IPO4_HUMAN
ID IPO4_HUMAN Reviewed; 1081 AA.
AC Q8TEX9; B2RN95; Q2NL96; Q86TZ9; Q8NCG8; Q96SJ3; Q9BTI4; Q9H5L0;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Importin-4 {ECO:0000303|PubMed:11823430};
DE Short=Imp4 {ECO:0000303|PubMed:11823430};
DE AltName: Full=Importin-4b {ECO:0000303|PubMed:11823430};
DE Short=Imp4b {ECO:0000303|PubMed:11823430};
DE AltName: Full=Ran-binding protein 4;
DE Short=RanBP4;
GN Name=IPO4; Synonyms=IMP4B, RANBP4;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH RPS3A,
RP AND VARIANTS VAL-513 AND ALA-580.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Skin;
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 1-11; 24-33; 55-62; 82-90; 402-411; 528-534; 751-761;
RP 900-916; 941-951 AND 1042-1053, ACETYLATION AT MET-1, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-1081 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 538-1081 (ISOFORM 2), AND VARIANTS VAL-513
RP AND ALA-580.
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 [8]
RP FUNCTION, AND 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16207705; DOI=10.1074/jbc.m509347200;
RA Miyauchi Y., Michigami T., Sakaguchi N., Sekimoto T., Yoneda Y., Pike J.W.,
RA Yamagata M., Ozono K.;
RT "Importin 4 is responsible for ligand-independent nuclear translocation of
RT vitamin D receptor.";
RL J. Biol. Chem. 280:40901-40908(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17682055; DOI=10.1128/mcb.00519-07;
RA Pradeepa M.M., Manjunatha S., Sathish V., Agrawal S., Rao M.R.;
RT "Involvement of importin-4 in the transport of transition protein 2 into
RT the spermatid nucleus.";
RL Mol. Cell. Biol. 28:4331-4341(2008).
RN [11]
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 [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 FUNCTION.
RX PubMed=21454524; DOI=10.1074/jbc.m111.223453;
RA Alvarez F., Munoz F., Schilcher P., Imhof A., Almouzni G., Loyola A.;
RT "Sequential establishment of marks on soluble histones H3 and H4.";
RL J. Biol. Chem. 286:17714-17721(2011).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; HISTONES H3 AND H4.
RX PubMed=22407294; DOI=10.1038/emboj.2012.55;
RA Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
RT "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in
RT S-phase histone supply.";
RL EMBO J. 31:2013-2023(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
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 [17] {ECO:0007744|PDB:5XAH, ECO:0007744|PDB:5XBK}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 668-1081 IN COMPLEX WITH HISTONE
RP H3.2, AND FUNCTION.
RX PubMed=29408485; DOI=10.1016/j.jmb.2018.01.015;
RA Yoon J., Kim S.J., An S., Cho S., Leitner A., Jung T., Aebersold R.,
RA Hebert H., Cho U.S., Song J.J.;
RT "Integrative structural investigation on the architecture of human
RT Importin4_Histone H3/H4_Asf1a complex and its histone H3 tail binding.";
RL J. Mol. Biol. 430:822-841(2018).
CC -!- FUNCTION: Nuclear transport receptor that mediates nuclear import of
CC proteins, such as histones, RPS3A, TNP2 and VDR (PubMed:11823430,
CC PubMed:16207705, PubMed:17682055, PubMed:21454524). Serves as receptor
CC for nuclear localization signals (NLS) in cargo substrates
CC (PubMed:11823430, PubMed:16207705). Is thought to mediate docking of
CC the importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-dependent
CC mechanism (PubMed:11823430, PubMed:16207705). At the nucleoplasmic side
CC of the NPC, Ran binds to the importin, the importin/substrate complex
CC dissociates and importin is re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran (PubMed:11823430). 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 (PubMed:11823430). Mediates the nuclear
CC import of the histone H3-H4 dimer when in complex with ASF1 (ASF1A or
CC ASF1B) (PubMed:21454524, PubMed:29408485). Mediates the ligand-
CC independent nuclear import of vitamin D receptor (VDR)
CC (PubMed:16207705). In vitro, mediates the nuclear import of human
CC cytomegalovirus UL84 by recognizing a non-classical NLS
CC (PubMed:12610148). {ECO:0000269|PubMed:11823430,
CC ECO:0000269|PubMed:12610148, ECO:0000269|PubMed:16207705,
CC ECO:0000269|PubMed:17682055, ECO:0000269|PubMed:21454524,
CC ECO:0000269|PubMed:29408485}.
CC -!- SUBUNIT: Found in a cytosolic complex with ASF1 (ASF1A or ASF1B) and
CC histones H3 and H4. {ECO:0000269|PubMed:21454524,
CC ECO:0000269|PubMed:22407294}.
