IMA1_MOUSE
ID IMA1_MOUSE Reviewed; 529 AA.
AC P52293; Q64292;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Importin subunit alpha-1 {ECO:0000305};
DE AltName: Full=Importin alpha P1;
DE AltName: Full=Karyopherin subunit alpha-2;
DE AltName: Full=Pendulin;
DE AltName: Full=Pore targeting complex 58 kDa subunit;
DE Short=PTAC58;
DE AltName: Full=RAG cohort protein 1;
DE AltName: Full=SRP1-alpha;
GN Name=Kpna2 {ECO:0000312|MGI:MGI:103561}; Synonyms=Rch1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7641681; DOI=10.1002/j.1460-2075.1995.tb00031.x;
RA Imamoto N., Shimamoto T., Takao T., Tachibana T., Kose S., Matsubae M.,
RA Sekimoto T., Shimonishi Y., Yoneda Y.;
RT "In vivo evidence for involvement of a 58 kDa component of nuclear pore-
RT targeting complex in nuclear protein import.";
RL EMBO J. 14:3617-3626(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7565597; DOI=10.1007/bf02191602;
RA Kuessel P., Frasch M.;
RT "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is
RT required for normal migration, division, and integrity of nuclei during
RT mitosis.";
RL Mol. Gen. Genet. 248:351-363(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8631802; DOI=10.1074/jbc.271.13.7654;
RA Prieve M.G., Guttridge K.L., Waterman M.L.;
RT "The nuclear localization signal of lymphoid enhancer factor-1 is
RT recognized by two differentially expressed Srp1-nuclear localization
RT sequence receptor proteins.";
RL J. Biol. Chem. 271:7654-7658(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH ANP32E.
RX PubMed=10692581; DOI=10.1016/s0014-5793(00)01218-7;
RA Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.;
RT "Characterization of the nuclear transport of a novel leucine-rich acidic
RT nuclear protein-like protein.";
RL FEBS Lett. 468:171-175(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTS WITH SNAI1.
RX PubMed=21454664; DOI=10.1074/jbc.m110.213579;
RA Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.;
RT "Importin alpha protein acts as a negative regulator for Snail protein
RT nuclear import.";
RL J. Biol. Chem. 286:15126-15131(2011).
RN [8]
RP INTERACTION WITH AIFM2.
RX PubMed=26689472; DOI=10.1016/j.freeradbiomed.2015.12.002;
RA Miriyala S., Thippakorn C., Chaiswing L., Xu Y., Noel T., Tovmasyan A.,
RA Batinic-Haberle I., Vander Kooi C.W., Chi W., Latif A.A., Panchatcharam M.,
RA Prachayasittikul V., Butterfield D.A., Vore M., Moscow J., St Clair D.K.;
RT "Novel role of 4-hydroxy-2-nonenal in AIFm2-mediated mitochondrial stress
RT signaling.";
RL Free Radic. Biol. Med. 91:68-80(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 72-497, AND NUCLEAR LOCALIZATION
RP SIGNAL RECOGNITION.
RX PubMed=10764582; DOI=10.1006/jmbi.2000.3642;
RA Fontes M.R., Teh T., Kobe B.;
RT "Structural basis of recognition of monopartite and bipartite nuclear
RT localization sequences by mammalian importin-alpha.";
RL J. Mol. Biol. 297:1183-1194(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-496, NUCLEAR LOCALIZATION
RP SIGNAL, AND AUTOINHIBITION.
RX PubMed=10201409; DOI=10.1038/7625;
RA Kobe B.;
RT "Autoinhibition by an internal nuclear localization signal revealed by the
RT crystal structure of mammalian importin alpha.";
RL Nat. Struct. Biol. 6:388-397(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-54, AND AUTOINHIBITION.
RX PubMed=11448961; DOI=10.1074/jbc.m103531200;
RA Catimel B., Teh T., Fontes M.R., Jennings I.G., Jans D.A., Howlett G.J.,
RA Nice E.C., Kobe B.;
RT "Biophysical characterization of interactions involving importin-alpha
RT during nuclear import.";
RL J. Biol. Chem. 276:34189-34198(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-498 IN COMPLEX WITH NUP50.
