ID IMA1_HUMAN Reviewed; 529 AA. AC P52292; B9EJD6; Q53YE3; Q6NVW7; Q9BRU5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 251. DE RecName: Full=Importin subunit alpha-1 {ECO:0000305}; DE AltName: Full=Karyopherin subunit alpha-2; DE AltName: Full=RAG cohort protein 1; DE AltName: Full=SRP1-alpha; GN Name=KPNA2 {ECO:0000312|HGNC:HGNC:6395}; Synonyms=RCH1, SRP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7754385; DOI=10.1126/science.7754385; RA Weis K., Mattaj I.W., Lamond A.I.; RT "Identification of hSRP1 alpha as a functional receptor for nuclear RT localization sequences."; RL Science 268:1049-1053(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-165. RX PubMed=11735022; DOI=10.1007/s004390100605; RA Doerr S., Schlicker M., Hansmann I.; RT "Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy repeat RT on chromosome 17q23-q24 and mutation analysis in patients with Russell- RT Silver syndrome."; RL Hum. Genet. 109:479-486(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-157 AND ASN-453. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-157; ARG-165 AND RP ASN-453. RC TISSUE=Bone marrow, and Testis; 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 [6] RP PROTEIN SEQUENCE OF 2-13; 69-101; 107-117; 239-258; 292-315; 354-388 AND RP 487-494, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-529. RC TISSUE=Cervix carcinoma; RX PubMed=8016130; DOI=10.1073/pnas.91.13.6156; RA Cuomo C.A., Kirch S.A., Gyuris J., Brent R., Oettinger M.A.; RT "Rch1, a protein that specifically interacts with the RAG-1 recombination- RT activating protein."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6156-6160(1994). RN [8] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=7604027; DOI=10.1073/pnas.92.14.6532; RA Moroianu J., Hijikata M., Blobel G., Radu A.; RT "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 RT or alpha 2 subunit binds nuclear localization signal and beta subunit RT interacts with peptide repeat-containing nucleoporins."; RL Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995). RN [9] RP DOMAIN IBB. RX PubMed=8617227; DOI=10.1002/j.1460-2075.1996.tb00531.x; RA Weis K., Ryder U., Lamond A.I.; RT "The conserved amino-terminal domain of hSRP1 alpha is essential for RT nuclear protein import."; RL EMBO J. 15:1818-1825(1996). RN [10] RP IDENTIFICATION IN A COMPLEX WITH RAN AND CSE1L. RX PubMed=9323134; DOI=10.1016/s0092-8674(00)80372-4; RA Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.; RT "Export of importin-alpha from the nucleus is mediated by a specific RT nuclear transport factor."; RL Cell 90:1061-1071(1997). RN [11] RP INTERACTION WITH EPSTEIN-BARR VIRUS EBNA1 (MICROBIAL INFECTION). RX PubMed=9020106; DOI=10.1074/jbc.272.7.3999; RA Fischer N., Kremmer E., Lautscham G., Mueller-Lantzsch N., Graesser F.A.; RT "Epstein-Barr virus nuclear antigen 1 forms a complex with the nuclear RT transporter karyopherin alpha2."; RL J. Biol. Chem. 272:3999-4005(1997). RN [12] RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION). RX PubMed=9463369; DOI=10.1093/emboj/17.4.909; RA Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L., RA Lane C.M., Moore M.S., Blobel G., Bukrinsky M.; RT "Viral protein R regulates nuclear import of the HIV-1 pre-integration RT complex."; RL EMBO J. 17:909-917(1998). RN [13] RP INTERACTION WITH XPO2/CSE1L. RX PubMed=9786944; DOI=10.1083/jcb.143.2.309; RA Herold A., Truant R., Wiegand H., Cullen B.R.; RT "Determination of the functional domain organization of the importin alpha RT nuclear import factor."; RL J. Cell Biol. 143:309-318(1998). RN [14] RP INTERACTION