CSE1_YEAST
ID CSE1_YEAST Reviewed; 960 AA.
AC P33307; D6VV96;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Importin alpha re-exporter;
DE AltName: Full=Chromosome segregation protein CSE1;
GN Name=CSE1; OrderedLocusNames=YGL238W; ORFNames=HRC135;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8336709; DOI=10.1128/mcb.13.8.4691-4702.1993;
RA Xiao Z., McGrew J.T., Schroeder A.J., Fitzgerald-Hayes M.;
RT "CSE1 and CSE2, two new genes required for accurate mitotic chromosome
RT segregation in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:4691-4702(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8750240; DOI=10.1002/yea.320111507;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left
RT arm of chromosome VII, reveals the presence of eight open reading frames.";
RL Yeast 11:1519-1523(1995).
RN [5]
RP FUNCTION.
RX PubMed=9744791; DOI=10.1016/s0014-5793(98)00892-8;
RA Kunzler M., Hurt E.C.;
RT "Cse1p functions as the nuclear export receptor for importin alpha in
RT yeast.";
RL FEBS Lett. 433:185-190(1998).
RN [6]
RP FUNCTION.
RX PubMed=9857050; DOI=10.1074/jbc.273.52.35142;
RA Hood J.K., Silver P.A.;
RT "Cse1p is required for export of Srp1p/importin-alpha from the nucleus in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:35142-35146(1998).
RN [7]
RP FUNCTION.
RX PubMed=9774694; DOI=10.1128/mcb.18.11.6805;
RA Solsbacher J., Maurer P., Bischoff F.R., Schlenstedt G.;
RT "Cse1p is involved in export of yeast importin alpha from the nucleus.";
RL Mol. Cell. Biol. 18:6805-6815(1998).
RN [8]
RP FUNCTION.
RX PubMed=10394916; DOI=10.1007/s004380050022;
RA Schroeder A.J., Chen X.H., Xiao Z., Fitzgerald-Hayes M.;
RT "Genetic evidence for interactions between yeast importin alpha (Srp1p) and
RT its nuclear export receptor, Cse1p.";
RL Mol. Gen. Genet. 261:788-795(1999).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SRP1 CARGO AND DOG
RP RANGTP.
RX PubMed=15602554; DOI=10.1038/nature03144;
RA Matsuura Y., Stewart M.;
RT "Structural basis for the assembly of a nuclear export complex.";
RL Nature 432:872-877(2004).
CC -!- FUNCTION: Export receptor for importin alpha (SRP1). Mediates importin-
CC alpha re-export from the nucleus to the cytoplasm after import
CC substrates have been released into the nucleoplasm.
CC {ECO:0000269|PubMed:10394916, ECO:0000269|PubMed:9744791,
CC ECO:0000269|PubMed:9774694, ECO:0000269|PubMed:9857050}.
CC -!- SUBUNIT: Binds with high affinity to SRP1 only in the presence of
CC RanGTP. The complex is dissociated by the RanGTP-binding protein YRB1.
CC {ECO:0000269|PubMed:15602554}.
CC -!- INTERACTION:
CC P33307; Q02821: SRP1; NbExp=2; IntAct=EBI-5168, EBI-1797;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 23500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
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DR EMBL; L14838; AAA34531.1; -; Genomic_DNA.
DR EMBL; Z72761; CAA96957.1; -; Genomic_DNA.
DR EMBL; Z49149; CAA89018.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07880.1; -; Genomic_DNA.
DR PIR; A48083; A48083.
DR RefSeq; NP_011276.1; NM_001181104.1.
DR PDB; 1WA5; X-ray; 2.00 A; C=1-960.
DR PDB; 1Z3H; X-ray; 3.10 A; A/B=1-960.
DR PDBsum; 1WA5; -.
DR PDBsum; 1Z3H; -.
DR AlphaFoldDB; P33307; -.
DR SMR; P33307; -.
DR BioGRID; 33001; 247.
DR DIP; DIP-1131N; -.
DR IntAct; P33307; 22.
DR MINT; P33307; -.
DR STRING; 4932.YGL238W; -.
DR iPTMnet; P33307; -.
DR MaxQB; P33307; -.
DR PaxDb; P33307; -.
DR PRIDE; P33307; -.
DR EnsemblFungi; YGL238W_mRNA; YGL238W; YGL238W.
DR GeneID; 852612; -.
DR KEGG; sce:YGL238W; -.
DR SGD; S000003207; CSE1.
DR VEuPathDB; FungiDB:YGL238W; -.
DR eggNOG; KOG1992; Eukaryota.
DR GeneTree; ENSGT00550000074884; -.
DR HOGENOM; CLU_009614_0_0_1; -.
DR InParanoid; P33307; -.
DR OMA; YRYEFKS; -.
DR BioCyc; YEAST:G3O-30711-MON; -.
DR EvolutionaryTrace; P33307; -.