RX PubMed=16222336; DOI=10.1038/sj.emboj.7600843;
RA Matsuura Y., Stewart M.;
RT "Nup50/Npap60 function in nuclear protein import complex disassembly and
RT importin recycling.";
RL EMBO J. 24:3681-3689(2005).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter protein for
CC nuclear receptor KPNB1. Binds specifically and directly to substrates
CC containing either a simple or bipartite NLS motif. Docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) is
CC mediated by KPNB1 through binding to nucleoporin FxFG repeats and the
CC complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the
CC NPC, Ran binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus.
CC -!- SUBUNIT: Heterodimer; with KPNB1 (By similarity). Component of a
CC complex containing CSE1L, RAN and KPNA2 (By similarity). Interacts
CC directly with CSE1L (By similarity). Interacts with PLAG1 (By
CC similarity). Interacts with APEX1 (via N-terminus) (By similarity).
CC Interacts with FRG1 (via N-terminus) (By similarity). Interacts with
CC ARL4A, CTNNBL1 and NBN (By similarity). Interacts with ANP32E
CC (PubMed:10692581). Interacts with SNAI1 (via zinc fingers)
CC (PubMed:21454664). Interacts with SNAI2 (via zinc fingers) (By
CC similarity). Interacts with BAG6 (By similarity). Interacts with AIFM2;
CC this interaction likely mediates the translocation of AIFM2 into the
CC nucleus upon oxidative stress. {ECO:0000250|UniProtKB:P52292,
CC ECO:0000269|PubMed:10692581, ECO:0000269|PubMed:21454664,
CC ECO:0000269|PubMed:26689472}.
CC -!- INTERACTION:
CC P52293; P01580: Ifng; NbExp=5; IntAct=EBI-3043908, EBI-7892102;
CC P52293; Q9BYF1: ACE2; Xeno; NbExp=4; IntAct=EBI-3043908, EBI-7730807;
CC P52293; B4LTG5: Dvir\dUTPase; Xeno; NbExp=6; IntAct=EBI-3043908, EBI-9821342;
CC P52293; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-3043908, EBI-6051231;
CC P52293; P29034: S100A2; Xeno; NbExp=2; IntAct=EBI-3043908, EBI-752230;
CC P52293; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-3043908, EBI-744603;
CC P52293; Q3SYU7: TNPO1; Xeno; NbExp=3; IntAct=EBI-3043908, EBI-8469003;
CC P52293; P03070; Xeno; NbExp=3; IntAct=EBI-3043908, EBI-617698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52292}. Nucleus
CC {ECO:0000250|UniProtKB:P52292}.
CC -!- TISSUE SPECIFICITY: Slightly detected in brain but not in cerebellum
CC and skeletal muscle, highly expressed in testis and spleen.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic
CC central region composed of 10 repeats, and a short hydrophilic C-
CC terminus. The N-terminal hydrophilic region contains the importin beta
CC binding domain (IBB domain), which is sufficient for binding importin
CC beta and essential for nuclear protein import.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal autoinhibitory
CC NLS. Binding of KPNB1 probably overlaps the internal NLS and
CC contributes to a high affinity for cytoplasmic NLS-containing cargo
CC substrates. After dissociation of the importin/substrate complex in the
CC nucleus the internal autohibitory NLS contributes to a low affinity for
CC nuclear NLS-containing proteins.
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved in
CC recognition of simple or bipartite NLS motifs. Structurally located
CC within in a helical surface groove they contain several conserved Trp
CC and Asn residues of the corresponding third helices (H3) of ARM repeats
CC which mainly contribute to binding.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; D55720; BAA09536.1; -; mRNA.
DR EMBL; U12270; AAA85281.1; -; mRNA.
DR EMBL; U34229; AAC52451.1; -; mRNA.
DR EMBL; BC003274; AAH03274.1; -; mRNA.
DR EMBL; BC006720; AAH06720.1; -; mRNA.
DR CCDS; CCDS25565.1; -.
DR PIR; S57345; S57345.
DR PIR; S57873; S57873.
DR PIR; S62116; S62116.
DR RefSeq; NP_034785.1; NM_010655.3.
DR PDB; 1EJL; X-ray; 2.80 A; I=70-529.
DR PDB; 1EJY; X-ray; 2.90 A; I=70-529.
DR PDB; 1IAL; X-ray; 2.50 A; A=44-496.
DR PDB; 1IQ1; X-ray; 2.80 A; A/B=44-54, C=70-529.
DR PDB; 1PJM; X-ray; 2.50 A; B=70-529.
DR PDB; 1PJN; X-ray; 2.50 A; B=70-529.
DR PDB; 1Q1S; X-ray; 2.30 A; C=70-529.
