IMA3_HUMAN
ID IMA3_HUMAN Reviewed; 521 AA.
AC O00629; A8K4S6; D3DNM2; O00190;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Importin subunit alpha-3;
DE AltName: Full=Importin alpha Q1;
DE Short=Qip1;
DE AltName: Full=Karyopherin subunit alpha-4;
GN Name=KPNA4; Synonyms=QIP1;
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=9168958; DOI=10.1006/bbrc.1997.6535;
RA Seki T., Tada S., Katada T., Enomoto T.;
RT "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1:
RT discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact
RT with DNA helicase Q1/RecQL.";
RL Biochem. Biophys. Res. Commun. 234:48-53(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9395085; DOI=10.1016/s0014-5793(97)01265-9;
RA Koehler M., Ansieau S., Prehn S., Leutz A., Haller H., Hartmann E.;
RT "Cloning of two novel human importin-alpha subunits and analysis of the
RT expression pattern of the importin-alpha protein family.";
RL FEBS Lett. 417:104-108(1997).
RN [3]
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 INTERACTION WITH HCMV UL84.
RX PubMed=12610148; DOI=10.1128/jvi.77.6.3734-3748.2003;
RA Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.;
RT "A nonconventional nuclear localization signal within the UL84 protein of
RT human cytomegalovirus mediates nuclear import via the importin alpha/beta
RT pathway.";
RL J. Virol. 77:3734-3748(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, 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 [11]
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 [12]
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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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 [16]
RP INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=23864635; DOI=10.1128/jvi.00786-13;
RA Cohen M.J., Yousef A.F., Massimi P., Fonseca G.J., Todorovic B., Pelka P.,
RA Turnell A.S., Banks L., Mymryk J.S.;
RT "Dissection of the C-terminal region of E1A redefines the roles of CtBP and
RT other cellular targets in oncogenic transformation.";
RL J. Virol. 87:10348-10355(2013).
RN [17]
RP INTERACTION WITH CHIKUNGUNYA VIRUS CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=23984714; DOI=10.1186/1743-422x-10-269;
RA Thomas S., Rai J., John L., Schaefer S., Puetzer B.M., Herchenroeder O.;
RT "Chikungunya virus capsid protein contains nuclear import and export
RT signals.";
RL Virol. J. 10:269-269(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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).
RN [19]
RP INTERACTION WITH MERS VIRUS PROTEIN ORF4B.
RX PubMed=29370303; DOI=10.1371/journal.ppat.1006838;
RA Canton J., Fehr A.R., Fernandez-Delgado R., Gutierrez-Alvarez F.J.,
RA Sanchez-Aparicio M.T., Garcia-Sastre A., Perlman S., Enjuanes L., Sola I.;
RT "MERS-CoV 4b protein interferes with the NF-kappaB-dependent innate immune
RT response during infection.";
RL PLoS Pathog. 14:E1006838-E1006838(2018).
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. In vitro, mediates the nuclear import of
CC human cytomegalovirus UL84 by recognizing a non-classical NLS. In
CC vitro, mediates the nuclear import of human cytomegalovirus UL84 by
CC recognizing a non-classical NLS.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. Interacts with
CC SNAI1. Interacts with TALDO1 isoform 1 (By similarity).
CC {ECO:0000250|UniProtKB:O35343, ECO:0000269|PubMed:12610148,
CC ECO:0000269|PubMed:21454664}.
CC -!- SUBUNIT: (Microbial infection) Interacts with MERS virus protein OF4b;
CC this interaction prevents the translocation of NF-kappa-B complex to
CC the nucleus. {ECO:0000250|UniProtKB:O35343,
CC ECO:0000269|PubMed:29370303}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1A
CC protein; this interaction allows E1A import into the host nucleus.
CC {ECO:0000269|PubMed:23864635}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Chikungunya virus capsid
CC protein; this interaction allows the nuclear import of the viral capsid
CC protein. {ECO:0000269|PubMed:23984714}.
