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Q02821 (IMA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Importin subunit alpha
Alternative name(s):
Karyopherin subunit alpha
Karyopherin-60
Serine-rich RNA polymerase I suppressor protein
Gene names
Name:SRP1
Synonyms:KAP60
Ordered Locus Names:YNL189W
ORF Names:N1606
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.13

Subunit structure

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. Ref.8 Ref.10 Ref.12 Ref.13

Subcellular location

Cytoplasmperinuclear region. Note: Mainly localized at the periphery of the nucleus.

Domain

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.

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.

Sequence similarities

Belongs to the importin alpha family.

Contains 10 ARM repeats.

Contains 1 IBB domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Importin subunit alpha
PRO_0000120744

Regions

Domain1 – 6565IBB
Repeat89 – 12234ARM 1; truncated
Repeat123 – 16240ARM 2
Repeat163 – 20442ARM 3
Repeat205 – 25147ARM 4
Repeat252 – 28837ARM 5
Repeat289 – 33042ARM 6
Repeat331 – 37242ARM 7
Repeat373 – 41745ARM 8
Repeat418 – 47154ARM 9
Repeat472 – 50837ARM 10; atypical
Region209 – 335127NLS binding site 1
Region419 – 50587NLS binding site 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14

Experimental info

Mutagenesis1161S → F in SRP1-31; temperature-sensitive mutant; reduced growth rate and chromosome loss.
Mutagenesis1451E → K in SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology.
Mutagenesis2191P → Q in SRP1-1; temperature-sensitive mutant.
Mutagenesis2861D → N in SRP1-3; temperature-sensitive mutant.
Mutagenesis3601E → K in SRP1-2; temperature-sensitive mutant.
Mutagenesis4591G → V in SRP1-54; temperature-sensitive mutant; reduced growth rate.

Secondary structure

........................................................................ 542
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02821 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 8D3A0CB76F2E7C00

FASTA54260,441
        10         20         30         40         50         60 
MDNGTDSSTS KFVPEYRRTN FKNKGRFSAD ELRRRRDTQQ VELRKAKRDE ALAKRRNFIP 

        70         80         90        100        110        120 
PTDGADSDEE DESSVSADQQ FYSQLQQELP QMTQQLNSDD MQEQLSATVK FRQILSREHR 

       130        140        150        160        170        180 
PPIDVVIQAG VVPRLVEFMR ENQPEMLQLE AAWALTNIAS GTSAQTKVVV DADAVPLFIQ 

       190        200        210        220        230        240 
LLYTGSVEVK EQAIWALGNV AGDSTDYRDY VLQCNAMEPI LGLFNSNKPS LIRTATWTLS 

       250        260        270        280        290        300 
NLCRGKKPQP DWSVVSQALP TLAKLIYSMD TETLVDACWA ISYLSDGPQE AIQAVIDVRI 

       310        320        330        340        350        360 
PKRLVELLSH ESTLVQTPAL RAVGNIVTGN DLQTQVVINA GVLPALRLLL SSPKENIKKE 

       370        380        390        400        410        420 
ACWTISNITA GNTEQIQAVI DANLIPPLVK LLEVAEYKTK KEACWAISNA SSGGLQRPDI 

       430        440        450        460        470        480 
IRYLVSQGCI KPLCDLLEIA DNRIIEVTLD ALENILKMGE ADKEARGLNI NENADFIEKA 

       490        500        510        520        530        540 
GGMEKIFNCQ QNENDKIYEK AYKIIETYFG EEEDAVDETM APQNAGNTFG FGSNVNQQFN 


FN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae."
Yano R., Oakes M., Yamaghishi M., Dodd J.A., Nomura M.
Mol. Cell. Biol. 12:5640-5651(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 [GENOMIC DNA], FUNCTION.
Strain: ATCC 200060 / W303.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure."
Yano R., Oakes M.L., Tabb M.M., Nomura M.
Proc. Natl. Acad. Sci. U.S.A. 91:6880-6884(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[6]"Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes."
Enenkel C., Blobel G., Rexach M.
J. Biol. Chem. 270:16499-16502(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins."
Rexach M., Blobel G.
Cell 83:683-692(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOPORIN REPEAT BINDING REQUIREMENT.
[8]"Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation."
Tabb M.M., Tongaonkar P., Vu L., Nomura M.
Mol. Cell. Biol. 20:6062-6073(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STS1.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Karyopherin-mediated import of integral inner nuclear membrane proteins."
King M.C., Lusk C.P., Blobel G.
Nature 442:1003-1007(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEH2.
[11]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[12]"Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p."
Shen Z., Paquin N., Forget A., Chartrand P.
Mol. Biol. Cell 20:2265-2275(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHE2.
[13]"Sts1 plays a key role in targeting proteasomes to the nucleus."
Chen L., Romero L., Chuang S.M., Tournier V., Joshi K.K., Lee J.A., Kovvali G., Madura K.
J. Biol. Chem. 286:3104-3118(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STS1.
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha."
Conti E., Uy M., Leighton L., Blobel G., Kuriyan J.
Cell 94:193-204(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 89-510.
[16]"Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha."
Conti E., Kuriyan J.
Structure 8:329-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-509 IN COMPLEX WITH NLS PEPTIDE.
[17]"Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import."
Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.
EMBO J. 22:5358-5369(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 88-530 IN COMPLEX WITH NUP2.
[18]"Structural basis for the assembly of a nuclear export complex."
Matsuura Y., Stewart M.
Nature 432:872-877(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-530 IN COMPLEX WITH CSE1 AND RANGTP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75849 Genomic DNA. Translation: AAA35090.1.
Z71465 Genomic DNA. Translation: CAA96083.1.
BK006947 Genomic DNA. Translation: DAA10364.1.
PIRS30884.
RefSeqNP_014210.1. NM_001183027.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ02821.
SMRQ02821. Positions 37-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35644. 240 interactions.
DIPDIP-728N.
IntActQ02821. 134 interactions.
MINTMINT-386354.
STRING4932.YNL189W.

Proteomic databases

PaxDbQ02821.
PeptideAtlasQ02821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL189W; YNL189W; YNL189W.
GeneID855532.
KEGGsce:YNL189W.

Organism-specific databases

CYGDYNL189w.
SGDS000005133. SRP1.

Phylogenomic databases

eggNOGCOG5064.
GeneTreeENSGT00610000085856.
HOGENOMHOG000167616.
OMAEMIANIQ.
OrthoDBEOG7DC2DF.

Enzyme and pathway databases

BioCycYEAST:G3O-33200-MONOMER.

Gene expression databases

GenevestigatorQ02821.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamPF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFPIRSF005673. Importin_alpha. 1 hit.
SMARTSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 2 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02821.
NextBio979583.
PROQ02821.

Entry information

Entry nameIMA1_YEAST
AccessionPrimary (citable) accession number: Q02821
Secondary accession number(s): D6W0Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: March 19, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references