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Protein

Importin subunit alpha-5

Gene

Kpna1

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-211227. Activation of DNA fragmentation factor.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-5
Alternative name(s):
Importin alpha-S1
Karyopherin subunit alpha-1
Nucleoprotein interactor 1
Short name:
NPI-1
RAG cohort protein 2
SRP1-beta
Cleaved into the following chain:
Gene namesi
Name:Kpna1
Synonyms:Rch2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:103560. Kpna1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Importin subunit alpha-5PRO_0000120720Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 538537Importin subunit alpha-5, N-terminally processedPRO_0000424492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei3 – 31PhosphothreonineBy similarity
Modified residuei63 – 631PhosphoserineBy similarity

Post-translational modificationi

Polyubiquitinated in the presence of RAG1 (in vitro).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60960.
MaxQBiQ60960.
PaxDbiQ60960.
PeptideAtlasiQ60960.
PRIDEiQ60960.

PTM databases

iPTMnetiQ60960.
PhosphoSiteiQ60960.

Expressioni

Tissue specificityi

Low levels in all tissues examined.

Gene expression databases

BgeeiENSMUSG00000022905.
CleanExiMM_KPNA1.
ExpressionAtlasiQ60960. baseline and differential.
GenevisibleiQ60960. MM.

Interactioni

Subunit structurei

Heterodimer; with KPNB1 (By similarity). Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 (By similarity). Interacts with APEX1 (via its N-terminus). Interacts with CTNNBL1 (via its N-terminal). Interacts with AICDA (via its NLS) (By similarity). Interacts with ANP32E and ZIC3. Interacts with SNAI1 (via zinc fingers) (By similarity). Interacts with DCAF8.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SF1Q156373EBI-8573008,EBI-744603From a different organism.

Protein-protein interaction databases

BioGridi201006. 5 interactions.
DIPiDIP-48614N.
IntActiQ60960. 2 interactions.
MINTiMINT-4597096.
STRINGi10090.ENSMUSP00000004054.

Structurei

3D structure databases

ProteinModelPortaliQ60960.
SMRiQ60960. Positions 10-509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5757IBBPROSITE-ProRule annotationAdd
BLAST
Repeati77 – 11741ARM 1; truncatedAdd
BLAST
Repeati118 – 16144ARM 2Add
BLAST
Repeati162 – 20645ARM 3Add
BLAST
Repeati207 – 24539ARM 4Add
BLAST
Repeati246 – 29045ARM 5Add
BLAST
Repeati291 – 33040ARM 6Add
BLAST
Repeati331 – 37242ARM 7Add
BLAST
Repeati373 – 41240ARM 8Add
BLAST
Repeati413 – 45745ARM 9Add
BLAST
Repeati460 – 50445ARM 10; atypicalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 24193NLS binding site (major)By similarityAdd
BLAST
Regioni245 – 437193Binding to RAG1By similarityAdd
BLAST
Regioni318 – 40689NLS binding site (minor)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 5110Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 284Poly-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.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiQ60960.
KOiK15042.
OMAiWNCESES.
OrthoDBiEOG091G095Z.
PhylomeDBiQ60960.
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. 3 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV
60 70 80 90 100
ATAEEETEEE VMSDGGFHEA QINNMEMAPG GVITSDMTDM IFSNSPEQQL
110 120 130 140 150
SATQKFRKLL SKEPNPPIDE VINTPGVVAR FVEFLKRKEN CTLQFESAWV
160 170 180 190 200
LTNIASGNSL QTRNVIQAGA VPIFIELLSS EFEDVQEQAV WALGNIAGDS
210 220 230 240 250
TMCRDYVLNC NILPPLLQLF SKQNRLTMTR NAVWALSNLC RGKSPPPEFA
260 270 280 290 300
KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR
310 320 330 340 350
LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP
360 370 380 390 400
KESIKKEACW TISNITAGNR AQIQTVIDAN MFPALISILQ TAEFRTRKEA
410 420 430 440 450
AWAITNATSG GSAEQIKYLV ELGCIKPLCD LLTVMDAKIV QVALNGLENI
460 470 480 490 500
LRLGEQEAKR NGSGINPYCA LIEEAYGLDK IEFLQSHENQ EIYQKAFDLI
510 520 530
EHYFGTEDED SSIAPQVDLS QQQYIFQQCE APMEGFQL
Length:538
Mass (Da):60,183
Last modified:July 15, 1998 - v2
Checksum:i8FE16ACA99F2BA4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831I → T in AAC52450 (PubMed:8631802).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34228 mRNA. Translation: AAC52450.1.
AK028259 mRNA. Translation: BAC25847.1.
AK028307 mRNA. Translation: BAC25872.1.
AK154800 mRNA. Translation: BAE32838.1.
AK169311 mRNA. Translation: BAE41066.1.
AK169348 mRNA. Translation: BAE41098.1.
BC006771 mRNA. Translation: AAH06771.1.
U20619 mRNA. No translation available.
CCDSiCCDS28144.1.
RefSeqiNP_032491.2. NM_008465.5.
XP_006521877.1. XM_006521814.2.
UniGeneiMm.6952.

Genome annotation databases

EnsembliENSMUST00000004054; ENSMUSP00000004054; ENSMUSG00000022905.
GeneIDi16646.
KEGGimmu:16646.
UCSCiuc007zcb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34228 mRNA. Translation: AAC52450.1.
AK028259 mRNA. Translation: BAC25847.1.
AK028307 mRNA. Translation: BAC25872.1.
AK154800 mRNA. Translation: BAE32838.1.
AK169311 mRNA. Translation: BAE41066.1.
AK169348 mRNA. Translation: BAE41098.1.
BC006771 mRNA. Translation: AAH06771.1.
U20619 mRNA. No translation available.
CCDSiCCDS28144.1.
RefSeqiNP_032491.2. NM_008465.5.
XP_006521877.1. XM_006521814.2.
UniGeneiMm.6952.

3D structure databases

ProteinModelPortaliQ60960.
SMRiQ60960. Positions 10-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201006. 5 interactions.
DIPiDIP-48614N.
IntActiQ60960. 2 interactions.
MINTiMINT-4597096.
STRINGi10090.ENSMUSP00000004054.

PTM databases

iPTMnetiQ60960.
PhosphoSiteiQ60960.

Proteomic databases

EPDiQ60960.
MaxQBiQ60960.
PaxDbiQ60960.
PeptideAtlasiQ60960.
PRIDEiQ60960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004054; ENSMUSP00000004054; ENSMUSG00000022905.
GeneIDi16646.
KEGGimmu:16646.
UCSCiuc007zcb.1. mouse.

Organism-specific databases

CTDi3836.
MGIiMGI:103560. Kpna1.

Phylogenomic databases

eggNOGiKOG0166. Eukaryota.
COG5064. LUCA.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiQ60960.
KOiK15042.
OMAiWNCESES.
OrthoDBiEOG091G095Z.
PhylomeDBiQ60960.
TreeFamiTF354205.

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.

Miscellaneous databases

ChiTaRSiKpna1. mouse.
PROiQ60960.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022905.
CleanExiMM_KPNA1.
ExpressionAtlasiQ60960. baseline and differential.
GenevisibleiQ60960. 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. 3 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMA5_MOUSE
AccessioniPrimary (citable) accession number: Q60960
Secondary accession number(s): Q3TF32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 149 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.