CC -!- INTERACTION:
CC Q8TEX9; P49716: CEBPD; NbExp=5; IntAct=EBI-395967, EBI-7962058;
CC Q8TEX9; O14964: HGS; NbExp=5; IntAct=EBI-395967, EBI-740220;
CC Q8TEX9; P42858: HTT; NbExp=7; IntAct=EBI-395967, EBI-466029;
CC Q8TEX9; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-395967, EBI-2555179;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16207705,
CC ECO:0000269|PubMed:17682055}. Nucleus {ECO:0000269|PubMed:16207705,
CC ECO:0000269|PubMed:17682055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEX9-2; Sequence=VSP_009339;
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15616.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB55421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11174.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD62595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AF411122; AAL78660.1; -; mRNA.
DR EMBL; BX248267; CAD62595.1; ALT_INIT; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66078.1; -; Genomic_DNA.
DR EMBL; BC003690; AAH03690.2; -; mRNA.
DR EMBL; BC110804; AAI10805.1; -; mRNA.
DR EMBL; BC136759; AAI36760.1; -; mRNA.
DR EMBL; AK026991; BAB15616.1; ALT_FRAME; mRNA.
DR EMBL; AK027871; BAB55421.1; ALT_INIT; mRNA.
DR EMBL; AK074743; BAC11174.1; ALT_INIT; mRNA.
DR CCDS; CCDS9616.1; -. [Q8TEX9-1]
DR RefSeq; NP_078934.3; NM_024658.3. [Q8TEX9-1]
DR PDB; 5XAH; X-ray; 3.00 A; A/B/C/D=668-1081.
DR PDB; 5XBK; X-ray; 3.22 A; A/B/C/D=668-1081.
DR PDBsum; 5XAH; -.
DR PDBsum; 5XBK; -.
DR AlphaFoldDB; Q8TEX9; -.
DR SMR; Q8TEX9; -.
DR BioGRID; 122828; 180.
DR CORUM; Q8TEX9; -.
DR DIP; DIP-32944N; -.
DR IntAct; Q8TEX9; 57.
DR MINT; Q8TEX9; -.
DR STRING; 9606.ENSP00000346453; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR CarbonylDB; Q8TEX9; -.
DR GlyGen; Q8TEX9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TEX9; -.
DR MetOSite; Q8TEX9; -.
DR PhosphoSitePlus; Q8TEX9; -.
DR BioMuta; IPO4; -.
DR DMDM; 126302558; -.
DR EPD; Q8TEX9; -.
DR jPOST; Q8TEX9; -.
DR MassIVE; Q8TEX9; -.
DR MaxQB; Q8TEX9; -.
DR PaxDb; Q8TEX9; -.
DR PeptideAtlas; Q8TEX9; -.
DR PRIDE; Q8TEX9; -.
DR ProteomicsDB; 74523; -. [Q8TEX9-1]
DR ProteomicsDB; 74524; -. [Q8TEX9-2]
DR Antibodypedia; 47245; 112 antibodies from 20 providers.
DR DNASU; 79711; -.
DR Ensembl; ENST00000354464.11; ENSP00000346453.6; ENSG00000196497.17. [Q8TEX9-1]
DR Ensembl; ENST00000644546.2; ENSP00000494795.1; ENSG00000285248.2. [Q8TEX9-1]
DR GeneID; 79711; -.
DR KEGG; hsa:79711; -.
DR MANE-Select; ENST00000354464.11; ENSP00000346453.6; NM_024658.4; NP_078934.3.
DR UCSC; uc001wmv.2; human. [Q8TEX9-1]
DR CTD; 79711; -.
DR DisGeNET; 79711; -.
DR GeneCards; IPO4; -.
DR HGNC; HGNC:19426; IPO4.
DR HPA; ENSG00000196497; Tissue enhanced (testis).
DR neXtProt; NX_Q8TEX9; -.
DR OpenTargets; ENSG00000196497; -.
DR PharmGKB; PA134968932; -.
DR VEuPathDB; HostDB:ENSG00000196497; -.
DR eggNOG; KOG2171; Eukaryota.
DR GeneTree; ENSGT00550000075074; -.
DR HOGENOM; CLU_003794_1_2_1; -.
DR InParanoid; Q8TEX9; -.
DR OMA; VRGNAAY; -.
DR PhylomeDB; Q8TEX9; -.
DR TreeFam; TF323157; -.
DR PathwayCommons; Q8TEX9; -.
DR SignaLink; Q8TEX9; -.
DR BioGRID-ORCS; 79711; 32 hits in 1082 CRISPR screens.
DR ChiTaRS; IPO4; human.
DR GeneWiki; IPO4; -.
DR GenomeRNAi; 79711; -.
DR Pharos; Q8TEX9; Tbio.
