IPO7_HUMAN
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 03-AUG-2022, entry version 188.
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. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones.
CC {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607,
CC 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 SRP19 (PubMed:11682607). {ECO:0000250|UniProtKB:Q9EPL8,
CC ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:10228156,
CC ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:26878725,
CC 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 -!- INTERACTION:
CC O95373; Q14974: KPNB1; NbExp=2; IntAct=EBI-286735, EBI-286758;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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; 250.
DR DIP; DIP-32574N; -.
DR IntAct; O95373; 89.
DR MINT; O95373; -.
DR STRING; 9606.ENSP00000369042; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O95373; 1 site, 2 O-linked glycans (1 site).
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; O95373; -.
DR PeptideAtlas; O95373; -.
DR PRIDE; O95373; -.
DR ProteomicsDB; 50828; -.
DR Antibodypedia; 11566; 210 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 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; NHWWKCK; -.
DR OrthoDB; 159062at2759; -.
DR PhylomeDB; O95373; -.
DR TreeFam; TF300634; -.
DR PathwayCommons; O95373; -.
DR SignaLink; O95373; -.
DR BioGRID-ORCS; 10527; 582 hits in 1085 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 217 other tissues.
DR ExpressionAtlas; O95373; baseline and differential.
DR Genevisible; O95373; HS.
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:0006606; P:protein import into nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR013713; XPO2_central.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
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