DR PDB; 1Q1T; X-ray; 2.50 A; C=70-529.
DR PDB; 1Y2A; X-ray; 2.20 A; C=70-497.
DR PDB; 2C1M; X-ray; 2.20 A; A=75-498.
DR PDB; 2YNR; X-ray; 2.30 A; A=72-496.
DR PDB; 3BTR; X-ray; 2.60 A; C=70-496.
DR PDB; 3KND; X-ray; 2.15 A; A=70-529.
DR PDB; 3L3Q; X-ray; 2.30 A; A=71-497.
DR PDB; 3OQS; X-ray; 2.00 A; A=70-529.
DR PDB; 3Q5U; X-ray; 2.50 A; A=70-529.
DR PDB; 3RZ9; X-ray; 2.29 A; A=70-529.
DR PDB; 3RZX; X-ray; 2.61 A; A=70-529.
DR PDB; 3TPM; X-ray; 2.10 A; A=75-496.
DR PDB; 3TPO; X-ray; 2.10 A; A=1-529.
DR PDB; 3UKW; X-ray; 2.10 A; B=70-529.
DR PDB; 3UKX; X-ray; 2.20 A; B=70-529.
DR PDB; 3UKY; X-ray; 2.35 A; B=70-529.
DR PDB; 3UKZ; X-ray; 2.30 A; B=70-529.
DR PDB; 3UL0; X-ray; 2.00 A; B=70-529.
DR PDB; 3UL1; X-ray; 1.90 A; B=70-529.
DR PDB; 3UVU; X-ray; 2.38 A; A=70-529.
DR PDB; 3VE6; X-ray; 2.83 A; A=71-496.
DR PDB; 3ZIN; X-ray; 2.00 A; A=72-496.
DR PDB; 3ZIO; X-ray; 2.10 A; A=72-496.
DR PDB; 3ZIP; X-ray; 2.40 A; A=72-497.
DR PDB; 3ZIQ; X-ray; 2.10 A; A=72-497.
DR PDB; 3ZIR; X-ray; 2.30 A; A=72-497.
DR PDB; 4BA3; X-ray; 2.10 A; A=70-529.
DR PDB; 4HTV; X-ray; 3.00 A; A=70-528.
DR PDB; 4MZ5; X-ray; 2.10 A; E=70-528.
DR PDB; 4MZ6; X-ray; 1.88 A; E=70-528.
DR PDB; 4OIH; X-ray; 2.10 A; A=70-529.
DR PDB; 4U54; X-ray; 2.41 A; A=74-498.
DR PDB; 4U58; X-ray; 2.56 A; A=72-497.
DR PDB; 4U5L; X-ray; 2.53 A; A=72-497.
DR PDB; 4U5N; X-ray; 2.31 A; A=72-497.
DR PDB; 4U5O; X-ray; 2.00 A; A=72-497.
DR PDB; 4U5S; X-ray; 2.12 A; A=72-497.
DR PDB; 4U5U; X-ray; 1.96 A; A=72-497.
DR PDB; 4U5V; X-ray; 1.97 A; A=72-497.
DR PDB; 4UAF; X-ray; 1.70 A; B=69-529.
DR PDB; 4YI0; X-ray; 1.81 A; C=70-529.
DR PDB; 4ZDU; X-ray; 2.30 A; A=72-498.
DR PDB; 5B56; X-ray; 2.30 A; A/B=70-529.
DR PDB; 5CTT; X-ray; 1.70 A; A=72-497.
DR PDB; 5D5K; X-ray; 1.90 A; C=70-529.
DR PDB; 5E6Q; X-ray; 2.31 A; B=70-529.
DR PDB; 5EKF; X-ray; 2.00 A; A=70-529.
DR PDB; 5EKG; X-ray; 2.80 A; A=70-529.
DR PDB; 5FC8; X-ray; 2.10 A; E=71-529.
DR PDB; 5GXW; X-ray; 2.39 A; A=70-497.
DR PDB; 5HHG; X-ray; 2.20 A; E=71-497.
DR PDB; 5HUW; X-ray; 1.95 A; C=2-529.
DR PDB; 5HUY; X-ray; 1.98 A; C=2-529.
DR PDB; 5K9S; X-ray; 2.40 A; A=72-529.
DR PDB; 5KLR; X-ray; 2.20 A; B=70-529.
DR PDB; 5KLT; X-ray; 2.60 A; B=70-529.
