IMA7_HUMAN
ID IMA7_HUMAN Reviewed; 536 AA.
AC O60684; B2RDC7; D3DPP5; Q5VVU3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Importin subunit alpha-7;
DE AltName: Full=Karyopherin subunit alpha-6;
GN Name=KPNA6; Synonyms=IPOA7;
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], FUNCTION, INTERACTION WITH KPNB1, AND TISSUE
RP SPECIFICITY.
RX PubMed=10523667; DOI=10.1128/mcb.19.11.7782;
RA Koehler M., Speck C., Christiansen M., Bischoff F.R., Prehn S., Haller H.,
RA Goerlich D., Hartmann E.;
RT "Evidence for distinct substrate specificities of importin alpha family
RT members in nuclear protein import.";
RL Mol. Cell. Biol. 19:7782-7791(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [7]
RP INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION).
RX PubMed=17928350; DOI=10.1128/jvi.01097-07;
RA Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F.;
RT "Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily
RT karyopherin alpha proteins with activated STAT1.";
RL J. Virol. 81:13469-13477(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-113, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. {ECO:0000269|PubMed:10523667}.
CC -!- SUBUNIT: Interacts with ZIC3 (By similarity). Forms a complex with
CC importin subunit beta-1. {ECO:0000250, ECO:0000269|PubMed:10523667}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24.
CC {ECO:0000269|PubMed:17928350}.
CC -!- INTERACTION:
CC O60684; X5D778: ANKRD11; NbExp=5; IntAct=EBI-359923, EBI-17183751;
CC O60684; Q92688: ANP32B; NbExp=3; IntAct=EBI-359923, EBI-762428;
CC O60684; Q96C86: DCPS; NbExp=5; IntAct=EBI-359923, EBI-3917181;
CC O60684; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-359923, EBI-6658203;
CC O60684; O14893: GEMIN2; NbExp=5; IntAct=EBI-359923, EBI-443648;
CC O60684; P01583: IL1A; NbExp=3; IntAct=EBI-359923, EBI-1749782;
CC O60684; Q14653: IRF3; NbExp=3; IntAct=EBI-359923, EBI-2650369;
CC O60684; O75564-2: JRK; NbExp=3; IntAct=EBI-359923, EBI-17181882;
CC O60684; Q92993: KAT5; NbExp=3; IntAct=EBI-359923, EBI-399080;
CC O60684; Q14974: KPNB1; NbExp=2; IntAct=EBI-359923, EBI-286758;
CC O60684; P20700: LMNB1; NbExp=3; IntAct=EBI-359923, EBI-968218;
CC O60684; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-359923, EBI-716006;
CC O60684; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-359923, EBI-3917542;
CC O60684; P46087: NOP2; NbExp=3; IntAct=EBI-359923, EBI-356811;
CC O60684; Q9UKX7: NUP50; NbExp=6; IntAct=EBI-359923, EBI-2371082;
CC O60684; Q9BUI4: POLR3C; NbExp=5; IntAct=EBI-359923, EBI-5452779;
CC O60684; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-359923, EBI-11956563;
CC O60684; P78424: POU6F2; NbExp=3; IntAct=EBI-359923, EBI-12029004;
CC O60684; O43148: RNMT; NbExp=3; IntAct=EBI-359923, EBI-877832;
CC O60684; Q15637: SF1; NbExp=4; IntAct=EBI-359923, EBI-744603;
CC O60684; Q16594: TAF9; NbExp=4; IntAct=EBI-359923, EBI-712521;
CC O60684; P03466: NP; Xeno; NbExp=5; IntAct=EBI-359923, EBI-2547640;
CC O60684; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-359923, EBI-6051231;
CC O60684; Q05322: VP24; Xeno; NbExp=7; IntAct=EBI-359923, EBI-6153153;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10523667}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AF060543; AAC15233.1; -; mRNA.
DR EMBL; AK315490; BAG37874.1; -; mRNA.
DR EMBL; BT009843; AAP88845.1; -; mRNA.
DR EMBL; AL445248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07567.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07568.1; -; Genomic_DNA.
DR EMBL; BC020520; AAH20520.1; -; mRNA.
DR CCDS; CCDS352.1; -.
DR RefSeq; NP_036448.1; NM_012316.4.
DR PDB; 4UAD; X-ray; 2.42 A; A=59-536.
DR PDB; 7RHT; X-ray; 2.50 A; A=59-536.
