ID IPO7_HUMAN Reviewed; 1038 AA. AC O95373; A6NNM5; B2R786; Q1RMF7; Q9H177; Q9NTE3; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Importin-7; DE Short=Imp7; DE AltName: Full=Ran-binding protein 7; DE Short=RanBP7; GN Name=IPO7; Synonyms=RANBP7; 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, AND INTERACTION WITH RPL23A; RPS7; RP RPL5 AND KPNB1. RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491; RA Jaekel S., Goerlich D.; RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of RT ribosomal proteins in mammalian cells."; RL EMBO J. 17:4491-4502(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). 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]. 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, AND ACETYLATION AT MET-1. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-1038. RC TISSUE=Blood; RA Cichutek A., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.; RT "Comparative sequencing of a 1 Mb region in man (chromosome 11p15) and RT mouse (chromosome 7)."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1038. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP CHARACTERIZATION. RX PubMed=9214382; DOI=10.1083/jcb.138.1.65; RA Goerlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P., Hartmann E., RA Prehn S., Izaurralde E.; RT "A novel class of RanGTP binding proteins."; RL J. Cell Biol. 138:65-80(1997). RN [10] RP FUNCTION, INTERACTION WITH H1 HISTONE AND KPNB1, AND MUTAGENESIS OF LYS-61. RX PubMed=10228156; DOI=10.1093/emboj/18.9.2411; RA Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., RA Goerlich D.; RT "The importin beta/importin 7 heterodimer is a functional nuclear import RT receptor for histone H1."; RL EMBO J. 18:2411-2423(1999). RN [11] RP IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH KPNB1; RP SNUPN AND XPO1. RX PubMed=10209022; DOI=10.1083/jcb.145.2.255; RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., RA Hartmann E., Luehrmann R., Goerlich D.; RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm."; RL J. Cell Biol. 145:255-264(1999). RN [12] RP FUNCTION, AND INTERACTION WITH RPL23A AND SRP19. RX PubMed=11682607; DOI=10.1242/jcs.114.19.3479; RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.; RT "Signal recognition particle protein 19 is imported into the nucleus by RT importin 8 (RanBP8) and transportin."; RL J. Cell Sci. 114:3479-3485(2001). RN [13] RP FUNCTION, AND INTERACTION WITH INTEGRASE OF HIV-1 REVERSE TRANSCRIPTION RP COMPLEX (MICROBIAL INFECTION). RX PubMed=12853482; DOI=10.1093/emboj/cdg357; RA Fassati A., Goerlich D., Harrison I., Zaytseva L., Mingot J.-M.; RT "Nuclear import of HIV-1 intracellular reverse transcription complexes is RT mediated by importin 7."; RL EMBO J. 22:3675-3685(2003). RN [14] 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 [15] RP INTERACTION WITH HIV-1 REV (MICROBIAL INFECTION). RX PubMed=16704975; DOI=10.1074/jbc.m602189200; RA Arnold M., Nath A., Hauber J., Kehlenbach R.H.; RT "Multiple importins function as nuclear transport receptors for the Rev RT protein of human immunodeficiency virus type 1."; RL J. Biol. Chem. 281:20883-20890(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; THR-898 AND SER-903, 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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). RN [22] RP INTERACTION WITH SMAD4 AND NUP93. RX PubMed=26878725; DOI=10.1038/ng.3512; RA Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L., RA Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D., RA Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M., RA Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P., RA Antonin W., Hildebrandt F.; RT "Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid- RT resistant nephrotic syndrome."; RL Nat. Genet. 48:457-465(2016). CC -!