CC -!- INTERACTION:
CC O00629; Q9H2P0: ADNP; NbExp=3; IntAct=EBI-396343, EBI-1764854;
CC O00629; P51816: AFF2; NbExp=3; IntAct=EBI-396343, EBI-1754468;
CC O00629; Q05D32: CTDSPL2; NbExp=3; IntAct=EBI-396343, EBI-10039222;
CC O00629; Q6ZMK1: CYHR1; NbExp=3; IntAct=EBI-396343, EBI-3908824;
CC O00629; Q9Y222: DMTF1; NbExp=3; IntAct=EBI-396343, EBI-2814971;
CC O00629; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-396343, EBI-742802;
CC O00629; Q8NCD3: HJURP; NbExp=4; IntAct=EBI-396343, EBI-719429;
CC O00629; P07910: HNRNPC; NbExp=9; IntAct=EBI-396343, EBI-357966;
CC O00629; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-396343, EBI-3918847;
CC O00629; Q92993: KAT5; NbExp=3; IntAct=EBI-396343, EBI-399080;
CC O00629; P35968: KDR; NbExp=4; IntAct=EBI-396343, EBI-1005487;
CC O00629; Q14974: KPNB1; NbExp=4; IntAct=EBI-396343, EBI-286758;
CC O00629; Q9NZL9: MAT2B; NbExp=3; IntAct=EBI-396343, EBI-10317491;
CC O00629; Q9ULH7: MRTFB; NbExp=3; IntAct=EBI-396343, EBI-493007;
CC O00629; Q13330: MTA1; NbExp=4; IntAct=EBI-396343, EBI-714236;
CC O00629; P01106: MYC; NbExp=6; IntAct=EBI-396343, EBI-447544;
CC O00629; Q53F19: NCBP3; NbExp=5; IntAct=EBI-396343, EBI-6657994;
CC O00629; O75376: NCOR1; NbExp=4; IntAct=EBI-396343, EBI-347233;
CC O00629; Q9Y618: NCOR2; NbExp=10; IntAct=EBI-396343, EBI-80830;
CC O00629; Q16236: NFE2L2; NbExp=4; IntAct=EBI-396343, EBI-2007911;
CC O00629; P52952: NKX2-5; NbExp=2; IntAct=EBI-396343, EBI-936601;
CC O00629; Q9UKX7: NUP50; NbExp=6; IntAct=EBI-396343, EBI-2371082;
CC O00629; Q9Y263: PLAA; NbExp=3; IntAct=EBI-396343, EBI-1994037;
CC O00629; Q96PX9: PLEKHG4B; NbExp=2; IntAct=EBI-396343, EBI-11741362;
CC O00629; P46063: RECQL; NbExp=2; IntAct=EBI-396343, EBI-2823728;
CC O00629; Q9H040: SPRTN; NbExp=2; IntAct=EBI-396343, EBI-11128611;
CC O00629; Q13148: TARDBP; NbExp=3; IntAct=EBI-396343, EBI-372899;
CC O00629; Q9ULW0: TPX2; NbExp=3; IntAct=EBI-396343, EBI-1037322;
CC O00629; Q6R2W3: ZBED9; NbExp=2; IntAct=EBI-396343, EBI-21631759;
CC O00629; Q8NF64: ZMIZ2; NbExp=3; IntAct=EBI-396343, EBI-745786;
CC O00629; Q9HCE3: ZNF532; NbExp=2; IntAct=EBI-396343, EBI-9691987;
CC O00629; Q5FWF4: ZRANB3; NbExp=2; IntAct=EBI-396343, EBI-13954615;
CC O00629; PRO_0000042447 [P04585]: gag-pol; Xeno; NbExp=4; IntAct=EBI-396343, EBI-9872653;
CC O00629; Q8K4J6: Mrtfa; Xeno; NbExp=4; IntAct=EBI-396343, EBI-8291665;
CC O00629; K9N643: ORF4b; Xeno; NbExp=7; IntAct=EBI-396343, EBI-25641007;
CC O00629; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-396343, EBI-6051231;
CC O00629; P03070; Xeno; NbExp=2; IntAct=EBI-396343, EBI-617698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, small intestine,
CC heart, skeletal muscle, lung and pancreas, but barely detectable in
CC kidney, thymus, colon and peripheral blood leukocytes.
