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UniProtKB/Swiss-Prot entry Q02821

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IMA1_YEAST
Primary accession number Q02821
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 88)
Name and origin of the protein
Protein name Importin subunit alpha
Synonyms Karyopherin subunit alpha
Karyopherin-60
Serine-rich RNA polymerase I suppressor protein
Gene name
Name: SRP1
Synonyms: KAP60
OrderedLocusNames: YNL189W
ORFNames: N1606
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1448093 [NCBI, ExPASy, EBI, Israel, Japan]
Yano R., Oakes M., Yamaghishi M., Dodd J.A., Nomura M.;
"Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 12:5640-5651(1992).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 200060 / W303;
DOI=10.1007/BF02191602; PubMed=7565597 [NCBI, ExPASy, EBI, Israel, Japan]
Kuessel P., Frasch M.;
"Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis.";
Mol. Gen. Genet. 248:351-363(1995).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
 MUTAGENESIS.
PubMed=8041713 [NCBI, ExPASy, EBI, Israel, Japan]
Yano R., Oakes M.L., Tabb M.M., Nomura M.;
"Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure.";
Proc. Natl. Acad. Sci. U.S.A. 91:6880-6884(1994).
[5]
 IDENTIFICATION.
DOI=10.1074/jbc.270.28.16499; PubMed=7622450 [NCBI, ExPASy, EBI, Israel, Japan]
Enenkel C., Blobel G., Rexach M.;
"Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes.";
J. Biol. Chem. 270:16499-16502(1995).
[6]
 NUCLEOPORIN REPEAT BINDING REQUIREMENT.
DOI=10.1016/0092-8674(95)90181-7; PubMed=8521485 [NCBI, ExPASy, EBI, Israel, Japan]
Rexach M., Blobel G.;
"Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins.";
Cell 83:683-692(1995).
[7]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 89-510.
DOI=10.1016/S0092-8674(00)81419-1; PubMed=9695948 [NCBI, ExPASy, EBI, Israel, Japan]
Conti E., Uy M., Leighton L., Blobel G., Kuriyan J.;
"Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.";
Cell 94:193-204(1998).
[9]
 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-509 IN COMPLEX WITH NLS PEPTIDE.
DOI=10.1016/S0969-2126(00)00107-6; PubMed=10745017 [NCBI, ExPASy, EBI, Israel, Japan]
Conti E., Kuriyan J.;
"Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha.";
Structure 8:329-338(2000).
[10]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 88-530 IN COMPLEX WITH NUP2.
DOI=10.1093/emboj/cdg538; PubMed=14532109 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.;
"Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.";
EMBO J. 22:5358-5369(2003).
[11]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-530 IN COMPLEX WITH CSE1 AND RANGTP.
DOI=10.1038/nature03144; PubMed=15602554 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuura Y., Stewart M.;
"Structural basis for the assembly of a nuclear export complex.";
Nature 432:872-877(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M75849; AAA35090.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71465; CAA96083.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S30884; S30884.
RefSeq NP_014210.1; -.
3D structure databases
PDB
1BK5; X-ray; 2.20 A; A/B=89-510.[ExPASy / RCSB / EBI]
1BK6; X-ray; 2.80 A; A/B=89-510.[ExPASy / RCSB / EBI]
1EE4; X-ray; 2.10 A; A/B=87-509.[ExPASy / RCSB / EBI]
1EE5; X-ray; 2.40 A; A=87-510.[ExPASy / RCSB / EBI]
1UN0; X-ray; 2.60 A; A/B=88-530.[ExPASy / RCSB / EBI]
1WA5; X-ray; 2.00 A; B=1-530.[ExPASy / RCSB / EBI]
2C1T; X-ray; 2.60 A; A/B=88-541.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BK5; -.
1BK6; -.
1EE4; -.
1EE5; -.
1UN0; -.
1WA5; -.
2C1T; -.
ModBase Q02821.
Protein-protein interaction databases
DIP DIP:728N; -.
IntAct Q02821; -.
Organism-specific databases
CYGD YNL189w; -.
