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Protein

Importin subunit alpha-1

Gene

Kpna2

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-5693548. Sensing of DNA Double Strand Breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-1
Alternative name(s):
Importin alpha P1
Karyopherin subunit alpha-2
Pendulin
Pore targeting complex 58 kDa subunit
Short name:
PTAC58
RAG cohort protein 1
SRP1-alpha
Gene namesi
Name:Kpna2
Synonyms:Rch1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 11, Chromosome 17

Organism-specific databases

MGIiMGI:103561. Kpna2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001207232 – 529Importin subunit alpha-1Add BLAST528

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei62PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP52293.
PaxDbiP52293.
PeptideAtlasiP52293.
PRIDEiP52293.

PTM databases

iPTMnetiP52293.
PhosphoSitePlusiP52293.

Expressioni

Tissue specificityi

Slightly detected in brain but not in cerebellum and skeletal muscle, highly expressed in testis and spleen.

Gene expression databases

BgeeiENSMUSG00000018362.
CleanExiMM_KPNA2.
ExpressionAtlasiP52293. baseline and differential.
GenevisibleiP52293. MM.

Interactioni

Subunit structurei

Heterodimer; with KPNB1 (By similarity). Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with PLAG1. Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N-terminus) (By similarity). Interacts with ARL4A, CTNNBL1 and NBN (By similarity). Interacts with ANP32E. Interacts with SNAI1 (via zinc fingers). Interacts with SNAI2 (via zinc fingers) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P030703EBI-3043908,EBI-617698From a different organism.
dUTPaseB4LTG56EBI-3043908,EBI-9821342From a different organism.
IfngP015805EBI-3043908,EBI-7892102
S100A2P290342EBI-3043908,EBI-752230From a different organism.
SF1Q156373EBI-3043908,EBI-744603From a different organism.
TNPO1Q3SYU73EBI-3043908,EBI-8469003From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201007. 16 interactors.
DIPiDIP-47774N.
IntActiP52293. 12 interactors.
STRINGi10090.ENSMUSP00000137310.

Structurei

Secondary structure

1529
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi71 – 73Combined sources3
Helixi78 – 85Combined sources8
Beta strandi86 – 88Combined sources3
Helixi90 – 105Combined sources16
Beta strandi106 – 109Combined sources4
Helixi112 – 117Combined sources6
Helixi121 – 128Combined sources8
Helixi131 – 133Combined sources3
Helixi134 – 148Combined sources15
Helixi152 – 160Combined sources9
Helixi163 – 170Combined sources8
Helixi176 – 191Combined sources16
Helixi194 – 202Combined sources9
Helixi206 – 211Combined sources6
Helixi218 – 220Combined sources3
Helixi223 – 236Combined sources14
Helixi246 – 259Combined sources14
Helixi265 – 278Combined sources14
Beta strandi280 – 282Combined sources3
Helixi283 – 290Combined sources8
Turni291 – 293Combined sources3
Helixi295 – 302Combined sources8
Helixi307 – 320Combined sources14
Helixi325 – 333Combined sources9
Helixi336 – 339Combined sources4
Helixi340 – 343Combined sources4
Helixi349 – 362Combined sources14
Helixi367 – 375Combined sources9
Helixi378 – 387Combined sources10
Helixi391 – 407Combined sources17
Helixi410 – 418Combined sources9
Helixi422 – 427Combined sources6
Helixi428 – 430Combined sources3
Helixi434 – 454Combined sources21
Helixi457 – 466Combined sources10
Helixi469 – 476Combined sources8
Beta strandi478 – 480Combined sources3
Helixi482 – 495Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJLX-ray2.80I70-529[»]
1EJYX-ray2.90I70-529[»]
1IALX-ray2.50A44-496[»]
1IQ1X-ray2.80A/B44-54[»]
C70-529[»]
1PJMX-ray2.50B70-529[»]
1PJNX-ray2.50B70-529[»]
1Q1SX-ray2.30C70-529[»]
1Q1TX-ray2.50C70-529[»]
1Y2AX-ray2.20C70-497[»]
2C1MX-ray2.20A75-498[»]
2YNRX-ray2.30A72-496[»]
3BTRX-ray2.60C70-496[»]
3KNDX-ray2.15A70-529[»]
3L3QX-ray2.30A71-497[»]
3OQSX-ray2.00A70-529[»]
3Q5UX-ray2.50A70-529[»]
3RZ9X-ray2.29A70-529[»]
3RZXX-ray2.61A70-529[»]
3TPMX-ray2.10A75-496[»]
3TPOX-ray2.10A1-529[»]
3UKWX-ray2.10B70-529[»]
3UKXX-ray2.20B70-529[»]
3UKYX-ray2.35B70-529[»]
3UKZX-ray2.30B70-529[»]
3UL0X-ray2.00B70-529[»]
3UL1X-ray1.90B70-529[»]
3UVUX-ray2.38A70-529[»]
3VE6X-ray2.83A71-496[»]
3ZINX-ray2.00A72-496[»]
3ZIOX-ray2.10A72-496[»]
3ZIPX-ray2.40A72-497[»]
3ZIQX-ray2.10A72-497[»]
3ZIRX-ray2.30A72-497[»]
4BA3X-ray2.10A70-529[»]
4HTVX-ray3.00A70-528[»]
4MZ5X-ray2.10E70-528[»]
4MZ6X-ray1.88E70-528[»]
4OIHX-ray2.10A70-529[»]
4U54X-ray2.41A74-498[»]
4U58X-ray2.56A72-497[»]
4U5LX-ray2.53A72-497[»]
4U5NX-ray2.31A72-497[»]
4U5OX-ray2.00A72-497[»]
4U5SX-ray2.12A72-497[»]
4U5UX-ray1.96A72-497[»]
4U5VX-ray1.97A72-497[»]
4UAFX-ray1.70B69-529[»]
4YI0X-ray1.81C70-529[»]
4ZDUX-ray2.30A72-498[»]
5B56X-ray2.30A/B70-529[»]
5CTTX-ray1.70A72-497[»]
5D5KX-ray1.90C70-529[»]
5E6QX-ray2.31B70-529[»]
5EKFX-ray2.00A70-529[»]
5EKGX-ray2.80A70-529[»]
5FC8X-ray2.10E71-529[»]
5HHGX-ray2.20E71-497[»]
5HUWX-ray1.95C2-529[»]
5HUYX-ray1.98C2-529[»]
5KLRX-ray2.20B70-529[»]
5KLTX-ray2.60B70-529[»]
5SVZX-ray2.00A70-529[»]
ProteinModelPortaliP52293.
SMRiP52293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 60IBBPROSITE-ProRule annotationAdd BLAST59
Repeati71 – 111ARM 1; truncatedAdd BLAST41
Repeati112 – 151ARM 2Add BLAST40
Repeati152 – 193ARM 3Add BLAST42
Repeati200 – 244ARM 4Add BLAST45
Repeati246 – 282ARM 5Add BLAST37
Repeati283 – 322ARM 6Add BLAST40
Repeati325 – 364ARM 7Add BLAST40
Repeati367 – 409ARM 8Add BLAST43
Repeati410 – 456ARM 9Add BLAST47
Repeati457 – 496ARM 10; atypicalAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 238NLS binding site (major)Add BLAST97
Regioni315 – 403NLS binding site (minor)Add BLAST89