DR PDBsum; 4UAD; -.
DR PDBsum; 7RHT; -.
DR AlphaFoldDB; O60684; -.
DR SMR; O60684; -.
DR BioGRID; 117163; 142.
DR ComplexPortal; CPX-1064; Importin complex, KPNA6 variant.
DR DIP; DIP-27609N; -.
DR ELM; O60684; -.
DR IntAct; O60684; 87.
DR MINT; O60684; -.
DR STRING; 9606.ENSP00000362728; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O60684; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60684; -.
DR MetOSite; O60684; -.
DR PhosphoSitePlus; O60684; -.
DR SwissPalm; O60684; -.
DR BioMuta; KPNA6; -.
DR EPD; O60684; -.
DR jPOST; O60684; -.
DR MassIVE; O60684; -.
DR MaxQB; O60684; -.
DR PaxDb; O60684; -.
DR PeptideAtlas; O60684; -.
DR PRIDE; O60684; -.
DR ProteomicsDB; 49527; -.
DR Antibodypedia; 16877; 184 antibodies from 34 providers.
DR DNASU; 23633; -.
DR Ensembl; ENST00000373625.8; ENSP00000362728.3; ENSG00000025800.14.
DR GeneID; 23633; -.
DR KEGG; hsa:23633; -.
DR MANE-Select; ENST00000373625.8; ENSP00000362728.3; NM_012316.5; NP_036448.1.
DR UCSC; uc001bug.4; human.
DR CTD; 23633; -.
DR DisGeNET; 23633; -.
DR GeneCards; KPNA6; -.
DR HGNC; HGNC:6399; KPNA6.
DR HPA; ENSG00000025800; Low tissue specificity.
DR MIM; 610563; gene.
DR neXtProt; NX_O60684; -.
DR OpenTargets; ENSG00000025800; -.
DR PharmGKB; PA30190; -.
DR VEuPathDB; HostDB:ENSG00000025800; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; O60684; -.
DR OMA; SEAPMEG; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; O60684; -.
DR TreeFam; TF354205; -.
DR PathwayCommons; O60684; -.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR SignaLink; O60684; -.
DR SIGNOR; O60684; -.
DR BioGRID-ORCS; 23633; 105 hits in 1091 CRISPR screens.
DR ChiTaRS; KPNA6; human.
DR GeneWiki; KPNA6; -.
DR GenomeRNAi; 23633; -.
DR Pharos; O60684; Tbio.
DR PRO; PR:O60684; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60684; protein.
DR Bgee; ENSG00000025800; Expressed in buccal mucosa cell and 216 other tissues.
DR ExpressionAtlas; O60684; baseline and differential.
DR Genevisible; O60684; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0075506; P:entry of viral genome into host nucleus through nuclear pore complex via importin; IMP:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0019079; P:viral genome replication; IEA:Ensembl.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
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; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Host-virus interaction; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..536
FT /note="Importin subunit alpha-7"
FT /id="PRO_0000120729"
FT DOMAIN 1..60
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 76..115
FT /note="ARM 1; truncated"
FT REPEAT 116..159
FT /note="ARM 2"
FT REPEAT 160..204
FT /note="ARM 3"
FT REPEAT 205..243
FT /note="ARM 4"
FT REPEAT 244..288
FT /note="ARM 5"
FT REPEAT 289..328
FT /note="ARM 6"
FT REPEAT 329..370
FT /note="ARM 7"
FT REPEAT 371..410
FT /note="ARM 8"
FT REPEAT 411..453
FT /note="ARM 9"
FT REPEAT 457..502
FT /note="ARM 10; atypical"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..239
FT /note="NLS binding site (major)"
FT /evidence="ECO:0000250"
FT REGION 316..404
FT /note="NLS binding site (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 45..54
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:4UAD"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:4UAD"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:4UAD"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 368..376
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 392..408
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 423..427
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 435..455
FT /evidence="ECO:0007829|PDB:4UAD"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 467..472
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:4UAD"
FT HELIX 488..501
FT /evidence="ECO:0007829|PDB:4UAD"
SQ SEQUENCE 536 AA; 60030 MW; 9D0E27482B9BDED3 CRC64;
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
NTPRVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
EDVQEQAVWA LGNIAGDSSV CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSPKE SIRKEACWTI
SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQEGKRSG SGVNPYCGLI EEAYGLDKIE
FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