- FUNCTION: Functions in nuclear protein import, either by acting as CC autonomous nuclear transport receptor or as an adapter-like protein in CC association with the importin-beta subunit KPNB1. Acting autonomously, CC is thought to serve itself as receptor for nuclear localization signals CC (NLS) and to promote translocation of import substrates through the CC nuclear pore complex (NPC) by an energy requiring, Ran-dependent CC mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, CC the importin/substrate complex dissociates and importin is re-exported CC from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. CC The 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. Mediates autonomously the nuclear import of CC ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In CC association with KPNB1 mediates the nuclear import of H1 histone and CC the Ran-binding site of IPO7 is not required but synergizes with that CC of KPNB1 in importin/substrate complex dissociation. Promotes CC odontoblast differentiation via promoting nuclear translocation of CC DLX3, KLF4, SMAD2, thereby facilitating the transcription of target CC genes that play a role in odontoblast differentiation (By similarity). CC Facilitates BMP4-induced translocation of SMAD1 to the nucleus and CC recruitment to the MSX1 gene promoter, thereby promotes the expression CC of the odontogenic regulator MSX1 in dental mesenchymal cells (By CC similarity). Also promotes odontoblast differentiation by facilitating CC the nuclear translocation of HDAC6 and subsequent repression of RUNX2 CC expression (By similarity). Inhibits osteoblast differentiation by CC inhibiting nuclear translocation of RUNX2 and therefore inhibition of CC RUNX2 target gene transcription (By similarity). In vitro, mediates CC nuclear import of H2A, H2B, H3 and H4 histones. CC {ECO:0000250|UniProtKB:Q9EPL8, ECO:0000269|PubMed:10228156, CC ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}. CC -!- FUNCTION: (Microbial infection) Mediates the nuclear import of HIV-1 CC reverse transcription complex (RTC) integrase. Binds and mediates the CC nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:12853482, CC ECO:0000269|PubMed:16704975}. CC -!- SUBUNIT: Forms a heterodimer with KPNB1 (PubMed:9687515, CC PubMed:10228156, PubMed:10209022). Interacts with histone H1 CC (PubMed:10228156). Interacts with H2A, H2B, H3 and H4 histones (By CC similarity). Interacts with SNUPN and XPO1 (PubMed:10209022). Interacts CC with RPS7 and RPL5 (PubMed:9687515). Interacts with RPL23A (via BIB CC domain) (PubMed:9687515, PubMed:11682607). Binds directly to nuclear CC pore complexes (By similarity). Interacts with SMAD4 and NUP93; CC translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation CC resulting in activation of SMAD4 signaling (PubMed:26878725). Interacts CC with phosphorylated SMAD2; the interaction facilitates translocation of CC SMAD2 to the nucleus (By similarity). Interacts with SRP19 CC (PubMed:11682607). Interacts with RUNX2; the interaction inhibits RUNX2 CC nuclear translocation in osteoblasts (By similarity). Interacts with CC HDAC6, DLX3 and KLF4; the interaction facilitates HDAC6, DLX3 and KLF4 CC nuclear translocation in dental papilla cells (By similarity). CC {ECO:0000250|UniProtKB:Q9EPL8, ECO:0000269|PubMed:10209022, CC ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607, CC ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9687515}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 reverse CC transcription complex integrase and rev. {ECO:0000269|PubMed:12853482, CC ECO:0000269|PubMed:16704975}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EPL8}. Nucleus CC {ECO:0000250|UniProtKB:Q9EPL8}. Note=Localizes to the nucleus in the CC presence of BMP4. {ECO:0000250|UniProtKB:Q9EPL8}. CC -!- SIMILARITY: Belongs to the importin beta 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; AF098799; AAC68903.1; -; mRNA. DR EMBL; AK312885; BAG35733.1; -; mRNA. DR EMBL; AC055845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68593.1; -; Genomic_DNA. DR EMBL; BC114929; AAI14930.1; -; mRNA. DR EMBL; AJ295844; CAC17609.1; -; Genomic_DNA. DR EMBL; AL137335; CAB70698.1; -; mRNA. DR CCDS; CCDS31425.1; -. DR PIR; T46501; T46501. DR RefSeq; NP_006382.1; NM_006391.2. DR AlphaFoldDB; O95373; -. DR SMR; O95373; -. DR BioGRID; 115782; 303. DR DIP; DIP-32574N; -. DR IntAct; O95373; 92. DR MINT; O95373; -. DR STRING; 9606.ENSP00000369042; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyCosmos; O95373; 