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Protein

Importin subunit alpha-8

Gene

Kpna7

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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-8
Alternative name(s):
Karyopherin subunit alpha-7
Gene namesi
Name:Kpna7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2141165. Kpna7.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: In MII-stage oocytes, localizes to the spindle.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice exhibit abnormal preimplantation development. About half of the mutant embryos fail to develop into the blastocyst stage, or are delayed. Lethality is greater among female than among male embryos.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Importin subunit alpha-8PRO_0000413537Add
BLAST

Proteomic databases

PaxDbiC0LLJ0.
PRIDEiC0LLJ0.

PTM databases

PhosphoSiteiC0LLJ0.

Expressioni

Tissue specificityi

Expressed predominantly in ovary. Isoform 1 is the predominant form.1 Publication

Developmental stagei

Expressed at high levels in germinal vesicle-stage oocytes, as well as in zygotes and 2-cell embryos (at protein level). Drastically down-regulated after the 2-cell stage.1 Publication

Gene expression databases

BgeeiC0LLJ0.
ExpressionAtlasiC0LLJ0. baseline and differential.
GenevisibleiC0LLJ0. MM.

Interactioni

Subunit structurei

Binds very efficiently to importin subunit beta-1/KPNB1 via the IBB domain. This complex dissociates in the presence of RAN-GTP (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000106300.

Structurei

3D structure databases

ProteinModelPortaliC0LLJ0.
SMRiC0LLJ0. Positions 41-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5757IBBPROSITE-ProRule annotationAdd
BLAST
Repeati101 – 14141ARM 1Add
BLAST
Repeati144 – 18340ARM 2Add
BLAST
Repeati186 – 22641ARM 3Add
BLAST
Repeati229 – 26840ARM 4Add
BLAST
Repeati271 – 31040ARM 5Add
BLAST
Repeati313 – 35240ARM 6Add
BLAST
Repeati354 – 39340ARM 7Add
BLAST
Repeati397 – 43640ARM 8Add
BLAST

Sequence similaritiesi

Belongs to the importin alpha family.Curated
Contains 8 ARM repeats.PROSITE-ProRule annotation
Contains 1 IBB domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiC0LLJ0.
OMAiNKNPYPC.
OrthoDBiEOG7VHSWV.
PhylomeDBiC0LLJ0.
TreeFamiTF101178.

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. 5 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: C0LLJ0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATSKAPKER LKNYKYRGKE MSLPRQQRIA SSLQLRKTRK DEQVLKRRNI
60 70 80 90 100
DLFSSDMVSQ ALVKEVNFTL DDIIQAVNSS DPILHFRATR AAREMISQEN
110 120 130 140 150
TPPLNLIIEA GLIPKLVDFL KATPHPKLQF EAAWVLTNIA SGTSEQTRAV
160 170 180 190 200
VKEGAIQPLI ELLCSPHLTV SEQAVWALGN IAGDCAEFRD CVISNNAIPH
210 220 230 240 250
LINLISKGIP ITFLRNISWT LSNLCRNKDP YPSESAVRQM LPPLCQLLLH
260 270 280 290 300
RDNEILADTC WALSYLTKGG KEYIHHVVTT GILPRLVELM TSSELSISIP
310 320 330 340 350
CLHTIGNIVA GTDEQTQMAI DAGMLKVLGQ VLKHPKTSIQ VLAAWTMSNV
360 370 380 390 400
AAGPRHQVEQ LLCNLLPILV DLLRNAELKV QKEVVCTVIN IATGASQDQL
410 420 430 440 450
TLLAHSGILE PMLSLLSAPD LEVVIIVLDI ISYLLQHIDN LQEKKRLYFQ
460 470 480 490
IEKFGGFEKI ECLQHHHNIS ISNSALDIIE KYFCEDGDGD SLPGPGLRV
Length:499
Mass (Da):55,458
Last modified:May 5, 2009 - v1
Checksum:i0B1094E04CAFA556
GO
Isoform 2 (identifier: C0LLJ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     182-182: A → ADRKMPDTQVQIFTPSTREAKA