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 (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 -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
CC -!- CAUTION: Was termed importin alpha-3. {ECO:0000305|PubMed:9395085}.
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DR EMBL; AB002533; BAA19546.1; -; mRNA.
DR EMBL; AK291041; BAF83730.1; -; mRNA.
DR EMBL; CH471052; EAW78632.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78633.1; -; Genomic_DNA.
DR EMBL; U93240; AAC25605.1; -; mRNA.
DR EMBL; Y12393; CAA73025.1; -; mRNA.
DR EMBL; BC028691; AAH28691.1; -; mRNA.
DR EMBL; BC034493; AAH34493.1; -; mRNA.
DR CCDS; CCDS3191.1; -.
DR PIR; JC5505; JC5505.
DR RefSeq; NP_002259.1; NM_002268.4.
DR PDB; 4UAE; X-ray; 2.70 A; A=68-487.
DR PDB; 5TBK; X-ray; 3.45 A; A/B/C/D/E/F/G/H=1-521.
DR PDB; 5XZX; X-ray; 3.00 A; A=70-485.
DR PDB; 6BVV; X-ray; 2.30 A; A=64-521.
DR PDB; 6BVZ; X-ray; 2.30 A; A=64-521.
DR PDB; 6BW9; X-ray; 1.60 A; A=64-521.
DR PDB; 6BWA; X-ray; 2.20 A; A=64-521.
DR PDB; 6BWB; X-ray; 2.30 A; A=64-521.
DR PDB; 6WX8; X-ray; 2.30 A; A/C=64-521.
DR PDB; 7JJL; X-ray; 2.60 A; A=64-521.
DR PDB; 7LF4; X-ray; 2.85 A; A/C=1-521.
DR PDB; 7LFC; X-ray; 2.10 A; A=1-521.
DR PDB; 7RFY; X-ray; 2.50 A; A=64-521.
DR PDB; 7RG5; X-ray; 2.15 A; A=64-521.
DR PDBsum; 4UAE; -.
DR PDBsum; 5TBK; -.
DR PDBsum; 5XZX; -.
DR PDBsum; 6BVV; -.
DR PDBsum; 6BVZ; -.
DR PDBsum; 6BW9; -.
DR PDBsum; 6BWA; -.
DR PDBsum; 6BWB; -.
DR PDBsum; 6WX8; -.
DR PDBsum; 7JJL; -.
DR PDBsum; 7LF4; -.
DR PDBsum; 7LFC; -.
DR PDBsum; 7RFY; -.
DR PDBsum; 7RG5; -.
DR AlphaFoldDB; O00629; -.
DR SMR; O00629; -.
DR BioGRID; 110038; 146.
DR ComplexPortal; CPX-1060; Importin complex, KPNA4 variant.
DR DIP; DIP-32982N; -.
DR IntAct; O00629; 126.
DR MINT; O00629; -.
DR STRING; 9606.ENSP00000334373; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O00629; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00629; -.
DR MetOSite; O00629; -.
DR PhosphoSitePlus; O00629; -.
DR SwissPalm; O00629; -.
DR BioMuta; KPNA4; -.
DR EPD; O00629; -.
DR jPOST; O00629; -.
DR MassIVE; O00629; -.
DR MaxQB; O00629; -.
DR PaxDb; O00629; -.
DR PeptideAtlas; O00629; -.
DR PRIDE; O00629; -.
DR ProteomicsDB; 48002; -.
DR TopDownProteomics; O00629; -.
DR Antibodypedia; 18521; 353 antibodies from 40 providers.
DR DNASU; 3840; -.
DR Ensembl; ENST00000334256.9; ENSP00000334373.4; ENSG00000186432.10.
DR GeneID; 3840; -.
DR KEGG; hsa:3840; -.
DR MANE-Select; ENST00000334256.9; ENSP00000334373.4; NM_002268.5; NP_002259.1.
DR UCSC; uc003fdn.3; human.
DR CTD; 3840; -.
DR DisGeNET; 3840; -.
