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Protein

Importin-7

Gene

Ipo7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones.By similarity1 Publication

GO - Molecular functioni

  • histone binding Source: MGI

GO - Biological processi

  • innate immune response Source: MGI
  • protein import into nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Importin-7
Short name:
Imp7
Alternative name(s):
Ran-binding protein 7
Short name:
RanBP7
Gene namesi
Name:Ipo7
Synonyms:Ranbp7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2152414. Ipo7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038Importin-7PRO_0000120751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei886 – 8861PhosphoserineBy similarity
Modified residuei898 – 8981PhosphothreonineBy similarity
Modified residuei903 – 9031PhosphoserineBy similarity
Modified residuei1020 – 10201PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9EPL8.
MaxQBiQ9EPL8.
PaxDbiQ9EPL8.
PRIDEiQ9EPL8.

PTM databases

iPTMnetiQ9EPL8.
PhosphoSiteiQ9EPL8.
SwissPalmiQ9EPL8.

Expressioni

Gene expression databases

BgeeiQ9EPL8.
CleanExiMM_IPO7.
GenevisibleiQ9EPL8. MM.

Interactioni

Subunit structurei

Forms a heterodimer with KPNB1. Interacts with KPNB1, RNUT1, XPO1, RPL23A, RPS7, RPL5 and HIV-1 reverse transcription complex integrase. Binds directly to nuclear pore complexes (By similarity). Interacts with H2A, H2B, H3 and H4 histones.By similarity1 Publication

GO - Molecular functioni

  • histone binding Source: MGI

Protein-protein interaction databases

BioGridi231437. 3 interactions.
IntActiQ9EPL8. 6 interactions.
MINTiMINT-4468718.
STRINGi10090.ENSMUSP00000081782.

Structurei

3D structure databases

ProteinModelPortaliQ9EPL8.
SMRiQ9EPL8. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180Importin N-terminalPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi886 – 95873Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the importin beta family.Curated
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1991. Eukaryota.
COG5656. LUCA.
GeneTreeiENSGT00550000074736.
HOGENOMiHOG000006586.
HOVERGENiHBG006824.
InParanoidiQ9EPL8.
OMAiPIDEYQI.
OrthoDBiEOG7TF787.
PhylomeDBiQ9EPL8.
TreeFamiTF300634.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08506. Cse1. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL
60 70 80 90 100
PVRQAGVIYL KNMITQYWPD REATPGDIAP YTIPEEDRHC IRENIVEAII
110 120 130 140 150
HSPELIRVQL TTCIHHIIKH DYPSRWTAIV DKIGFYLQSD NSACWLGILL
160 170 180 190 200
CLYQLVKNYE YKKPEERSPL VAAMQHFLPV LKDRFIQLLS DQSDQSVLIQ
210 220 230 240 250
KQIFKIFYAL VQYTLPLELI NQQNLTEWVE ILKTVVNRDV PNETLQVEED
260 270 280 290 300
DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV
310 320 330 340 350
QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII
360 370 380 390 400
QDVIFPLMCY TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA
410 420 430 440 450
CSKRKEVLQK TMGFCYQILT EPNADPRKKD GALHMIGSLA EILLKKKIYK
460 470 480 490 500
DQMEYMLQNH VFPLFSSELG YMRARACWVL HYFCEVKFKS DQNLQTALEL
510 520 530 540 550
TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR PVMQALLHII
560 570 580 590 600
RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG
610 620 630 640 650
SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE
660 670 680 690 700
FYEEIFSLAH SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY
710 720 730 740 750
VTVDTDTLLS DTKYLEMIYS MCKKVLTGVA GEDAECHAAK LLEVIILQCK
760 770 780 790 800
GRGIDQCIPL FVEAALERLT REVKTSELRT MCLQVAIAAL YYNPHLLLNT
810 820 830 840 850
LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG LCALIDMEQI
860 870 880 890 900
PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDE DAEDDDETEE
910 920 930 940 950
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID
960 970 980 990 1000
DEDNPVDEYQ IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD
1010 1020 1030
QRRAAHESKM IEKHGGYKFS APVVPSSFNF GGPAPGMN
Length:1,038
Mass (Da):119,486
Last modified:March 15, 2004 - v2
Checksum:i0AB7104A93FA72EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601E → G in BAC35405 (PubMed:16141072).Curated
Sequence conflicti407 – 4071V → VV in CAC17143 (PubMed:11528126).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278435 Genomic DNA. Translation: CAC17143.1.
AY316153 mRNA. Translation: AAP79888.1.
AK039534 mRNA. Translation: BAC30376.1.
AK053498 mRNA. Translation: BAC35405.1.
BC053524 mRNA. Translation: AAH53524.1.
BC064825 mRNA. Translation: AAH64825.1.
CCDSiCCDS40085.1.
RefSeqiNP_852658.2. NM_181517.3.
UniGeneiMm.222328.

