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Protein

Importin subunit alpha

Gene

SRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).By similarity3 Publications

GO - Molecular functioni

  • nuclear localization sequence binding Source: GO_Central
  • protein transporter activity Source: SGD

GO - Biological processi

  • NLS-bearing protein import into nucleus Source: GO_Central
  • proteasome localization Source: SGD
  • protein import into nucleus Source: SGD
  • protein targeting to membrane Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha
Alternative name(s):
Karyopherin subunit alpha
Karyopherin-60
Serine-rich RNA polymerase I suppressor protein
Gene namesi
Name:SRP1
Synonyms:KAP60
Ordered Locus Names:YNL189W
ORF Names:N1606
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL189W.
SGDiS000005133. SRP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: GO_Central
  • nuclear pore Source: GO_Central
  • nucleoplasm Source: GO_Central
  • nucleus Source: SGD
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi116S → F in SRP1-31; temperature-sensitive mutant; reduced growth rate and chromosome loss. 1 Publication1
Mutagenesisi145E → K in SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology. 1 Publication1
Mutagenesisi219P → Q in SRP1-1; temperature-sensitive mutant. 1 Publication1
Mutagenesisi286D → N in SRP1-3; temperature-sensitive mutant. 1 Publication1
Mutagenesisi360E → K in SRP1-2; temperature-sensitive mutant. 1 Publication1
Mutagenesisi459G → V in SRP1-54; temperature-sensitive mutant; reduced growth rate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001207441 – 542Importin subunit alphaAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ02821.
PRIDEiQ02821.

PTM databases

iPTMnetiQ02821.

Interactioni

Subunit structurei

Forms a complex with an importin beta subunit. In the nucleus, interacts with NUP2 which accelerate release of NLSs, NUP2 is subsequently displaced by CSE1:RanGTP which mediates re-export and recycling. Interacts with HEH2, SHE2, and STS1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBC2Q089203EBI-1797,EBI-33556
CSE1P333072EBI-1797,EBI-5168
KAP95Q061425EBI-1797,EBI-9145
NUP2P324993EBI-1797,EBI-12401

Protein-protein interaction databases

BioGridi35644. 247 interactors.
DIPiDIP-728N.
IntActiQ02821. 135 interactors.
MINTiMINT-386354.

Structurei

Secondary structure

1542
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 17Combined sources3
Helixi89 – 96Combined sources8
Beta strandi97 – 99Combined sources3
Helixi101 – 114Combined sources14
Beta strandi118 – 120Combined sources3
Helixi123 – 128Combined sources6
Helixi132 – 137Combined sources6
Helixi145 – 158Combined sources14
Helixi163 – 171Combined sources9
Helixi175 – 184Combined sources10
Helixi187 – 201Combined sources15
Helixi205 – 213Combined sources9
Helixi217 – 222Combined sources6
Helixi223 – 225Combined sources3
Helixi229 – 243Combined sources15
Beta strandi246 – 248Combined sources3
Helixi252 – 255Combined sources4
Helixi256 – 258Combined sources3
Helixi259 – 265Combined sources7
Helixi271 – 285Combined sources15
Beta strandi286 – 288Combined sources3
Helixi289 – 297Combined sources9
Helixi301 – 306Combined sources6
Helixi307 – 309Combined sources3
Helixi313 – 326Combined sources14
Helixi331 – 339Combined sources9
Helixi342 – 349Combined sources8
Helixi355 – 368Combined sources14
Helixi373 – 381Combined sources9
Helixi385 – 394Combined sources10
Helixi397 – 413Combined sources17
Turni414 – 416Combined sources3
Helixi419 – 426Combined sources8
Helixi430 – 436Combined sources7
Turni437 – 439Combined sources3
Helixi442 – 466Combined sources25
Helixi472 – 479Combined sources8
Helixi482 – 487Combined sources6
Helixi488 – 491Combined sources4
Beta strandi492 – 494Combined sources3
Helixi495 – 508Combined sources14
Beta strandi509 – 511Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BK5X-ray2.20A/B89-510[»]
1BK6X-ray2.80A/B89-510[»]
1EE4X-ray2.10A/B87-509[»]
1EE5X-ray2.40A87-510[»]
1UN0X-ray2.60A/B88-530[»]
1WA5X-ray2.00B1-530[»]
2C1TX-ray2.60A/B88-541[»]
4PVZX-ray2.50A/B88-509[»]
4XZRX-ray2.25B88-509[»]
ProteinModelPortaliQ02821.
SMRiQ02821.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 65IBBPROSITE-ProRule annotationAdd BLAST65
Repeati89 – 122ARM 1; truncatedPROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati123 – 162ARM 2PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati163 – 204ARM 3PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati205 – 251ARM 4PROSITE-ProRule annotation1 PublicationAdd BLAST47
Repeati252 – 288ARM 5PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati289 – 330ARM 6PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati331 – 372ARM 7PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati373 – 417ARM 8PROSITE-ProRule annotation1 PublicationAdd BLAST45
Repeati418 – 471ARM 9PROSITE-ProRule annotation1 PublicationAdd BLAST54
Repeati472 – 508ARM 10; atypicalPROSITE-ProRule annotation1 PublicationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 335NLS binding site 1Add BLAST127
Regioni419 – 505NLS binding site 2Add BLAST87