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi45 – 54Nuclear localization signal2 Publications10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 31Poly-Arg4
Compositional biasi499 – 502Poly-Glu4

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.
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.

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.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52293.
KOiK15043.
OMAiIVPICIR.
OrthoDBiEOG091G095Z.
PhylomeDBiP52293.
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. 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. 6 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNENANLP AARLNRFKNK GKDSTEMRRR RIEVNVELRK AKKDEQMLKR
60 70 80 90 100
RNVSSFPDDA TSPLQENRNN QGTVNWSVED IVKGINSNNL ESQLQATQAA
110 120 130 140 150
RKLLSREKQP PIDNIIRAGL IPKFVSFLGK TDCSPIQFES AWALTNIASG
160 170 180 190 200
TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSAFRDLV
210 220 230 240 250
IKHGAIDPLL ALLAVPDLST LACGYLRNLT WTLSNLCRNK NPAPPLDAVE
260 270 280 290 300
QILPTLVRLL HHNDPEVLAD SCWAISYLTD GPNERIEMVV KKGVVPQLVK
310 320 330 340 350
LLGATELPIV TPALRAIGNI VTGTDEQTQK VIDAGALAVF PSLLTNPKTN
360 370 380 390 400
IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVGVLSKAD FKTQKEAAWA
410 420 430 440 450
ITNYTSGGTV EQIVYLVHCG IIEPLMNLLS AKDTKIIQVI LDAISNIFQA
460 470 480 490 500
AEKLGETEKL SIMIEECGGL DKIEALQRHE NESVYKASLN LIEKYFSVEE
510 520
EEDQNVVPET TSEGFAFQVQ DGAPGTFNF
Length:529
Mass (Da):57,928
Last modified:November 1, 1997 - v2
Checksum:i19E64AA3E9C3C7B5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti242P → S in AAA85281 (PubMed:7565597).Curated1
Sequence conflicti418H → P in AAA85281 (PubMed:7565597).Curated1
Sequence conflicti420G → R in AAA85281 (PubMed:7565597).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55720 mRNA. Translation: BAA09536.1.
U12270 mRNA. Translation: AAA85281.1.
U34229 mRNA. Translation: AAC52451.1.
BC003274 mRNA. Translation: AAH03274.1.
BC006720 mRNA. Translation: AAH06720.1.
CCDSiCCDS25565.1.
PIRiS57345.
S57873.
S62116.
RefSeqiNP_034785.1. NM_010655.3.
UniGeneiMm.12508.
Mm.391577.
Mm.423000.