1 site, 2 glycans. DR GlyGen; O95373; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; O95373; -. DR MetOSite; O95373; -. DR PhosphoSitePlus; O95373; -. DR SwissPalm; O95373; -. DR BioMuta; IPO7; -. DR EPD; O95373; -. DR jPOST; O95373; -. DR MassIVE; O95373; -. DR MaxQB; O95373; -. DR PaxDb; 9606-ENSP00000369042; -. DR PeptideAtlas; O95373; -. DR ProteomicsDB; 50828; -. DR Pumba; O95373; -. DR Antibodypedia; 11566; 226 antibodies from 31 providers. DR DNASU; 10527; -. DR Ensembl; ENST00000379719.8; ENSP00000369042.3; ENSG00000205339.10. DR GeneID; 10527; -. DR KEGG; hsa:10527; -. DR MANE-Select; ENST00000379719.8; ENSP00000369042.3; NM_006391.3; NP_006382.1. DR UCSC; uc001mho.4; human. DR AGR; HGNC:9852; -. DR CTD; 10527; -. DR DisGeNET; 10527; -. DR GeneCards; IPO7; -. DR HGNC; HGNC:9852; IPO7. DR HPA; ENSG00000205339; Low tissue specificity. DR MIM; 605586; gene. DR neXtProt; NX_O95373; -. DR OpenTargets; ENSG00000205339; -. DR PharmGKB; PA34213; -. DR VEuPathDB; HostDB:ENSG00000205339; -. DR eggNOG; KOG1991; Eukaryota. DR GeneTree; ENSGT00940000154666; -. DR HOGENOM; CLU_004196_1_1_1; -. DR InParanoid; O95373; -. DR OMA; WVAKTSW; -. DR OrthoDB; 168511at2759; -. DR PhylomeDB; O95373; -. DR TreeFam; TF300634; -. DR PathwayCommons; O95373; -. DR SignaLink; O95373; -. DR BioGRID-ORCS; 10527; 616 hits in 1163 CRISPR screens. DR ChiTaRS; IPO7; human. DR GeneWiki; IPO7; -. DR GenomeRNAi; 10527; -. DR Pharos; O95373; Tbio. DR PRO; PR:O95373; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O95373; Protein. DR Bgee; ENSG00000205339; Expressed in gluteal muscle and 219 other cell types or tissues. DR ExpressionAtlas; O95373; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central. DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0030695; F:GTPase regulator activity; TAS:ProtInc. DR GO; GO:0042393; F:histone binding; IEA:Ensembl. DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; TAS:ProtInc. DR GO; GO:0045087; P:innate immune response; IEA:Ensembl. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ARUK-UCL. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:1901331; P:positive regulation of odontoblast differentiation; ISS:UniProtKB. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR001494; Importin-beta_N. DR InterPro; IPR013713; XPO2_central. DR PANTHER; PTHR10997:SF27; IMPORTIN-7; 1. DR PANTHER; PTHR10997; IMPORTIN-7, 8, 11; 1. DR Pfam; PF08506; Cse1; 1. DR Pfam; PF03810; IBN_N; 1. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; O95373; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Host-virus interaction; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..1038 FT /note="Importin-7" FT /id="PRO_0000120750" FT DOMAIN 22..101 FT /note="Importin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115" FT REGION 881..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 884..910 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 886 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 898 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 903 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1020 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EPL8" FT VARIANT 111 FT /note="T -> N (in dbSNP:rs11042340)" FT /id="VAR_050003" FT MUTAGEN 61 FT /note="K->A,D: Lowered affinity for RanGTP-binding." FT /evidence="ECO:0000269|PubMed:10228156" SQ SEQUENCE 1038 AA; 119517 MW; 355237CA1DA2D313 CRC64; MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV PNETLQVEED DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII QDVIFPLMCY TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA CSKRKEVLQK TMGFCYQILT EPNADPRKKD GALHMIGSLA EILLKKKIYK DQMEYMLQNH VFPLFSSELG YMRARACWVL HYFCEVKFKS DQNLQTALEL TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR PVMQALLHII RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE FYEEIFSLAH SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY VTVDTDTLLS DTKYLEMIYS MCKKVLTGVA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVEAALERLT REVKTSELRT MCLQVAIAAL YYNPHLLLNT LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG LCALIDMEQI PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS APVVPSSFNF GGPAPGMN //