Genome annotation databases

EnsembliENSMUST00000084731; ENSMUSP00000081782; ENSMUSG00000066232.
GeneIDi233726.
KEGGimmu:233726.
UCSCiuc009jeu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278435 Genomic DNA. Translation: CAC17143.1.
AY316153 mRNA. Translation: AAP79888.1.
AK039534 mRNA. Translation: BAC30376.1.
AK053498 mRNA. Translation: BAC35405.1.
BC053524 mRNA. Translation: AAH53524.1.
BC064825 mRNA. Translation: AAH64825.1.
CCDSiCCDS40085.1.
RefSeqiNP_852658.2. NM_181517.3.
UniGeneiMm.222328.

3D structure databases

ProteinModelPortaliQ9EPL8.
SMRiQ9EPL8. Positions 2-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231437. 3 interactions.
IntActiQ9EPL8. 6 interactions.
MINTiMINT-4468718.
STRINGi10090.ENSMUSP00000081782.

Chemistry

ChEMBLiCHEMBL2176785.

PTM databases

iPTMnetiQ9EPL8.
PhosphoSiteiQ9EPL8.
SwissPalmiQ9EPL8.

Proteomic databases

EPDiQ9EPL8.
MaxQBiQ9EPL8.
PaxDbiQ9EPL8.
PRIDEiQ9EPL8.

Protocols and materials databases

DNASUi233726.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084731; ENSMUSP00000081782; ENSMUSG00000066232.
GeneIDi233726.
KEGGimmu:233726.
UCSCiuc009jeu.1. mouse.

Organism-specific databases

CTDi10527.
MGIiMGI:2152414. Ipo7.

Phylogenomic databases

eggNOGiKOG1991. Eukaryota.
COG5656. LUCA.
GeneTreeiENSGT00550000074736.
HOGENOMiHOG000006586.
HOVERGENiHBG006824.
InParanoidiQ9EPL8.
OMAiPIDEYQI.
OrthoDBiEOG7TF787.
PhylomeDBiQ9EPL8.
TreeFamiTF300634.

Miscellaneous databases

NextBioi381799.
PROiQ9EPL8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPL8.
CleanExiMM_IPO7.
GenevisibleiQ9EPL8. MM.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08506. Cse1. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative architectural aspects of regions of conserved synteny on human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and LMO1)."
    Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S., Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.
    Cytogenet. Cell Genet. 93:277-283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation of cDNA for mouse RAN binding protein 7/importin 7."
    Pelka P., Joch M., Scime A., Whyte P.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-895.
    Strain: C57BL/6J.
    Tissue: Eye and Spinal cord.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-1038.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Multiple pathways contribute to nuclear import of core histones."
    Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.
    EMBO Rep. 2:690-696(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1020, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiIPO7_MOUSE
AccessioniPrimary (citable) accession number: Q9EPL8
Secondary accession number(s): Q7TN09
, Q7TQ63, Q8BKD8, Q8BYI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.