DR PDB; 5SVZ; X-ray; 2.00 A; A=70-529.
DR PDB; 5U5P; X-ray; 2.17 A; A=70-529.
DR PDB; 5U5R; X-ray; 2.10 A; A=70-529.
DR PDB; 5UMZ; X-ray; 1.90 A; B=70-528.
DR PDB; 5V5O; X-ray; 2.24 A; C=2-529.
DR PDB; 5V5P; X-ray; 2.15 A; C=2-529.
DR PDB; 5W41; X-ray; 2.20 A; A=70-529.
DR PDB; 5W4E; X-ray; 2.18 A; B=37-529.
DR PDB; 5W4F; X-ray; 1.98 A; B=70-529.
DR PDB; 5W4G; X-ray; 2.04 A; B=70-529.
DR PDB; 5WUM; X-ray; 2.00 A; A=70-529.
DR PDB; 5WUN; X-ray; 2.20 A; A=70-529.
DR PDB; 5X8N; X-ray; 2.15 A; A=70-529.
DR PDB; 6BVT; X-ray; 2.50 A; E=70-529.
DR PDB; 6BW0; X-ray; 2.10 A; E=70-529.
DR PDB; 6BW1; X-ray; 2.20 A; E=70-529.
DR PDB; 6D7M; X-ray; 2.19 A; B=37-529.
DR PDB; 6D7N; X-ray; 2.30 A; B=70-529.
DR PDB; 6IU7; X-ray; 1.90 A; A=72-498.
DR PDB; 6IUA; X-ray; 1.70 A; A=72-498.
DR PDB; 6IW8; X-ray; 2.80 A; C=70-498.
DR PDB; 6IWA; X-ray; 2.40 A; C=70-498.
DR PDB; 6K06; X-ray; 1.75 A; C=70-498.
DR PDB; 6MJL; X-ray; 2.50 A; B=72-497.
DR PDB; 6P6A; X-ray; 2.15 A; B=70-529.
DR PDB; 6P6E; X-ray; 1.99 A; A=70-529.
DR PDB; 6WBA; X-ray; 2.15 A; A=70-529.
DR PDB; 6WBB; X-ray; 2.66 A; I=70-529.
DR PDB; 6WBC; X-ray; 2.15 A; A=70-529.
DR PDB; 6WX7; X-ray; 2.70 A; A=70-529.
DR PDB; 7JJM; X-ray; 2.06 A; B=62-529.
DR PDB; 7JK7; X-ray; 1.96 A; B=62-529.
DR PDB; 7JVO; X-ray; 2.20 A; A=70-529.
DR PDB; 7L04; X-ray; 2.26 A; E=70-529.
DR PDB; 7LEQ; X-ray; 2.24 A; E=70-497.
DR PDB; 7LET; X-ray; 2.40 A; E=70-497.
DR PDB; 7LEU; X-ray; 2.82 A; E=70-497.
DR PDB; 7M60; X-ray; 2.30 A; A=70-529.
DR PDB; 7RFX; X-ray; 2.10 A; A=70-529.
DR PDB; 7RFZ; X-ray; 1.95 A; A=70-529.
DR PDB; 7RG0; X-ray; 2.00 A; A=70-529.
DR PDB; 7RG1; X-ray; 1.85 A; A=70-529.
DR PDB; 7RG2; X-ray; 2.00 A; A=70-529.
DR PDB; 7RG3; X-ray; 2.00 A; A=70-529.
DR PDB; 7RG4; X-ray; 2.60 A; E=70-529.
DR PDB; 7RG6; X-ray; 2.10 A; A=70-529.
DR PDBsum; 1EJL; -.
DR PDBsum; 1EJY; -.
DR PDBsum; 1IAL; -.
DR PDBsum; 1IQ1; -.
DR PDBsum; 1PJM; -.
DR PDBsum; 1PJN; -.
DR PDBsum; 1Q1S; -.
DR PDBsum; 1Q1T; -.
DR PDBsum; 1Y2A; -.
DR PDBsum; 2C1M; -.
DR PDBsum; 2YNR; -.
DR PDBsum; 3BTR; -.
DR PDBsum; 3KND; -.
DR PDBsum; 3L3Q; -.
DR PDBsum; 3OQS; -.
DR PDBsum; 3Q5U; -.
DR PDBsum; 3RZ9; -.
DR PDBsum; 3RZX; -.
DR PDBsum; 3TPM; -.
DR PDBsum; 3TPO; -.
DR PDBsum; 3UKW; -.