WITH EPSTEIN-BARR VIRUS EBNA1 (MICROBIAL INFECTION). RX PubMed=10612665; DOI=10.1006/viro.1999.0054; RA Ito S., Ikeda M., Kato N., Matsumoto A., Ishikawa Y., Kumakubo S., RA Yanagi K.; RT "Epstein-barr virus nuclear antigen-1 binds to nuclear transporter RT karyopherin alpha1/NPI-1 in addition to karyopherin alpha2/Rch1."; RL Virology 266:110-119(2000). RN [15] RP INTERACTION WITH ARL4A. RX PubMed=10980193; DOI=10.1074/jbc.m002470200; RA Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C., RA Patton W.A., Massenburg D., Moss J., Lee F.J.; RT "ARL4, an ARF-like protein that is developmentally regulated and localized RT to nuclei and nucleoli."; RL J. Biol. Chem. 275:37815-37823(2000). RN [16] RP INTERACTION WITH PLAG1. RX PubMed=11882654; DOI=10.1074/jbc.m112112200; RA Braem C.V., Kas K., Meyen E., Debiec-Rychter M., Van De Ven W.J.M., RA Voz M.L.; RT "Identification of a karyopherin alpha 2 recognition site in PLAG1, which RT functions as a nuclear localization signal."; RL J. Biol. Chem. 277:19673-19678(2002). RN [17] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line protein RT expression map database."; RL Proteomics 2:212-223(2002). RN [18] RP INTERACTION WITH NBN. RX PubMed=16188882; DOI=10.1074/jbc.m508425200; RA Tseng S.-F., Chang C.-Y., Wu K.-J., Teng S.-C.; RT "Importin KPNA2 is required for proper nuclear localization and multiple RT functions of NBS1."; RL J. Biol. Chem. 280:39594-39600(2005). RN [19] RP INTERACTION WITH APEX1. RX PubMed=15942031; DOI=10.1093/nar/gki641; RA Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.; RT "Analysis of nuclear transport signals in the human apurinic/apyrimidinic RT endonuclease (APE1/Ref1)."; RL Nucleic Acids Res. 33:3303-3312(2005). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [22] RP INTERACTION WITH SARS VIRUS ORF6 PROTEIN (MICROBIAL INFECTION), SUBCELLULAR RP LOCATION (MICROBIAL INFECTION), MUTAGENESIS OF 2-SER--ASP-80, AND RP INTERACTION WITH KPNB1. RX PubMed=17596301; DOI=10.1128/jvi.01012-07; RA Frieman M., Yount B., Heise M., Kopecky-Bromberg S.A., Palese P., RA Baric R.S.; RT "Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 RT function by sequestering nuclear import factors on the rough endoplasmic RT reticulum/Golgi membrane."; RL J. Virol. 81:9812-9824(2007). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [27] RP INTERACTION WITH SNAI1 AND SNAI2. RX PubMed=19386897; DOI=10.1242/jcs.041749; RA Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.; RT "Characterization of Snail nuclear import pathways as representatives of RT C2H2 zinc finger transcription factors."; RL J. Cell Sci. 122:1452-1460(2009). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] RP IDENTIFICATION IN COMPLEX WITH CRM1 AND VENEZUELAN EQUINE ENCEPHALITIS RP VIRUS CAPSID PROTEIN (MICROBIAL INFECTION). RX PubMed=20147401; DOI=10.1128/jvi.02554-09; RA Atasheva S., Fish A., Fornerod M., Frolova E.I.; RT "Venezuelan equine encephalitis virus capsid protein forms a tetrameric RT complex with CRM1 and importin alpha/beta that obstructs nuclear pore RT complex function."; RL J. Virol. 84:4158-4171(2010). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [32] RP INTERACTION 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 [33] RP INTERACTION WITH CTNNBL1. RX PubMed=21385873; DOI=10.1074/jbc.m110.208769; RA Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.; RT "CTNNBL1 is a novel nuclear localization sequence-binding protein that RT recognizes RNA-splicing factors CDC5L and Prp31."; RL J. Biol. Chem. 286:17091-17102(2011). RN [34] RP INTERACTION WITH FRG1. RX PubMed=21699900; DOI=10.1016/j.jmb.2011.06.014; RA Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K., Klooster R., RA Jones T.I., Bellini M., Levesque L., Brieher W.M., van der Maarel S.M., RA Jones P.L.; RT "Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA- RT associated and actin-bundling protein."; RL J. Mol. Biol. 411:397-416(2011). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-62, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [36] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [38] RP INTERACTION WITH BAG6. RX PubMed=29042515; DOI=10.1073/pnas.1702940114; RA Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.; RT "Structural basis for regulation of the nucleo-cytoplasmic distribution of RT Bag6 by TRC35."; RL Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017). RN [39] RP INTERACTION WITH ZIKA VIRUS RNA-DIRECTED RNA POLYMERASE NS5 (MICROBIAL RP INFECTION). RX PubMed=30848123; DOI=10.1021/acsinfecdis.8b00373; RA Ng I.H.W., Chan K.W., Tan M.J.A., Gwee C.P., Smith K.M., Jeffress S.J., RA Saw W.G., Swarbrick C.M.D., Watanabe S., Jans D.A., Grueber G., RA Forwood J.K., Vasudevan S.G.; RT "Zika Virus NS5 Forms Supramolecular Nuclear Bodies That Sequester RT Importin-alpha and Modulate the Host Immune and Pro-Inflammatory Response RT in Neuronal Cells."; RL ACS Infect. Dis. 5:932-948(2019). RN [40] RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION). RX PubMed=32979938; DOI=10.1016/j.celrep.2020.108234; RA Xia H., Cao Z., Xie X., Zhang X., Chen J.Y., Wang H., Menachery V.D., RA Rajsbaum R., Shi P.Y.; RT "Evasion of Type I Interferon by SARS-CoV-2."; RL Cell Rep. 33:108234-108234(2020). RN [41] RP INTERACTION WITH RSL1D1. RX PubMed=36647821; DOI=10.1172/jci159951; RA Wang W., Miyamoto Y., Chen B., Shi J., Diao F., Zheng W., Li Q., Yu L., RA Li L., Xu Y., Wu L., Mao X., Fu J., Li B., Yan Z., Shi R., Xue X., Mu J., RA Zhang Z., Wu T., Zhao L., Wang W., Zhou Z., Dong J., Li Q., Jin L., He L., RA Sun X., Lin G., Kuang Y., Wang L., Sang Q.; RT "Karyopherin alpha deficiency contributes to human preimplantation embryo RT arrest."; RL J. Clin. Invest. 133:0-0(2023). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 11-54. RX PubMed=10353244; DOI=10.1038/20367; RA Cingolani G., Petosa C., Weis K., Muller C.W.; RT "Structure of importin-beta bound to the IBB domain of importin-alpha."; RL Nature 399:221-229(1999). 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 (PubMed:17596301). Interacts with CC ANP32E (By similarity). Component of a complex containing CSE1L, RAN CC and KPNA2. Interacts directly with CSE1L. Interacts with PLAG1. CC Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N- CC terminus). Interacts with ARL4A, CTNNBL1 and NBN. Interacts with SNAI1 CC (via zinc fingers) and SNAI2 (via zinc fingers). Interacts with BAG6 CC (PubMed:29042515). Interacts with AIFM2; this interaction likely CC mediates the translocation of AIFM2 into the nucleus upon oxidative CC stress. Interacts with RSL1D1 (PubMed:36647821). {ECO:0000250, CC ECO:0000250|UniProtKB:P52293, ECO:0000269|PubMed:10980193, CC ECO:0000269|PubMed:11882654, ECO:0000269|PubMed:15942031, CC ECO:0000269|PubMed:16188882, ECO:0000269|PubMed:17596301, CC ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:21385873, CC ECO:0000269|PubMed:21454664, ECO:0000269|PubMed:21699900, CC ECO:0000269|PubMed:29042515, ECO:0000269|PubMed:36647821, CC ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:9323134, CC ECO:0000269|PubMed:9786944}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr. CC {ECO:0000269|PubMed:9463369}. CC -!