SGD S000005133; SRP1.
Yeast-GFP YNL189W.
Gene expression databases
ArrayExpress Q02821; -.
GermOnline YNL189W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0008320; Molecular function: protein transmembrane transporter activity (traceable author statement from SGD).
GO:0006913; Biological process: nucleocytoplasmic transport (traceable author statement from SGD).
GO:0006612; Biological process: protein targeting to membrane (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR000225; Armadillo.
IPR002652; Importin-a-like_IBB-bd.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
G3DSA:1.20.5.690; Importin-a-like_IBB-bd; 1.
Pfam PF00514; Arm; 8.
PF01749; IBB; 1.
Pfam graphical view of domain structure.
SMART SM00185; ARM; 8.
SMART graphical view of domain structure.
PROSITE PS50176; ARM_REPEAT; 2.
PS51214; IBB; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q02821.
ProtoNet Q02821.
Proteomic databases
PeptideAtlas Q02821; -.
Genome annotation databases
Ensembl YNL189W; Saccharomyces cerevisiae. [Contig view]
GeneID 855532; -.
GenomeReviews Y13139_GR; YNL189W.
KEGG sce:YNL189W; -.
NMPDR fig|4932.3.peg.5275; -.
Phylogenomic databases
HOGENOM Q02821; -.
Other
LinkHub Q02821; -.
NextBio 979583; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Protein transport; Repeat; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   542  542     Importin subunit alpha. PRO_0000120744
DOMAIN   1    65  65     IBB. 
REPEAT   89   122  34     ARM 1; truncated. 
REPEAT   123   162  40     ARM 2. 
REPEAT   163   204  42     ARM 3. 
REPEAT   205   251  47     ARM 4. 
REPEAT   252   288  37     ARM 5. 
REPEAT   289   330  42     ARM 6. 
REPEAT   331   372  42     ARM 7. 
REPEAT   373   417  45     ARM 8. 
REPEAT   418   471  54     ARM 9. 
REPEAT   472   508  37     ARM 10; atypical. 
REGION   209   335  127     NLS binding site 1. 
REGION   419   505  87     NLS binding site 2. 
MUTAGEN   116   116        S->F: In SRP1-31; temperature-sensitive mutant; reduced growth rate and chromosome loss. 
MUTAGEN   145   145        E->K: In SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology. 
MUTAGEN   219   219        P->Q: In SRP1-1; temperature-sensitive mutant. 
MUTAGEN   286   286        D->N: In SRP1-3; temperature-sensitive mutant. 
MUTAGEN   360   360        E->K: In SRP1-2; temperature-sensitive mutant. 
MUTAGEN   459   459        G->V: In SRP1-54; temperature-sensitive mutant; reduced growth rate. 
HELIX   15    17  3      
HELIX   90    96  7      
HELIX   101   114  14      
HELIX   123   128  6      
HELIX   132   137  6      
HELIX   145   159  15      
HELIX   163   171  9      
HELIX   175   184  10      
HELIX   187   203  17      
HELIX   205   213  9      
HELIX   217   222  6      
HELIX   223   225  3      
HELIX   229   243  15      
STRAND   246   248  3      
HELIX   252   255  4      
HELIX   256   258  3      
HELIX   259   265  7      
HELIX   271   284  14      
HELIX   289   297  9      
HELIX   301   307  7      
HELIX   313   326  14      
HELIX   331   339  9      
HELIX   342   349  8      
HELIX   355   369  15      
HELIX   373   381  9      
HELIX   385   394  10      
HELIX   397   412  16      
TURN   413   416  4      
HELIX   418   426  9      
HELIX   430   439  10      
HELIX   442   465  24      
HELIX   472   480  9      
HELIX   482   488  7      
HELIX   489   491  3      
HELIX   495   508  14      
Sequence information
Length: 542 AA [This is the length of the unprocessed precursor] Molecular weight: 60441 Da [This is the MW of the unprocessed precursor] CRC64: 8D3A0CB76F2E7C00 [This is a checksum on the sequence] 
        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
Q02821 in FASTA format

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