DR PDBsum; 3UKX; -.
DR PDBsum; 3UKY; -.
DR PDBsum; 3UKZ; -.
DR PDBsum; 3UL0; -.
DR PDBsum; 3UL1; -.
DR PDBsum; 3UVU; -.
DR PDBsum; 3VE6; -.
DR PDBsum; 3ZIN; -.
DR PDBsum; 3ZIO; -.
DR PDBsum; 3ZIP; -.
DR PDBsum; 3ZIQ; -.
DR PDBsum; 3ZIR; -.
DR PDBsum; 4BA3; -.
DR PDBsum; 4HTV; -.
DR PDBsum; 4MZ5; -.
DR PDBsum; 4MZ6; -.
DR PDBsum; 4OIH; -.
DR PDBsum; 4U54; -.
DR PDBsum; 4U58; -.
DR PDBsum; 4U5L; -.
DR PDBsum; 4U5N; -.
DR PDBsum; 4U5O; -.
DR PDBsum; 4U5S; -.
DR PDBsum; 4U5U; -.
DR PDBsum; 4U5V; -.
DR PDBsum; 4UAF; -.
DR PDBsum; 4YI0; -.
DR PDBsum; 4ZDU; -.
DR PDBsum; 5B56; -.
DR PDBsum; 5CTT; -.
DR PDBsum; 5D5K; -.
DR PDBsum; 5E6Q; -.
DR PDBsum; 5EKF; -.
DR PDBsum; 5EKG; -.
DR PDBsum; 5FC8; -.
DR PDBsum; 5GXW; -.
DR PDBsum; 5HHG; -.
DR PDBsum; 5HUW; -.
DR PDBsum; 5HUY; -.
DR PDBsum; 5K9S; -.
DR PDBsum; 5KLR; -.
DR PDBsum; 5KLT; -.
DR PDBsum; 5SVZ; -.
DR PDBsum; 5U5P; -.
DR PDBsum; 5U5R; -.
DR PDBsum; 5UMZ; -.
DR PDBsum; 5V5O; -.
DR PDBsum; 5V5P; -.
DR PDBsum; 5W41; -.
DR PDBsum; 5W4E; -.
DR PDBsum; 5W4F; -.
DR PDBsum; 5W4G; -.
DR PDBsum; 5WUM; -.
DR PDBsum; 5WUN; -.
DR PDBsum; 5X8N; -.
DR PDBsum; 6BVT; -.
DR PDBsum; 6BW0; -.
DR PDBsum; 6BW1; -.
DR PDBsum; 6D7M; -.
DR PDBsum; 6D7N; -.
DR PDBsum; 6IU7; -.
DR PDBsum; 6IUA; -.
DR PDBsum; 6IW8; -.
DR PDBsum; 6IWA; -.
DR PDBsum; 6K06; -.
DR PDBsum; 6MJL; -.
DR PDBsum; 6P6A; -.
DR PDBsum; 6P6E; -.
DR PDBsum; 6WBA; -.
DR PDBsum; 6WBB; -.
DR PDBsum; 6WBC; -.
DR PDBsum; 6WX7; -.
DR PDBsum; 7JJM; -.
DR PDBsum; 7JK7; -.
DR PDBsum; 7JVO; -.
DR PDBsum; 7L04; -.
DR PDBsum; 7LEQ; -.
DR PDBsum; 7LET; -.
DR PDBsum; 7LEU; -.
DR PDBsum; 7M60; -.
DR PDBsum; 7RFX; -.
DR PDBsum; 7RFZ; -.
DR PDBsum; 7RG0; -.
DR PDBsum; 7RG1; -.
DR PDBsum; 7RG2; -.
DR PDBsum; 7RG3; -.
DR PDBsum; 7RG4; -.
DR PDBsum; 7RG6; -.
DR AlphaFoldDB; P52293; -.
DR SMR; P52293; -.
DR BioGRID; 201007; 27.
DR ComplexPortal; CPX-1054; Importin complex, KPNA2 variant.
DR CORUM; P52293; -.
DR DIP; DIP-47774N; -.
DR ELM; P52293; -.
DR IntAct; P52293; 16.
DR MINT; P52293; -.
DR STRING; 10090.ENSMUSP00000018506; -.
DR iPTMnet; P52293; -.
DR PhosphoSitePlus; P52293; -.
DR SwissPalm; P52293; -.
DR EPD; P52293; -.
DR PaxDb; P52293; -.
