[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=9154134 [NCBI, ExPASy, EBI, Israel, Japan]
Takeda S.,
Fujiwara T.,
Shimizu F.,
Kawai A.,
Shinomiya K.,
Okuno S.,
Ozaki K.,
Katagiri T.,
Shimada Y.,
Nagata M.,
Watanabe T.,
Takaichi A.,
Kuga Y.,
Suzuki M.,
Hishigaki H.,
Takahashi E.,
Shin S.,
Nakamura Y.,
Hirai Y.;
"Isolation and mapping of karyopherin alpha 3 (KPNA3), a human gene that is highly homologous to genes encoding Xenopus importin, yeast SRP1 and human RCH1.";
Cytogenet. Cell Genet. 76:87-93(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
DOI=10.1016/S0014-5793(97)01265-9; PubMed=9395085 [NCBI, ExPASy, EBI, Israel, Japan]
Koehler M.,
Ansieau S.,
Prehn S.,
Leutz A.,
Haller H.,
Hartmann E.;
"Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family.";
FEBS Lett. 417:104-108(1997).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.95.2.582; PubMed=9435235 [NCBI, ExPASy, EBI, Israel, Japan]
Nachury M.V.,
Ryder U.W.,
Lamond A.I.,
Weis K.;
"Cloning and characterization of hSRP1 gamma, a tissue-specific nuclear transport factor.";
Proc. Natl. Acad. Sci. U.S.A. 95:582-587(1998).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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INTERACTION WITH INFLUENZA VIRUS NP.
DOI=10.1074/jbc.M303571200; PubMed=12740372 [NCBI, ExPASy, EBI, Israel, Japan]
Melen K.,
Fagerlund R.,
Franke J.,
Koehler M.,
Kinnunen L.,
Julkunen I.;
"Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein.";
J. Biol. Chem. 278:28193-28200(2003).
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[6]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G.,
Ye M.,
Zhou H.,
Jiang X.,
Feng S.,
Jiang X.,
Tian R.,
Wan D.,
Zou H.,
Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
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- FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9.
- SUBUNIT: Forms a complex with importin subunit beta-1.
- INTERACTION:
P06914:- (xeno); NbExp=1; IntAct=EBI-358297, EBI-1555692;
P49407:ARRB1; NbExp=1; IntAct=EBI-358297, EBI-743313;
P32121:ARRB2; NbExp=1; IntAct=EBI-358297, EBI-714559;
P46527:CDKN1B; NbExp=1; IntAct=EBI-358297, EBI-519280;
- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity).
- TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart and skeletal muscle.
- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
- DOMAIN: The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity).
- DOMAIN: The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity).
- SIMILARITY: Belongs to the importin alpha family.
- SIMILARITY: Contains 10 ARM repeats.
- SIMILARITY: Contains 1 IBB domain.
- CAUTION: PubMed:9395085 termed this protein 'importin alpha-4'.
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