Genome annotation databases

EnsembliENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
GeneIDi16647.
KEGGimmu:16647.
UCSCiuc007lzz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55720 mRNA. Translation: BAA09536.1.
U12270 mRNA. Translation: AAA85281.1.
U34229 mRNA. Translation: AAC52451.1.
BC003274 mRNA. Translation: AAH03274.1.
BC006720 mRNA. Translation: AAH06720.1.
CCDSiCCDS25565.1.
PIRiS57345.
S57873.
S62116.
RefSeqiNP_034785.1. NM_010655.3.
UniGeneiMm.12508.
Mm.391577.
Mm.423000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJLX-ray2.80I70-529[»]
1EJYX-ray2.90I70-529[»]
1IALX-ray2.50A44-496[»]
1IQ1X-ray2.80A/B44-54[»]
C70-529[»]
1PJMX-ray2.50B70-529[»]
1PJNX-ray2.50B70-529[»]
1Q1SX-ray2.30C70-529[»]
1Q1TX-ray2.50C70-529[»]
1Y2AX-ray2.20C70-497[»]
2C1MX-ray2.20A75-498[»]
2YNRX-ray2.30A72-496[»]
3BTRX-ray2.60C70-496[»]
3KNDX-ray2.15A70-529[»]
3L3QX-ray2.30A71-497[»]
3OQSX-ray2.00A70-529[»]
3Q5UX-ray2.50A70-529[»]
3RZ9X-ray2.29A70-529[»]
3RZXX-ray2.61A70-529[»]
3TPMX-ray2.10A75-496[»]
3TPOX-ray2.10A1-529[»]
3UKWX-ray2.10B70-529[»]
3UKXX-ray2.20B70-529[»]
3UKYX-ray2.35B70-529[»]
3UKZX-ray2.30B70-529[»]
3UL0X-ray2.00B70-529[»]
3UL1X-ray1.90B70-529[»]
3UVUX-ray2.38A70-529[»]
3VE6X-ray2.83A71-496[»]
3ZINX-ray2.00A72-496[»]
3ZIOX-ray2.10A72-496[»]
3ZIPX-ray2.40A72-497[»]
3ZIQX-ray2.10A72-497[»]
3ZIRX-ray2.30A72-497[»]
4BA3X-ray2.10A70-529[»]
4HTVX-ray3.00A70-528[»]
4MZ5X-ray2.10E70-528[»]
4MZ6X-ray1.88E70-528[»]
4OIHX-ray2.10A70-529[»]
4U54X-ray2.41A74-498[»]
4U58X-ray2.56A72-497[»]
4U5LX-ray2.53A72-497[»]
4U5NX-ray2.31A72-497[»]
4U5OX-ray2.00A72-497[»]
4U5SX-ray2.12A72-497[»]
4U5UX-ray1.96A72-497[»]
4U5VX-ray1.97A72-497[»]
4UAFX-ray1.70B69-529[»]
4YI0X-ray1.81C70-529[»]
4ZDUX-ray2.30A72-498[»]
5B56X-ray2.30A/B70-529[»]
5CTTX-ray1.70A72-497[»]
5D5KX-ray1.90C70-529[»]
5E6QX-ray2.31B70-529[»]
5EKFX-ray2.00A70-529[»]
5EKGX-ray2.80A70-529[»]
5FC8X-ray2.10E71-529[»]
5HHGX-ray2.20E71-497[»]
5HUWX-ray1.95C2-529[»]
5HUYX-ray1.98C2-529[»]
5KLRX-ray2.20B70-529[»]
5KLTX-ray2.60B70-529[»]
5SVZX-ray2.00A70-529[»]
ProteinModelPortaliP52293.
SMRiP52293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201007. 16 interactors.
DIPiDIP-47774N.
IntActiP52293. 12 interactors.
STRINGi10090.ENSMUSP00000137310.

PTM databases

iPTMnetiP52293.
PhosphoSitePlusiP52293.

Proteomic databases

EPDiP52293.
PaxDbiP52293.
PeptideAtlasiP52293.
PRIDEiP52293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
GeneIDi16647.
KEGGimmu:16647.
UCSCiuc007lzz.1. mouse.

Organism-specific databases

CTDi3838.
MGIiMGI:103561. Kpna2.

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52293.
KOiK15043.
OMAiIVPICIR.
OrthoDBiEOG091G095Z.
PhylomeDBiP52293.
TreeFamiTF101178.

Enzyme and pathway databases

ReactomeiR-MMU-5693548. Sensing of DNA Double Strand Breaks.

Miscellaneous databases

EvolutionaryTraceiP52293.
PROiP52293.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018362.
CleanExiMM_KPNA2.
ExpressionAtlasiP52293. baseline and differential.
GenevisibleiP52293. 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. 6 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMA1_MOUSE
AccessioniPrimary (citable) accession number: P52293
Secondary accession number(s): Q64292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 163 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.