DR GeneCards; KPNA4; -.
DR HGNC; HGNC:6397; KPNA4.
DR HPA; ENSG00000186432; Group enriched (skeletal muscle, tongue).
DR MIM; 602970; gene.
DR neXtProt; NX_O00629; -.
DR OpenTargets; ENSG00000186432; -.
DR PharmGKB; PA30188; -.
DR VEuPathDB; HostDB:ENSG00000186432; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244891; -.
DR HOGENOM; CLU_018084_6_1_1; -.
DR InParanoid; O00629; -.
DR OMA; SAQTNKV; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; O00629; -.
DR TreeFam; TF101178; -.
DR PathwayCommons; O00629; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR SignaLink; O00629; -.
DR SIGNOR; O00629; -.
DR BioGRID-ORCS; 3840; 94 hits in 1074 CRISPR screens.
DR ChiTaRS; KPNA4; human.
DR GeneWiki; KPNA4; -.
DR GenomeRNAi; 3840; -.
DR Pharos; O00629; Tbio.
DR PRO; PR:O00629; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O00629; protein.
DR Bgee; ENSG00000186432; Expressed in biceps brachii and 206 other tissues.
DR ExpressionAtlas; O00629; baseline and differential.
DR Genevisible; O00629; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IDA:ComplexPortal.
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; Cytoplasm; Host-virus interaction; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..521
FT /note="Importin subunit alpha-3"
FT /id="PRO_0000120726"
FT DOMAIN 2..58
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 66..106
FT /note="ARM 1; truncated"
FT REPEAT 107..149
FT /note="ARM 2"
FT REPEAT 150..194
FT /note="ARM 3"
FT REPEAT 195..233
FT /note="ARM 4"
FT REPEAT 234..278
FT /note="ARM 5"
FT REPEAT 279..318
FT /note="ARM 6"
FT REPEAT 319..360
FT /note="ARM 7"
FT REPEAT 361..400
FT /note="ARM 8"
FT REPEAT 401..443
FT /note="ARM 9"
FT REPEAT 447..485
FT /note="ARM 10; atypical"
FT REGION 137..229
FT /note="NLS binding site (major)"
FT /evidence="ECO:0000250"
FT REGION 306..394
FT /note="NLS binding site (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 43..52
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 241
FT /note="Q -> T (in Ref. 2; CAA73025)"
FT /evidence="ECO:0000305"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6BW9"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6BVZ"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:6BW9"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6BW9"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:7RG5"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:6BW9"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:7LF4"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:6BW9"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:6BW9"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 425..441
FT /evidence="ECO:0007829|PDB:6BW9"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:6BW9"
FT HELIX 471..484
FT /evidence="ECO:0007829|PDB:6BW9"
SQ SEQUENCE 521 AA; 57887 MW; D98BC45002C9F57E CRC64;
MADNEKLDNQ RLKNFKNKGR DLETMRRQRN EVVVELRKNK RDEHLLKRRN VPHEDICEDS
DIDGDYRVQN TSLEAIVQNA SSDNQGIQLS AVQAARKLLS SDRNPPIDDL IKSGILPILV
HCLERDDNPS LQFEAAWALT NIASGTSEQT QAVVQSNAVP LFLRLLHSPH QNVCEQAVWA
LGNIIGDGPQ CRDYVISLGV VKPLLSFISP SIPITFLRNV TWVMVNLCRH KDPPPPMETI
QEILPALCVL IHHTDVNILV DTVWALSYLT DAGNEQIQMV IDSGIVPHLV PLLSHQEVKV
QTAALRAVGN IVTGTDEQTQ VVLNCDALSH FPALLTHPKE KINKEAVWFL SNITAGNQQQ
VQAVIDANLV PMIIHLLDKG DFGTQKEAAW AISNLTISGR KDQVAYLIQQ NVIPPFCNLL
TVKDAQVVQV VLDGLSNILK MAEDEAETIG NLIEECGGLE KIEQLQNHEN EDIYKLAYEI
IDQFFSSDDI DEDPSLVPEA IQGGTFGFNS SANVPTEGFQ F