DR PRO; PR:Q8TEX9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TEX9; protein.
DR Bgee; ENSG00000196497; Expressed in left testis and 94 other tissues.
DR ExpressionAtlas; Q8TEX9; baseline and differential.
DR Genevisible; Q8TEX9; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Nucleus; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..1081
FT /note="Importin-4"
FT /id="PRO_0000120748"
FT DOMAIN 24..90
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 348..385
FT /note="HEAT 1"
FT REPEAT 390..427
FT /note="HEAT 2"
FT REPEAT 431..471
FT /note="HEAT 3"
FT REPEAT 475..513
FT /note="HEAT 4"
FT REPEAT 895..932
FT /note="HEAT 5"
FT REPEAT 936..974
FT /note="HEAT 6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1038
FT /note="P -> PGE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009339"
FT VARIANT 513
FT /note="A -> V (in dbSNP:rs7146310)"
FT /evidence="ECO:0000269|PubMed:11823430,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_030758"
FT VARIANT 580
FT /note="P -> A (in dbSNP:rs11550452)"
FT /evidence="ECO:0000269|PubMed:11823430,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_030759"
FT CONFLICT 865
FT /note="K -> R (in Ref. 7; BAB15616)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="G -> E (in Ref. 7; BAB55421)"
FT /evidence="ECO:0000305"
FT HELIX 695..703
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 711..732
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 738..759
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 765..781
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 784..787
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 792..804
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 826..846
FT /evidence="ECO:0007829|PDB:5XAH"
FT TURN 849..851
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 852..864
FT /evidence="ECO:0007829|PDB:5XAH"
FT STRAND 867..870
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 872..889
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 890..896
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 897..907
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 913..935
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 938..945
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 948..951
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 955..971
FT /evidence="ECO:0007829|PDB:5XAH"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:5XBK"
FT HELIX 979..988
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 997..1011
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1020..1025
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1027..1029
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1038..1054
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1056..1062
FT /evidence="ECO:0007829|PDB:5XAH"
FT HELIX 1068..1077
FT /evidence="ECO:0007829|PDB:5XAH"
SQ SEQUENCE 1081 AA; 118715 MW; 36D11AF0D6DA8B1E CRC64;
MESAGLEQLL RELLLPDTER IRRATEQLQI VLRAPAALPA LCDLLASAAD PQIRQFAAVL
TRRRLNTRWR RLAAEQRESL KSLILTALQR ETEHCVSLSL AQLSATIFRK EGLEAWPQLL
QLLQHSTHSP HSPEREMGLL LLSVVVTSRP EAFQPHHREL LRLLNETLGE VGSPGLLFYS
LRTLTTMAPY LSTEDVPLAR MLVPKLIMAM QTLIPIDEAK ACEALEALDE LLESEVPVIT
PYLSEVLTFC LEVARNVALG NAIRIRILCC LTFLVKVKSK ALLKNRLLPP LLHTLFPIVA
AEPPPGQLDP EDQDSEEEEL EIELMGETPK HFAVQVVDML ALHLPPEKLC PQLMPMLEEA
LRSESPYQRK AGLLVLAVLS DGAGDHIRQR LLPPLLQIVC KGLEDPSQVV RNAALFALGQ
FSENLQPHIS SYSREVMPLL LAYLKSVPLG HTHHLAKACY ALENFVENLG PKVQPYLPEL
MECMLQLLRN PSSPRAKELA VSALGAIATA AQASLLPYFP AIMEHLREFL LTGREDLQPV
QIQSLETLGV LARAVGEPMR PLAEECCQLG LGLCDQVDDP DLRRCTYSLF AALSGLMGEG
LAPHLEQITT LMLLSLRSTE GIVPQYDGSS SFLLFDDESD GEEEEELMDE DVEEEDDSEI
SGYSVENAFF DEKEDTCAAV GEISVNTSVA FLPYMESVFE EVFKLLECPH LNVRKAAHEA
LGQFCCALHK ACQSCPSEPN TAALQAALAR VVPSYMQAVN RERERQVVMA VLEALTGVLR
SCGTLTLKPP GRLAELCGVL KAVLQRKTAC QDTDEEEEEE DDDQAEYDAM LLEHAGEAIP
ALAAAAGGDS FAPFFAGFLP LLVCKTKQGC TVAEKSFAVG TLAETIQGLG AASAQFVSRL
LPVLLSTAQE ADPEVRSNAI FGMGVLAEHG GHPAQEHFPK LLGLLFPLLA RERHDRVRDN
ICGALARLLM ASPTRKPEPQ VLAALLHALP LKEDLEEWVT IGRLFSFLYQ SSPDQVIDVA
PELLRICSLI LADNKIPPDT KAALLLLLTF LAKQHTDSFQ AALGSLPVDK AQELQAVLGL
S