Domaini

The 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

GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
InParanoidiQ02821.
OMAiNREQIQC.
OrthoDBiEOG092C1PRY.

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.

Q02821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNGTDSSTS KFVPEYRRTN FKNKGRFSAD ELRRRRDTQQ VELRKAKRDE
60 70 80 90 100
ALAKRRNFIP PTDGADSDEE DESSVSADQQ FYSQLQQELP QMTQQLNSDD
110 120 130 140 150
MQEQLSATVK FRQILSREHR PPIDVVIQAG VVPRLVEFMR ENQPEMLQLE
160 170 180 190 200
AAWALTNIAS GTSAQTKVVV DADAVPLFIQ LLYTGSVEVK EQAIWALGNV
210 220 230 240 250
AGDSTDYRDY VLQCNAMEPI LGLFNSNKPS LIRTATWTLS NLCRGKKPQP
260 270 280 290 300
DWSVVSQALP TLAKLIYSMD TETLVDACWA ISYLSDGPQE AIQAVIDVRI
310 320 330 340 350
PKRLVELLSH ESTLVQTPAL RAVGNIVTGN DLQTQVVINA GVLPALRLLL
360 370 380 390 400
SSPKENIKKE ACWTISNITA GNTEQIQAVI DANLIPPLVK LLEVAEYKTK
410 420 430 440 450
KEACWAISNA SSGGLQRPDI IRYLVSQGCI KPLCDLLEIA DNRIIEVTLD
460 470 480 490 500
ALENILKMGE ADKEARGLNI NENADFIEKA GGMEKIFNCQ QNENDKIYEK
510 520 530 540
AYKIIETYFG EEEDAVDETM APQNAGNTFG FGSNVNQQFN FN
Length:542
Mass (Da):60,441
Last modified:July 1, 1993 - v1
Checksum:i8D3A0CB76F2E7C00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75849 Genomic DNA. Translation: AAA35090.1.
Z71465 Genomic DNA. Translation: CAA96083.1.
BK006947 Genomic DNA. Translation: DAA10364.1.
PIRiS30884.
RefSeqiNP_014210.1. NM_001183027.1.

Genome annotation databases

EnsemblFungiiYNL189W; YNL189W; YNL189W.
GeneIDi855532.
KEGGisce:YNL189W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M75849 Genomic DNA. Translation: AAA35090.1.
Z71465 Genomic DNA. Translation: CAA96083.1.
BK006947 Genomic DNA. Translation: DAA10364.1.
PIRiS30884.
RefSeqiNP_014210.1. NM_001183027.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BK5X-ray2.20A/B89-510[»]
1BK6X-ray2.80A/B89-510[»]
1EE4X-ray2.10A/B87-509[»]
1EE5X-ray2.40A87-510[»]
1UN0X-ray2.60A/B88-530[»]
1WA5X-ray2.00B1-530[»]
2C1TX-ray2.60A/B88-541[»]
4PVZX-ray2.50A/B88-509[»]
4XZRX-ray2.25B88-509[»]
ProteinModelPortaliQ02821.
SMRiQ02821.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35644. 247 interactors.
DIPiDIP-728N.
IntActiQ02821. 135 interactors.
MINTiMINT-386354.

PTM databases

iPTMnetiQ02821.

Proteomic databases

MaxQBiQ02821.
PRIDEiQ02821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL189W; YNL189W; YNL189W.
GeneIDi855532.
KEGGisce:YNL189W.

Organism-specific databases

EuPathDBiFungiDB:YNL189W.
SGDiS000005133. SRP1.

Phylogenomic databases

GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
InParanoidiQ02821.
OMAiNREQIQC.
OrthoDBiEOG092C1PRY.

Enzyme and pathway databases

BioCyciYEAST:G3O-33200-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02821.
PROiQ02821.

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...

Entry informationi

Entry nameiIMA1_YEAST
AccessioniPrimary (citable) accession number: Q02821
Secondary accession number(s): D6W0Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds to nucleoporin FxFG but not GLFG repeat regions. Ran-GTP can disrupt the karyopherin heterodimer by binding to the beta subunit and releases both subunits from the docking site.
Present with 2790 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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.