- SUBUNIT: (Microbial infection) Part of a tetrameric complex composed of CC CRM1, importin alpha/beta dimer and the Venezuelan equine encephalitis CC virus (VEEV) capsid; this complex blocks the receptor-mediated CC transport through the nuclear pore. {ECO:0000269|PubMed:20147401}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-COV virus ORF6 CC protein; this interaction blocks the receptor-mediated transport CC through the nuclear pore. {ECO:0000269|PubMed:17596301}. CC -!- SUBUNIT: (Microbial infection) Interacts with Zika virus RNA-directed CC RNA polymerase NS5. {ECO:0000269|PubMed:30848123}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV-2 ORF6 protein; CC this interaction may inhibit IFN-beta production by blocking IRF3 CC nuclear translocation. {ECO:0000269|PubMed:32979938}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA1; CC this interaction allows the nuclear import of EBNA1. CC {ECO:0000269|PubMed:9020106}. CC -!- INTERACTION: CC P52292; P63010: AP2B1; NbExp=3; IntAct=EBI-349938, EBI-432924; CC P52292; P38398: BRCA1; NbExp=3; IntAct=EBI-349938, EBI-349905; CC P52292; Q96C86: DCPS; NbExp=3; IntAct=EBI-349938, EBI-3917181; CC P52292; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-349938, EBI-10172181; CC P52292; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-349938, EBI-740641; CC P52292; P07910: HNRNPC; NbExp=4; IntAct=EBI-349938, EBI-357966; CC P52292; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-349938, EBI-10172004; CC P52292; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-349938, EBI-769401; CC P52292; Q14653: IRF3; NbExp=2; IntAct=EBI-349938, EBI-2650369; CC P52292; P05412: JUN; NbExp=4; IntAct=EBI-349938, EBI-852823; CC P52292; Q14974: KPNB1; NbExp=10; IntAct=EBI-349938, EBI-286758; CC P52292; Q14974-1: KPNB1; NbExp=4; IntAct=EBI-349938, EBI-15488647; CC P52292; Q6A162: KRT40; NbExp=3; IntAct=EBI-349938, EBI-10171697; CC P52292; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-349938, EBI-741037; CC P52292; Q9Y5V3: MAGED1; NbExp=4; IntAct=EBI-349938, EBI-716006; CC P52292; Q99750: MDFI; NbExp=3; IntAct=EBI-349938, EBI-724076; CC P52292; P40692: MLH1; NbExp=9; IntAct=EBI-349938, EBI-744248; CC P52292; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-349938, EBI-10288852; CC P52292; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-349938, EBI-10172876; CC P52292; Q16236: NFE2L2; NbExp=4; IntAct=EBI-349938, EBI-2007911; CC P52292; Q9HAN9: NMNAT1; NbExp=8; IntAct=EBI-349938, EBI-3917542; CC P52292; Q9UKX7: NUP50; NbExp=9; IntAct=EBI-349938, EBI-2371082; CC P52292; P37198: NUP62; NbExp=3; IntAct=EBI-349938, EBI-347978; CC P52292; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-349938, EBI-10178410; CC P52292; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-349938, EBI-10171633; CC P52292; Q93062: RBPMS; NbExp=3; IntAct=EBI-349938, EBI-740322; CC P52292; P46063: RECQL; NbExp=2; IntAct=EBI-349938, EBI-2823728; CC P52292; O43148: RNMT; NbExp=3; IntAct=EBI-349938, EBI-877832; CC P52292; P29034: S100A2; NbExp=5; IntAct=EBI-349938, EBI-752230; CC P52292; P06703: S100A6; NbExp=3; IntAct=EBI-349938, EBI-352877; CC P52292; Q9UJW9: SERTAD3; NbExp=4; IntAct=EBI-349938, EBI-748621; CC P52292; Q15637: SF1; NbExp=5; IntAct=EBI-349938, EBI-744603; CC P52292; Q9UH99: SUN2; NbExp=3; IntAct=EBI-349938, EBI-1044964; CC P52292; O75478: TADA2A; NbExp=3; IntAct=EBI-349938, EBI-742268; CC P52292; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-349938, EBI-2130429; CC P52292; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-349938, EBI-739895; CC P52292; P0DTC6: 