IPO7_MOUSE
ID IPO7_MOUSE Reviewed; 1038 AA.
AC Q9EPL8; Q7TN09; Q7TQ63; Q8BKD8; Q8BYI0;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Importin-7;
DE Short=Imp7;
DE AltName: Full=Ran-binding protein 7;
DE Short=RanBP7;
GN Name=Ipo7; Synonyms=Ranbp7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11528126; DOI=10.1159/000056998;
RA Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S.,
RA Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.;
RT "Comparative architectural aspects of regions of conserved synteny on human
RT chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and
RT LMO1).";
RL Cytogenet. Cell Genet. 93:277-283(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Pelka P., Joch M., Scime A., Whyte P.;
RT "Isolation of cDNA for mouse RAN binding protein 7/importin 7.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-895.
RC STRAIN=C57BL/6J; TISSUE=Eye, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-1038.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
RX PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT "Multiple pathways contribute to nuclear import of core histones.";
RL EMBO Rep. 2:690-696(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1020, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Mediates autonomously the nuclear import of ribosomal proteins RPL23A,
CC RPS7 and RPL5 (By similarity). In association with KPNB1 mediates the
CC nuclear import of H1 histone and the Ran-binding site of IPO7 is not
CC required but synergizes with that of KPNB1 in importin/substrate
CC complex dissociation (By similarity). In vitro, mediates nuclear import
CC of H2A, H2B, H3 and H4 histones (PubMed:11493596).
CC {ECO:0000250|UniProtKB:O95373, ECO:0000269|PubMed:11493596}.
CC -!- SUBUNIT: Forms a heterodimer with KPNB1 (By similarity). Interacts with
CC histone H1 (By similarity). Interacts with H2A, H2B, H3 and H4 histones
CC (PubMed:11493596). Interacts with SNUPN and XPO1 (By similarity).
CC Interacts with RPS7 and RPL5 (By similarity). Interacts with RPL23A
CC (via BIB domain) (By similarity). Binds directly to nuclear pore
CC complexes (By similarity). Interacts with SMAD4 and NUP93; translocates
CC SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in
CC activation of SMAD4 signaling (By similarity). Interacts with SRP19 (By
CC similarity). {ECO:0000250|UniProtKB:O95373,
CC ECO:0000269|PubMed:11493596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; AJ278435; CAC17143.1; -; Genomic_DNA.
DR EMBL; AY316153; AAP79888.1; -; mRNA.
DR EMBL; AK039534; BAC30376.1; -; mRNA.
DR EMBL; AK053498; BAC35405.1; -; mRNA.
DR EMBL; BC053524; AAH53524.1; -; mRNA.
DR EMBL; BC064825; AAH64825.1; -; mRNA.
DR CCDS; CCDS40085.1; -.
DR RefSeq; NP_852658.2; NM_181517.3.
DR AlphaFoldDB; Q9EPL8; -.
DR SMR; Q9EPL8; -.
DR BioGRID; 231437; 19.
DR IntAct; Q9EPL8; 7.
DR MINT; Q9EPL8; -.
DR STRING; 10090.ENSMUSP00000081782; -.
DR ChEMBL; CHEMBL2176785; -.
DR iPTMnet; Q9EPL8; -.
DR PhosphoSitePlus; Q9EPL8; -.
DR SwissPalm; Q9EPL8; -.
DR EPD; Q9EPL8; -.
DR jPOST; Q9EPL8; -.
DR MaxQB; Q9EPL8; -.
DR PaxDb; Q9EPL8; -.
DR PeptideAtlas; Q9EPL8; -.
DR PRIDE; Q9EPL8; -.
DR ProteomicsDB; 301660; -.
DR Antibodypedia; 11566; 210 antibodies from 31 providers.
DR DNASU; 233726; -.
DR Ensembl; ENSMUST00000084731; ENSMUSP00000081782; ENSMUSG00000066232.
DR GeneID; 233726; -.
DR KEGG; mmu:233726; -.
DR UCSC; uc009jeu.1; mouse.
DR CTD; 10527; -.
DR MGI; MGI:2152414; Ipo7.
DR VEuPathDB; HostDB:ENSMUSG00000066232; -.
DR eggNOG; KOG1991; Eukaryota.
DR GeneTree; ENSGT00940000154666; -.
DR HOGENOM; CLU_004196_1_1_1; -.
DR InParanoid; Q9EPL8; -.
DR OMA; NHWWKCK; -.
DR OrthoDB; 159062at2759; -.
DR PhylomeDB; Q9EPL8; -.
DR TreeFam; TF300634; -.
DR BioGRID-ORCS; 233726; 34 hits in 112 CRISPR screens.
DR ChiTaRS; Ipo7; mouse.
DR PRO; PR:Q9EPL8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9EPL8; protein.
DR Bgee; ENSMUSG00000066232; Expressed in parotid gland and 260 other tissues.
DR ExpressionAtlas; Q9EPL8; baseline and differential.
DR Genevisible; Q9EPL8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
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; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1038
FT /note="Importin-7"
FT /id="PRO_0000120751"
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:0000250|UniProtKB:O95373"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95373"
FT MOD_RES 898
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95373"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95373"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 160
FT /note="E -> G (in Ref. 3; BAC35405)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="V -> VV (in Ref. 1; CAC17143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1038 AA; 119486 MW; 0AB7104A93FA72EC CRC64;
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL
KNMITQYWPD REATPGDIAP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH
DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV
LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWVE 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 EHENDSDDDE DAEDDDETEE
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ
IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS
APVVPSSFNF GGPAPGMN