DR PRO; PR:P33307; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33307; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IGI:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; IGI:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0061015; P:snRNA import into nucleus; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID50075; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR005043; XPO2_C.
DR InterPro; IPR013713; XPO2_central.
DR Pfam; PF03378; CAS_CSE1; 1.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..960
FT /note="Importin alpha re-exporter"
FT /id="PRO_0000117293"
FT REPEAT 1..33
FT /note="HEAT 1"
FT DOMAIN 23..96
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 34..73
FT /note="HEAT 2"
FT REPEAT 74..120
FT /note="HEAT 3"
FT REPEAT 121..157
FT /note="HEAT 4"
FT REPEAT 158..220
FT /note="HEAT 5"
FT REPEAT 221..278
FT /note="HEAT 6"
FT REPEAT 279..323
FT /note="HEAT 7"
FT REPEAT 324..392
FT /note="HEAT 8"
FT REPEAT 393..445
FT /note="HEAT 9"
FT REPEAT 446..489
FT /note="HEAT 10"
FT REPEAT 490..528
FT /note="HEAT 11"
FT REPEAT 529..586
FT /note="HEAT 12"
FT REPEAT 587..630
FT /note="HEAT 13"
FT REPEAT 631..674
FT /note="HEAT 14"
FT REPEAT 675..716
FT /note="HEAT 15"
FT REPEAT 717..751
FT /note="HEAT 16"
FT REPEAT 752..794
FT /note="HEAT 17"
FT REPEAT 795..826
FT /note="HEAT 18"
FT REPEAT 827..928
FT /note="HEAT 19; with insert"
FT REPEAT 929..960
FT /note="HEAT 20"
FT MOTIF 366..381
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT CONFLICT 515
FT /note="Y -> D (in Ref. 1; AAA34531)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1Z3H"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 161..191
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 196..215
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1Z3H"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 278..297
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 306..320
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 393..413
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 491..504
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 546..557
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 585..588
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 592..606
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 613..628
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 635..651
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 658..671
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:1Z3H"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 698..712
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 720..730
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 736..749
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 752..755
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 759..772
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 776..792
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 795..803
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 809..816
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 818..821
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 828..843
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 846..851
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 853..855
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 856..868
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:1Z3H"
FT HELIX 899..901
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 914..916
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 917..932
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:1Z3H"
FT HELIX 937..941
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 947..957
FT /evidence="ECO:0007829|PDB:1WA5"
SQ SEQUENCE 960 AA; 109356 MW; 0A32D221DFC2C483 CRC64;
MSDLETVAKF LAESVIASTA KTSERNLRQL ETQDGFGLTL LHVIASTNLP LSTRLAGALF
FKNFIKRKWV DENGNHLLPA NNVELIKKEI VPLMISLPNN LQVQIGEAIS SIADSDFPDR
WPTLLSDLAS RLSNDDMVTN KGVLTVAHSI FKRWRPLFRS DELFLEIKLV LDVFTAPFLN
LLKTVDEQIT ANENNKASLN ILFDVLLVLI KLYYDFNCQD IPEFFEDNIQ VGMGIFHKYL
SYSNPLLEDP DETEHASVLI KVKSSIQELV QLYTTRYEDV FGPMINEFIQ ITWNLLTSIS
NQPKYDILVS KSLSFLTAVT RIPKYFEIFN NESAMNNITE QIILPNVTLR EEDVELFEDD
PIEYIRRDLE GSDTDTRRRA CTDFLKELKE KNEVLVTNIF LAHMKGFVDQ YMSDPSKNWK
FKDLYIYLFT ALAINGNITN AGVSSTNNLL NVVDFFTKEI APDLTSNNIP HIILRVDAIK
YIYTFRNQLT KAQLIELMPI LATFLQTDEY VVYTYAAITI EKILTIRESN TSPAFIFHKE
DISNSTEILL KNLIALILKH GSSPEKLAEN EFLMRSIFRV LQTSEDSIQP LFPQLLAQFI
EIVTIMAKNP SNPRFTHYTF ESIGAILNYT QRQNLPLLVD SMMPTFLTVF SEDIQEFIPY
VFQIIAFVVE QSATIPESIK PLAQPLLAPN VWELKGNIPA VTRLLKSFIK TDSSIFPDLV
PVLGIFQRLI ASKAYEVHGF DLLEHIMLLI DMNRLRPYIK QIAVLLLQRL QNSKTERYVK
KLTVFFGLIS NKLGSDFLIH FIDEVQDGLF QQIWGNFIIT TLPTIGNLLD RKIALIGVLN
MVINGQFFQS KYPTLISSTM NSIIETASSQ SIANLKNDYV DLDNLEEIST FGSHFSKLVS
ISEKPFDPLP EIDVNNGVRL YVAEALNKYN AISGNTFLNT ILPQLTQENQ VKLNQLLVGN
