP15
(157)
RP35
(244)
RP55
(397)
RP75
(568)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

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Seed source: Pfam-B_544 (release 4.2)
Previous IDs: none
Type: Family
Author: Bashton M, Bateman A
Number in seed: 18
Number in full: 914
Average length of the domain: 92.30 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 18.60 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.8 23.8
Trusted cut-off 23.8 24.0
Noise cut-off 23.7 23.7
Model length: 97
Family (HMM) version: 15
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Structures

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 IBB domain has been found. There are 41 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.

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