Show »
Length:520
Mass (Da):57,860
Checksum:i63A6CCCEFD6D0546
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611E → D in ACN85342 (PubMed:20699224).Curated
Sequence conflicti161 – 1611E → D in AAX50192 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 1821A → ADRKMPDTQVQIFTPSTREA KA in isoform 2. 2 PublicationsVSP_041924

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ717332 mRNA. Translation: ACN85341.1.
FJ717333 mRNA. Translation: ACN85342.1.
AY950703 mRNA. Translation: AAX50192.1.
AC110556 Genomic DNA. No translation available.
AC113295 Genomic DNA. No translation available.
CH466529 Genomic DNA. Translation: EDL19009.1.
AK136027 mRNA. Translation: BAE22781.1.
CCDSiCCDS19852.1. [C0LLJ0-1]
RefSeqiNP_001013796.2. NM_001013774.2. [C0LLJ0-1]
XP_006504905.1. XM_006504842.2. [C0LLJ0-2]
UniGeneiMm.332837.

Genome annotation databases

EnsembliENSMUST00000110672; ENSMUSP00000106300; ENSMUSG00000038770. [C0LLJ0-1]
ENSMUST00000110673; ENSMUSP00000106301; ENSMUSG00000038770. [C0LLJ0-2]
ENSMUST00000116454; ENSMUSP00000112155; ENSMUSG00000038770. [C0LLJ0-1]
GeneIDi381686.
KEGGimmu:381686.
UCSCiuc009alx.1. mouse. [C0LLJ0-2]
uc009aly.1. mouse. [C0LLJ0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ717332 mRNA. Translation: ACN85341.1.
FJ717333 mRNA. Translation: ACN85342.1.
AY950703 mRNA. Translation: AAX50192.1.
AC110556 Genomic DNA. No translation available.
AC113295 Genomic DNA. No translation available.
CH466529 Genomic DNA. Translation: EDL19009.1.
AK136027 mRNA. Translation: BAE22781.1.
CCDSiCCDS19852.1. [C0LLJ0-1]
RefSeqiNP_001013796.2. NM_001013774.2. [C0LLJ0-1]
XP_006504905.1. XM_006504842.2. [C0LLJ0-2]
UniGeneiMm.332837.

3D structure databases

ProteinModelPortaliC0LLJ0.
SMRiC0LLJ0. Positions 41-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000106300.

PTM databases

PhosphoSiteiC0LLJ0.

Proteomic databases

PaxDbiC0LLJ0.
PRIDEiC0LLJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110672; ENSMUSP00000106300; ENSMUSG00000038770. [C0LLJ0-1]
ENSMUST00000110673; ENSMUSP00000106301; ENSMUSG00000038770. [C0LLJ0-2]
ENSMUST00000116454; ENSMUSP00000112155; ENSMUSG00000038770. [C0LLJ0-1]
GeneIDi381686.
KEGGimmu:381686.
UCSCiuc009alx.1. mouse. [C0LLJ0-2]
uc009aly.1. mouse. [C0LLJ0-1]

Organism-specific databases

CTDi402569.
MGIiMGI:2141165. Kpna7.

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiC0LLJ0.
OMAiNKNPYPC.
OrthoDBiEOG7VHSWV.
PhylomeDBiC0LLJ0.
TreeFamiTF101178.

Miscellaneous databases

ChiTaRSiKpna7. mouse.
NextBioi402427.
PROiC0LLJ0.
SOURCEiSearch...

Gene expression databases

BgeeiC0LLJ0.
ExpressionAtlasiC0LLJ0. baseline and differential.
GenevisibleiC0LLJ0. 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. 5 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. "Novel importin-alpha family member Kpna7 is required for normal fertility and fecundity in the mouse."
    Hu J., Wang F., Yuan Y., Zhu X., Wang Y., Zhang Y., Kou Z., Wang S., Gao S.
    J. Biol. Chem. 285:33113-33122(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH KPNB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: C57BL/6J.
    Tissue: Ovary.
  2. Hartmann E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 105-499 (ISOFORM 2).
    Tissue: Embryo.

Entry informationi

Entry nameiIMA8_MOUSE
AccessioniPrimary (citable) accession number: C0LLJ0
Secondary accession number(s): C0LLJ1, Q3UWY3, Q58HC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 5, 2009
Last modified: May 11, 2016
This is version 57 of the entry and version 1 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.