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P52293

- IMA1_MOUSE

UniProt

P52293 - IMA1_MOUSE

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Protein

Importin subunit alpha-1

Gene
Kpna2, Rch1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. protein binding Source: UniProtKB
  2. protein transporter activity Source: InterPro

GO - Biological processi

  1. protein import into nucleus Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

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
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:103561. Kpna2.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 529528Importin subunit alpha-1PRO_0000120723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei62 – 621Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52293.
PaxDbiP52293.
PRIDEiP52293.

PTM databases

PhosphoSiteiP52293.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP52293.
CleanExiMM_KPNA2.
GenevestigatoriP52293.

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 ARL4A, CTNNBL1 and NBN By similarity. Interacts with ANP32E. Interacts with SNAI1 (via zinc fingers). Interacts with SNAI2 (via zinc fingers) By similarity.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi201007. 12 interactions.
IntActiP52293. 9 interactions.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi71 – 733
Helixi78 – 858
Beta strandi86 – 883
Helixi90 – 10415
Beta strandi106 – 1083
Helixi112 – 1176
Helixi120 – 1289
Helixi131 – 1333
Helixi134 – 14815
Helixi152 – 1609
Helixi163 – 1708
Helixi176 – 19015
Helixi194 – 2029
Helixi206 – 2127
Helixi218 – 2203
Helixi223 – 23715
Helixi246 – 25914
Helixi265 – 27814
Beta strandi280 – 2823
Helixi283 – 2908
Turni291 – 2933
Helixi295 – 3028
Helixi307 – 32014
Helixi325 – 3339
Helixi336 – 3394
Helixi340 – 3434
Helixi349 – 36214
Helixi367 – 3759
Helixi378 – 38710
Helixi391 – 40717
Helixi410 – 4189
Helixi422 – 4276
Helixi428 – 4303
Helixi434 – 45421
Helixi457 – 46610
Helixi469 – 4768
Beta strandi479 – 4813
Helixi482 – 49514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP52293.
SMRiP52293. Positions 11-497.

Miscellaneous databases

EvolutionaryTraceiP52293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6059IBBAdd
BLAST
Repeati71 – 11141ARM 1; truncatedAdd
BLAST
Repeati112 – 15140ARM 2Add
BLAST
Repeati152 – 19342ARM 3Add
BLAST
Repeati200 – 24445ARM 4Add
BLAST
Repeati246 – 28237ARM 5Add
BLAST
Repeati283 – 32240ARM 6Add
BLAST
Repeati325 – 36440ARM 7Add
BLAST
Repeati367 – 40943ARM 8Add
BLAST
Repeati410 – 45647ARM 9Add
BLAST
Repeati457 – 49640ARM 10; atypicalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 23897NLS binding site (major)Add
BLAST
Regioni315 – 40389NLS binding site (minor)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5410Nuclear localization signal2 Publications

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 314Poly-Arg
Compositional biasi499 – 5024Poly-Glu

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.
Contains 10 ARM repeats.
Contains 1 IBB domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5064.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52293.
KOiK15043.
OMAiNETEKLC.
OrthoDBiEOG7VHSWV.
PhylomeDBiP52293.
TreeFamiTF101178.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
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

MSTNENANLP AARLNRFKNK GKDSTEMRRR RIEVNVELRK AKKDEQMLKR    50
RNVSSFPDDA TSPLQENRNN QGTVNWSVED IVKGINSNNL ESQLQATQAA 100
RKLLSREKQP PIDNIIRAGL IPKFVSFLGK TDCSPIQFES AWALTNIASG 150
TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSAFRDLV 200
IKHGAIDPLL ALLAVPDLST LACGYLRNLT WTLSNLCRNK NPAPPLDAVE 250
QILPTLVRLL HHNDPEVLAD SCWAISYLTD GPNERIEMVV KKGVVPQLVK 300
LLGATELPIV TPALRAIGNI VTGTDEQTQK VIDAGALAVF PSLLTNPKTN 350
IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVGVLSKAD FKTQKEAAWA 400
ITNYTSGGTV EQIVYLVHCG IIEPLMNLLS AKDTKIIQVI LDAISNIFQA 450
AEKLGETEKL SIMIEECGGL DKIEALQRHE NESVYKASLN LIEKYFSVEE 500
EEDQNVVPET TSEGFAFQVQ DGAPGTFNF 529
Length:529
Mass (Da):57,928
Last modified:November 1, 1997 - v2
Checksum:i19E64AA3E9C3C7B5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421P → S in AAA85281. 1 Publication
Sequence conflicti418 – 4181H → P in AAA85281. 1 Publication
Sequence conflicti420 – 4201G → R in AAA85281. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENSMUST00000091289; ENSMUSP00000137080; ENSMUSG00000069083.
GeneIDi16647.
KEGGimmu:16647.
UCSCiuc007lzz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25565.1.
PIRi S57345.
S57873.
S62116.
RefSeqi NP_034785.1. NM_010655.3.
UniGenei Mm.12508.
Mm.391577.
Mm.423000.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EJL X-ray 2.80 I 70-529 [» ]
1EJY X-ray 2.90 I 70-529 [» ]
1IAL X-ray 2.50 A 44-496 [» ]
1IQ1 X-ray 2.80 A/B 44-54 [» ]
C 70-529 [» ]
1PJM X-ray 2.50 B 70-529 [» ]
1PJN X-ray 2.50 B 70-529 [» ]
1Q1S X-ray 2.30 C 70-529 [» ]
1Q1T X-ray 2.50 C 70-529 [» ]
1Y2A X-ray 2.20 C 70-497 [» ]
2C1M X-ray 2.20 A 75-498 [» ]
2YNR X-ray 2.30 A 72-496 [» ]
3BTR X-ray 2.60 C 70-496 [» ]
3KND X-ray 2.15 A 70-529 [» ]
3L3Q X-ray 2.30 A 71-497 [» ]
3OQS X-ray 2.00 A 70-529 [» ]
3Q5U X-ray 2.50 A 70-529 [» ]
3RZ9 X-ray 2.29 A 70-529 [» ]
3RZX X-ray 2.61 A 70-529 [» ]
3TPM X-ray 2.10 A 75-496 [» ]
3TPO X-ray 2.10 A 1-529 [» ]
3UKW X-ray 2.10 B 70-529 [» ]
3UKX X-ray 2.20 B 70-529 [» ]
3UKY X-ray 2.35 B 70-529 [» ]
3UKZ X-ray 2.30 B 70-529 [» ]
3UL0 X-ray 2.00 B 70-529 [» ]
3UL1 X-ray 1.90 B 70-529 [» ]
3UVU X-ray 2.38 A 70-529 [» ]
3VE6 X-ray 2.83 A 71-496 [» ]
3ZIN X-ray 2.00 A 72-496 [» ]
3ZIO X-ray 2.10 A 72-496 [» ]
3ZIP X-ray 2.40 A 72-497 [» ]
3ZIQ X-ray 2.10 A 72-497 [» ]
3ZIR X-ray 2.30 A 72-497 [» ]
4BA3 X-ray 2.10 A 70-529 [» ]
4HTV X-ray 3.00 A 70-528 [» ]
4MZ5 X-ray 2.10 E 70-528 [» ]
4MZ6 X-ray 1.88 E 70-528 [» ]
4OIH X-ray 2.10 A 70-529 [» ]
ProteinModelPortali P52293.
SMRi P52293. Positions 11-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201007. 12 interactions.
IntActi P52293. 9 interactions.