DR PeptideAtlas; P52293; -.
DR PRIDE; P52293; -.
DR ProteomicsDB; 267239; -.
DR DNASU; 16647; -.
DR Ensembl; ENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
DR Ensembl; ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
DR GeneID; 16647; -.
DR KEGG; mmu:16647; -.
DR UCSC; uc007lzz.1; mouse.
DR CTD; 3838; -.
DR MGI; MGI:103561; Kpna2.
DR VEuPathDB; HostDB:ENSMUSG00000018362; -.
DR VEuPathDB; HostDB:ENSMUSG00000066878; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244891; -.
DR HOGENOM; CLU_018084_6_1_1; -.
DR InParanoid; P52293; -.
DR OMA; CSELPIM; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; P52293; -.
DR TreeFam; TF101178; -.
DR Reactome; R-MMU-5693548; Sensing of DNA Double Strand Breaks.
DR BioGRID-ORCS; 16647; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Kpna2; mouse.
DR EvolutionaryTrace; P52293; -.
DR PRO; PR:P52293; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P52293; protein.
DR Bgee; ENSMUSG00000018362; Expressed in animal zygote and 165 other tissues.
DR ExpressionAtlas; P52293; baseline and differential.
DR Genevisible; P52293; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098892; C:extrinsic component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISO:MGI.
DR GO; GO:0075506; P:entry of viral genome into host nucleus through nuclear pore complex via importin; IMP:MGI.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISO:MGI.
DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:MGI.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR GO; GO:0046015; P:regulation of transcription by glucose; ISO:MGI.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID50009; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 6.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52292"
FT CHAIN 2..529
FT /note="Importin subunit alpha-1"
FT /id="PRO_0000120723"
FT DOMAIN 2..60
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 71..111
FT /note="ARM 1; truncated"
FT REPEAT 112..151
FT /note="ARM 2"
FT REPEAT 152..193
FT /note="ARM 3"
FT REPEAT 200..244
FT /note="ARM 4"
FT REPEAT 246..282
FT /note="ARM 5"
FT REPEAT 283..322
FT /note="ARM 6"
FT REPEAT 325..364
FT /note="ARM 7"
FT REPEAT 367..409
FT /note="ARM 8"
FT REPEAT 410..456
FT /note="ARM 9"
FT REPEAT 457..496
FT /note="ARM 10; atypical"
FT REGION 45..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..238
FT /note="NLS binding site (major)"
FT REGION 315..403
FT /note="NLS binding site (minor)"
FT MOTIF 45..54
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:10201409,
FT ECO:0000269|PubMed:10764582"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P52292"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 242
FT /note="P -> S (in Ref. 2; AAA85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="H -> P (in Ref. 2; AAA85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="G -> R (in Ref. 2; AAA85281)"
FT /evidence="ECO:0000305"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3TPO"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2YNR"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1Q1S"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6K06"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:4UAF"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 307..320
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 391..407
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 434..454
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 457..466
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:5HUY"
FT HELIX 482..495
FT /evidence="ECO:0007829|PDB:4UAF"
SQ SEQUENCE 529 AA; 57928 MW; 19E64AA3E9C3C7B5 CRC64;
MSTNENANLP AARLNRFKNK GKDSTEMRRR RIEVNVELRK AKKDEQMLKR RNVSSFPDDA
TSPLQENRNN QGTVNWSVED IVKGINSNNL ESQLQATQAA RKLLSREKQP PIDNIIRAGL
IPKFVSFLGK TDCSPIQFES AWALTNIASG TSEQTKAVVD GGAIPAFISL LASPHAHISE
QAVWALGNIA GDGSAFRDLV IKHGAIDPLL ALLAVPDLST LACGYLRNLT WTLSNLCRNK
NPAPPLDAVE QILPTLVRLL HHNDPEVLAD SCWAISYLTD GPNERIEMVV KKGVVPQLVK
LLGATELPIV TPALRAIGNI VTGTDEQTQK VIDAGALAVF PSLLTNPKTN IQKEATWTMS
NITAGRQDQI QQVVNHGLVP FLVGVLSKAD FKTQKEAAWA ITNYTSGGTV EQIVYLVHCG
IIEPLMNLLS AKDTKIIQVI LDAISNIFQA AEKLGETEKL SIMIEECGGL DKIEALQRHE
NESVYKASLN LIEKYFSVEE EEDQNVVPET TSEGFAFQVQ DGAPGTFNF