6; Xeno; NbExp=2; IntAct=EBI-349938, EBI-25475897; CC P52292; P03126: E6; Xeno; NbExp=2; IntAct=EBI-349938, EBI-1177242; CC P52292; P03101: L1; Xeno; NbExp=3; IntAct=EBI-349938, EBI-7362698; CC P52292; P03107: L2; Xeno; NbExp=3; IntAct=EBI-349938, EBI-7362531; CC P52292; Q6GQG6: npm2.L; Xeno; NbExp=2; IntAct=EBI-349938, EBI-8469111; CC P52292; K9N643: ORF4b; Xeno; NbExp=2; IntAct=EBI-349938, EBI-25641007; CC P52292; P04620: rev; Xeno; NbExp=2; IntAct=EBI-349938, EBI-10687101; CC P52292; A0A3G5BIZ0; Xeno; NbExp=6; IntAct=EBI-349938, EBI-25564606; CC P52292; P03070; Xeno; NbExp=2; IntAct=EBI-349938, EBI-617698; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027, CC ECO:0000269|PubMed:9020106}. Nucleus {ECO:0000269|PubMed:7604027, CC ECO:0000269|PubMed:9020106}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Golgi apparatus CC membrane {ECO:0000269|PubMed:17596301}. Note=(Microbial infection) CC Retained in ER/Golgi membranes upon interaction with SARS-COV virus CC ORF6 protein. {ECO:0000269|PubMed:17596301}. CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. 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 {ECO:0000269|PubMed:8617227}. 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 (By similarity). {ECO:0000250}. 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 (By similarity). {ECO:0000250}. CC -!- MASS SPECTROMETRY: Mass=57861.92; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11840567}; CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U28386; AAA69957.1; -; mRNA. DR EMBL; AJ303086; CAC83080.1; -; Genomic_DNA. DR EMBL; BT006665; AAP35311.1; -; mRNA. DR EMBL; CH471099; EAW89041.1; -; Genomic_DNA. DR EMBL; BC005978; AAH05978.1; -; mRNA. DR EMBL; BC067848; AAH67848.1; -; mRNA. DR EMBL; BC146905; AAI46906.1; -; mRNA. DR EMBL; U09559; AAA65700.1; -; mRNA. DR CCDS; CCDS32713.1; -. DR PIR; A56516; A56516. DR RefSeq; NP_001307540.1; NM_001320611.1. DR RefSeq; NP_002257.1; NM_002266.3. DR PDB; 1EFX; X-ray; 3.00 A; C=204-212. DR PDB; 1QGK; X-ray; 2.50 A; B=11-54. DR PDB; 1QGR; X-ray; 2.30 A; B=28-54. DR PDB; 3FEX; X-ray; 3.55 A; C=70-529. DR PDB; 3FEY; X-ray; 2.20 A; C=70-529. DR PDB; 3WPT; X-ray; 2.63 A; A/B=75-497. DR PDB; 4E4V; X-ray; 2.53 A; A/B=70-529. DR PDB; 4WV6; X-ray; 1.75 A; A=60-529. DR PDB; 5H43; X-ray; 2.30 A; A=70-497. DR PDB; 7CRU; X-ray; 2.80 A; A/C=73-529. DR PDB; 7N8J; X-ray; 3.20 A; A=76-529. DR PDB; 7N9H; X-ray; 2.20 A; C=70-497. DR PDB; 8FZK; X-ray; 2.10 A; A/B/C/D=71-529. DR PDBsum; 1EFX; -. DR PDBsum; 1QGK; -. DR PDBsum; 1QGR; -. DR PDBsum; 3FEX; -. DR PDBsum; 3FEY; -. DR PDBsum; 3WPT; -. DR PDBsum; 4E4V; -. DR PDBsum; 4WV6; -. DR PDBsum; 5H43; -. DR PDBsum; 7CRU; -. DR PDBsum; 7N8J; -. DR PDBsum; 7N9H; -. DR PDBsum; 8FZK; -. DR AlphaFoldDB; P52292; -. DR SASBDB; P52292; -. DR SMR; P52292; -. DR BioGRID; 110036; 500. DR ComplexPortal; CPX-1027; Importin complex, KPNA2 variant. DR CORUM; P52292; -. DR DIP; DIP-6205N; -. DR IntAct; P52292; 181. DR MINT; P52292; -. DR STRING; 9606.ENSP00000438483; -. DR BindingDB; P52292; -. DR ChEMBL; CHEMBL1741187; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; P52292; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P52292; -. DR PhosphoSitePlus; P52292; -. DR SwissPalm; P52292; -. DR BioMuta; KPNA2; -. DR DMDM; 1708480; -. DR CPTAC; CPTAC-232; -. DR CPTAC; CPTAC-233; -. DR EPD; P52292; -. DR jPOST; P52292; -. DR MassIVE; P52292; -. DR MaxQB; P52292; -. DR PaxDb; 9606-ENSP00000438483; -. DR PeptideAtlas; P52292; -. DR ProteomicsDB; 56475; -. DR Pumba; P52292; -. DR Antibodypedia; 4226; 493 antibodies from 45 providers. DR DNASU; 3838; -. DR