PTM databases

PhosphoSitei P52293.

Proteomic databases

MaxQBi P52293.
PaxDbi P52293.
PRIDEi P52293.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018506 ; ENSMUSP00000018506 ; ENSMUSG00000018362 .
ENSMUST00000086423 ; ENSMUSP00000137310 ; ENSMUSG00000066878 .
ENSMUST00000091289 ; ENSMUSP00000137080 ; ENSMUSG00000069083 .
GeneIDi 16647.
KEGGi mmu:16647.
UCSCi uc007lzz.1. mouse.

Organism-specific databases

CTDi 3838.
MGIi MGI:103561. Kpna2.

Phylogenomic databases

eggNOGi COG5064.
HOGENOMi HOG000167616.
HOVERGENi HBG001846.
InParanoidi P52293.
KOi K15043.
OMAi NETEKLC.
OrthoDBi EOG7VHSWV.
PhylomeDBi P52293.
TreeFami TF101178.

Miscellaneous databases

EvolutionaryTracei P52293.
NextBioi 290325.
PROi P52293.
SOURCEi Search...

Gene expression databases

Bgeei P52293.
CleanExi MM_KPNA2.
Genevestigatori P52293.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view ]
Pfami PF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view ]
PIRSFi PIRSF005673. Importin_alpha. 1 hit.
SMARTi SM00185. ARM. 8 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 6 hits.
PS51214. IBB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import."
    Imamoto N., Shimamoto T., Takao T., Tachibana T., Kose S., Matsubae M., Sekimoto T., Shimonishi Y., Yoneda Y.
    EMBO J. 14:3617-3626(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis."
    Kuessel P., Frasch M.
    Mol. Gen. Genet. 248:351-363(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  3. "The nuclear localization signal of lymphoid enhancer factor-1 is recognized by two differentially expressed Srp1-nuclear localization sequence receptor proteins."
    Prieve M.G., Guttridge K.L., Waterman M.L.
    J. Biol. Chem. 271:7654-7658(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
  5. "Characterization of the nuclear transport of a novel leucine-rich acidic nuclear protein-like protein."
    Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.
    FEBS Lett. 468:171-175(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANP32E.
  6. "Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha."
    Fontes M.R., Teh T., Kobe B.
    J. Mol. Biol. 297:1183-1194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 72-497, NUCLEAR LOCALIZATION SIGNAL RECOGNITION.
  7. "Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha."
    Kobe B.
    Nat. Struct. Biol. 6:388-397(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-496, NUCLEAR LOCALIZATION SIGNAL, AUTOINHIBITION.
  8. "Biophysical characterization of interactions involving importin-alpha during nuclear import."
    Catimel B., Teh T., Fontes M.R., Jennings I.G., Jans D.A., Howlett G.J., Nice E.C., Kobe B.
    J. Biol. Chem. 276:34189-34198(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-54, AUTOINHIBITION.
  9. "Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling."
    Matsuura Y., Stewart M.
    EMBO J. 24:3681-3689(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-498 IN COMPLEX WITH NUP50.
  10. "Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
    Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
    J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTS WITH SNAI1.

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: July 9, 2014
This is version 140 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

External Data

Dasty 3

Similar proteinsi