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Protein

Importin subunit alpha-7

Gene

Kpna6

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

Functioni

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.

GO - Molecular functioni

  • protein transporter activity Source: MGI

GO - Biological processi

  • maternal process involved in female pregnancy Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein import into nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-7
Alternative name(s):
Importin alpha-S2
Karyopherin subunit alpha-6
Gene namesi
Name:Kpna6
Synonyms:Kpna5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1100836. Kpna6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Importin subunit alpha-7PRO_0000120730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO35345.
PaxDbiO35345.
PRIDEiO35345.

PTM databases

iPTMnetiO35345.
PhosphoSiteiO35345.

Expressioni

Tissue specificityi

Only slightly detected in Ehrlich ascites tumor cells, thymus and skeletal muscle, clearly detected in kidney, spleen, liver, heart, and lung. High expression in testis.

Gene expression databases

BgeeiO35345.
CleanExiMM_KPNA6.
ExpressionAtlasiO35345. baseline and differential.
GenevisibleiO35345. MM.

Interactioni

Subunit structurei

Forms a complex with importin subunit beta-1 (By similarity). Interacts with ZIC3.By similarity1 Publication

Protein-protein interaction databases

BioGridi201010. 3 interactions.
DIPiDIP-48616N.
IntActiO35345. 1 interaction.
STRINGi10090.ENSMUSP00000099650.

Structurei

3D structure databases

ProteinModelPortaliO35345.
SMRiO35345. Positions 32-506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6060IBBPROSITE-ProRule annotationAdd
BLAST
Repeati76 – 11540ARM 1; truncatedAdd
BLAST
Repeati116 – 15944ARM 2Add
BLAST
Repeati160 – 20445ARM 3Add
BLAST
Repeati205 – 24339ARM 4Add
BLAST
Repeati244 – 28845ARM 5Add
BLAST
Repeati289 – 32840ARM 6Add
BLAST
Repeati329 – 37042ARM 7Add
BLAST
Repeati371 – 41040ARM 8Add
BLAST
Repeati411 – 45343ARM 9Add
BLAST
Repeati457 – 50246ARM 10; atypicalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 23993NLS binding site (major)By similarityAdd
BLAST
Regioni316 – 40489NLS binding site (minor)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5410Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 314Poly-Arg

Domaini

Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins (By similarity).By similarity
The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding (By similarity).By similarity

Sequence similaritiesi

Belongs to the importin alpha family.Curated
Contains 10 ARM repeats.PROSITE-ProRule annotation
Contains 1 IBB domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiO35345.
OMAiSSTTCGE.
OrthoDBiEOG7VHSWV.
PhylomeDBiO35345.
TreeFamiTF354205.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032413. Arm_3.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
PF16186. Arm_3. 1 hit.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFiPIRSF005673. Importin_alpha. 1 hit.
SMARTiSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 2 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35345-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR
60 70 80 90 100
RNVELINEEA AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT
110 120 130 140 150
TQKFRKLLSK EPSPPIDEVI NTPGVVDRFV EFLKRNENCT LQFEAAWALT
160 170 180 190 200
NIASGTSQQT KIVIEAGAVP IFIELLNSDF EDVQEQAVWA LGNIAGDSSL
210 220 230 240 250
CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG KNPPPEFAKV
260 270 280 290 300
SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
310 320 330 340 350
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSSKE
360 370 380 390 400
SIRKEACWTI SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW
410 420 430 440 450
AITNATSGGT PEQIRYLVSL GCIKPLCDLL TVMDSKIVQV ALNGLENILR
460 470 480 490 500
LGEQESKRSG SGVNPYCGLI EEAYGLDKIE FLQSHENQEI YQKAFDLIEH
510 520 530
YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
Length:536
Mass (Da):59,964
Last modified:June 12, 2007 - v2
Checksum:i553A6265023052AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861V → E in BAE32900 (PubMed:16141072).Curated
Sequence conflicti280 – 2801S → A in BAE32900 (PubMed:16141072).Curated
Sequence conflicti435 – 4351S → T in BAB24841 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007053 mRNA. Translation: BAB24841.1.
AK154882 mRNA. Translation: BAE32900.1.
BC004833 mRNA. Translation: AAH04833.2.
AF020773 mRNA. Translation: AAC53373.1.
CCDSiCCDS18701.1.
RefSeqiNP_032494.3. NM_008468.4.
UniGeneiMm.202358.

Genome annotation databases

EnsembliENSMUST00000102590; ENSMUSP00000099650; ENSMUSG00000003731.
GeneIDi16650.
KEGGimmu:16650.
UCSCiuc008uxz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007053 mRNA. Translation: BAB24841.1.
AK154882 mRNA. Translation: BAE32900.1.
BC004833 mRNA. Translation: AAH04833.2.
AF020773 mRNA. Translation: AAC53373.1.
CCDSiCCDS18701.1.
RefSeqiNP_032494.3. NM_008468.4.
UniGeneiMm.202358.

3D structure databases

ProteinModelPortaliO35345.
SMRiO35345. Positions 32-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201010. 3 interactions.
DIPiDIP-48616N.
IntActiO35345. 1 interaction.
STRINGi10090.ENSMUSP00000099650.

PTM databases

iPTMnetiO35345.
PhosphoSiteiO35345.

Proteomic databases

EPDiO35345.
PaxDbiO35345.
PRIDEiO35345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102590; ENSMUSP00000099650; ENSMUSG00000003731.
GeneIDi16650.
KEGGimmu:16650.
UCSCiuc008uxz.2. mouse.

Organism-specific databases

CTDi23633.
MGIiMGI:1100836. Kpna6.

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiO35345.
OMAiSSTTCGE.
OrthoDBiEOG7VHSWV.
PhylomeDBiO35345.
TreeFamiTF354205.

Miscellaneous databases

ChiTaRSiKpna6. mouse.
PROiO35345.
SOURCEiSearch...

Gene expression databases

BgeeiO35345.
CleanExiMM_KPNA6.
ExpressionAtlasiO35345. baseline and differential.
GenevisibleiO35345. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032413. Arm_3.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
PF16186. Arm_3. 1 hit.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFiPIRSF005673. Importin_alpha. 1 hit.
SMARTiSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 2 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Testis.
  2. "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].
  3. "Identification of novel homologues of mouse importin alpha, the alpha subunit of the nuclear pore-targeting complex, and their tissue-specific expression."
    Tsuji L., Takumi T., Imamoto N., Yoneda Y.
    FEBS Lett. 416:30-34(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-536.
  4. "Functional and structural basis of the nuclear localization signal in the ZIC3 zinc finger domain."
    Hatayama M., Tomizawa T., Sakai-Kato K., Bouvagnet P., Kose S., Imamoto N., Yokoyama S., Utsunomiya-Tate N., Mikoshiba K., Kigawa T., Aruga J.
    Hum. Mol. Genet. 17:3459-3473(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZIC3.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiIMA7_MOUSE
AccessioniPrimary (citable) accession number: O35345
Secondary accession number(s): Q3U388, Q9CVP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 12, 2007
Last modified: June 8, 2016
This is version 131 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.