Ensembl; ENST00000330459.8; ENSP00000332455.3; ENSG00000182481.10. DR Ensembl; ENST00000537025.6; ENSP00000438483.2; ENSG00000182481.10. DR Ensembl; ENST00000579754.2; ENSP00000462331.2; ENSG00000182481.10. DR Ensembl; ENST00000584026.6; ENSP00000463602.2; ENSG00000182481.10. DR Ensembl; ENST00000677086.1; ENSP00000504655.1; ENSG00000182481.10. DR Ensembl; ENST00000679078.1; ENSP00000504685.1; ENSG00000182481.10. DR GeneID; 3838; -. DR KEGG; hsa:3838; -. DR MANE-Select; ENST00000330459.8; ENSP00000332455.3; NM_002266.4; NP_002257.1. DR UCSC; uc002jgk.4; human. DR AGR; HGNC:6395; -. DR CTD; 3838; -. DR DisGeNET; 3838; -. DR GeneCards; KPNA2; -. DR HGNC; HGNC:6395; KPNA2. DR HPA; ENSG00000182481; Tissue enhanced (testis). DR MIM; 600685; gene. DR neXtProt; NX_P52292; -. DR OpenTargets; ENSG00000182481; -. DR PharmGKB; PA30186; -. DR VEuPathDB; HostDB:ENSG00000182481; -. DR eggNOG; KOG0166; Eukaryota. DR GeneTree; ENSGT01050000244891; -. DR HOGENOM; CLU_018084_6_1_1; -. DR InParanoid; P52292; -. DR OMA; IVPICIR; -. DR OrthoDB; 916229at2759; -. DR PhylomeDB; P52292; -. DR TreeFam; TF101178; -. DR PathwayCommons; P52292; -. DR Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways. DR Reactome; R-HSA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde. DR Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; P52292; -. DR SIGNOR; P52292; -. DR BioGRID-ORCS; 3838; 108 hits in 1164 CRISPR screens. DR ChiTaRS; KPNA2; human. DR EvolutionaryTrace; P52292; -. DR GeneWiki; Karyopherin_alpha_2; -. DR GenomeRNAi; 3838; -. DR Pharos; P52292; Tbio. DR PRO; PR:P52292; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P52292; Protein. DR Bgee; ENSG00000182481; Expressed in ventricular zone and 98 other cell types or tissues. DR ExpressionAtlas; P52292; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043657; C:host cell; IEA:GOC. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal. DR GO; GO:0031965; C:nuclear membrane; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL. DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:UniProt. DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc. 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; IDA:UniProtKB. DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:MGI. DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProt. DR GO; GO:0000018; P:regulation of DNA recombination; TAS:ProtInc. DR Gene3D; 1.20.5.690; Importin-alpha, importin-beta-binding domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID00153; -. 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 PANTHER; PTHR23316; IMPORTIN ALPHA; 1. DR PANTHER; PTHR23316:SF12; IMPORTIN SUBUNIT ALPHA-1; 1. DR Pfam; PF00514; Arm; 7. 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; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 5. DR PROSITE; PS51214; IBB; 1. DR SWISS-2DPAGE; P52292; -. DR Genevisible; P52292; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Endoplasmic reticulum; Golgi apparatus; Host-virus interaction; Membrane; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT CHAIN 2..529 FT /note="Importin subunit alpha-1" FT /id="PRO_0000120722" 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 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 43..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 142..238 FT /note="NLS binding site (major)" FT /evidence="ECO:0000250" FT REGION 315..403 FT /note="NLS binding site (minor)" FT /evidence="ECO:0000250" FT MOTIF 45..54 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 55..72 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT MOD_RES 62 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT VARIANT 157 FT /note="A -> V (in dbSNP:rs17850032)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_067625" FT VARIANT 165 FT /note="P -> R (in dbSNP:rs11545989)" FT /evidence="ECO:0000269|PubMed:11735022, FT ECO:0000269|PubMed:15489334" FT /id="VAR_013137" FT VARIANT 365 FT /note="G -> S (in dbSNP:rs1059558)" FT /id="VAR_067626" FT VARIANT 453 FT /note="K -> N (in dbSNP:rs17850031)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_067627" FT MUTAGEN 2..80 FT /note="Missing: Complete loss of binding to KPNB1." FT /evidence="ECO:0000269|PubMed:17596301" FT CONFLICT 182 FT /note="A -> D (in Ref. 5; AAH67848)" FT /evidence="ECO:0000305" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1QGK" FT TURN 18..21 FT /evidence="ECO:0007829|PDB:1QGK" FT HELIX 30..48 FT /evidence="ECO:0007829|PDB:1QGR" FT HELIX 74..85 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 90..104 FT /evidence="ECO:0007829|PDB:4WV6" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:3FEY" FT HELIX 112..117 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 121..128 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 134..148 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 152..160 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 163..170 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 176..190 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 194..202 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 206..213 FT /evidence="ECO:0007829|PDB:4WV6" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:5H43" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 223..236 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 246..259 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 265..278 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 283..290 FT /evidence="ECO:0007829|PDB:4WV6" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 295..302 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 307..320 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 325..333 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 336..339 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 340..344 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 349..362 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 367..375 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 379..388 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 391..407 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 410..418 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 422..427 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 434..454 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 457..466 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 469..475 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:4WV6" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:3WPT" FT HELIX 482..495 FT /evidence="ECO:0007829|PDB:4WV6" SQ SEQUENCE 529 AA; 57862 MW; B0F94A0475B80EED CRC64; MSTNENANTP AARLHRFKNK GKDSTEMRRR RIEVNVELRK AKKDDQMLKR RNVSSFPDDA TSPLQENRNN QGTVNWSVDD IVKGINSSNV ENQLQATQAA RKLLSREKQP PIDNIIRAGL IPKFVSFLGR TDCSPIQFES AWALTNIASG TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSVFRDLV IKYGAVDPLL ALLAVPDMSS LACGYLRNLT WTLSNLCRNK NPAPPIDAVE QILPTLVRLL HHDDPEVLAD TCWAISYLTD GPNERIGMVV KTGVVPQLVK LLGASELPIV TPALRAIGNI VTGTDEQTQV VIDAGALAVF PSLLTNPKTN IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVSVLSKAD FKTQKEAVWA VTNYTSGGTV EQIVYLVHCG IIEPLMNLLT AKDTKIILVI LDAISNIFQA AEKLGETEKL SIMIEECGGL DKIEALQNHE NESVYKASLS LIEKYFSVEE EEDQNVVPET TSEGYTFQVQ DGAPGTFNF //