Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14068 (XPO1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-1
Alternative name(s):
Caffeine resistance protein 2
Chromosome region maintenance protein 1
Gene names
Name:xpo1
Synonyms:caf2, crm1
ORF Names:SPAC1805.17, SPAC1B2.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1078 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the leucine-rich nuclear export signal (NES). Ref.9

Subunit structure

Interacts with php4. Ref.9

Subcellular location

Nucleus. Note: Localized in the nucleus and at its periphery.

Miscellaneous

Cellular target of leptomycin B (LMB), a nuclear export inhibitor. LMB alkylates Cys-529 leading to CRM1 inactivation.

Sequence similarities

Belongs to the exportin family.

Contains 1 importin N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10781078Exportin-1
PRO_0000204709

Regions

Domain34 – 10067Importin N-terminal

Experimental info

Mutagenesis1291E → K in crm1-1R-9R. Ref.6
Mutagenesis2991E → K in crm1-14-R. Ref.6
Mutagenesis4301E → K in crm1-809; cold-sensitive and LMB hypersensitive. Ref.6
Mutagenesis5031G → D in crm1-N1. Ref.4
Mutagenesis5291C → S in crm1-K1; LMB resistant. Ref.5
Mutagenesis5461M → I in crm1-N1. Ref.4
Mutagenesis9921F → S in crm1-119; LMB resistant. Ref.6
Sequence conflict192 – 20817EIFQL…AQKPS → RFFNYAHKFSNVRKNLA no nucleotide entry Ref.3
Sequence conflict192 – 20817EIFQL…AQKPS → RFFNYAHKFSNVRKNLA in BAA03858. Ref.4
Sequence conflict484 – 4852IV → VI in AAG35722. Ref.6
Sequence conflict9891Missing no nucleotide entry Ref.3

Sequences

Sequence LengthMass (Da)Tools
P14068 [UniParc].

Last modified August 14, 2001. Version 3.
Checksum: 6CFA6955F1DF9F6D

FASTA1,078123,567
        10         20         30         40         50         60 
MEGILAFDRE LDVALLDRVV QTFYQGVGAE QQQAQQVLTQ FQAHPDAWSQ AYSILEKSEY 

        70         80         90        100        110        120 
PQTKYIALSV LDKLITTRWK MLPKEQRLGI RNYIVAVMIK NSSDETVLQQ QKTFLNKLDL 

       130        140        150        160        170        180 
TLVQILKQEW PHNWPNFIPE IVQASKTNLS LCENNMIVLR LLSEEIFDYS AEQMTQLKTK 

       190        200        210        220        230        240 
NLKNQMCGEF AEIFQLCSQI LERAQKPSLI KATLGTLLRF LNWIPLGYIF ETNIVELITN 

       250        260        270        280        290        300 
RFLNVPDFRN VTIECLTEIA SLTSQPQYND KFVTMFNLVM TSVNSMLPLQ TDFREAYEES 

       310        320        330        340        350        360 
STNEQDFIQN LALFLCAFFS SHLRPLENPE NQEVLLNAHS YLLNISRINE REIFKICLEY 

       370        380        390        400        410        420 
WSKLVAQLYE EMQQIPMSEM NPLLNLSSPT SLISSNPNML ANLPLRKHIY KDILSTLRLV 

       430        440        450        460        470        480 
MIENMVKPEE VLIVENDEGE IVREFVKETD TITLYKSMRE VLVYLTHLDV VDTEIVMTEK 

       490        500        510        520        530        540 
LARIVVGTEW SWQNLNTLCW AIGSISGAMN EEMEKRFLVN VIKDLLGLCE MKRGKDNKAV 

       550        560        570        580        590        600 
VASNIMYVVG QYPRFLKAHW KFLKTVVNKL FEFMHEYHEG VQDMACDTFI KIAQKCRRHF 

       610        620        630        640        650        660 
VAQQLGETEP FINEIIRNLA KTTEDLTPQQ THTFYEACGY MISAQPQKHL QERLIFDLMA 

       670        680        690        700        710        720 
LPNQAWENIV AQAAQNAQVL GDPQTVKILA NVLKTNVAAC TSIGSGFYPQ IAKNYVDMLG 

       730        740        750        760        770        780 
LYKAVSGLIS EVVAAQGNIA TKTPHVRGLR TIKKEILKLV DAYISRAEDL ELVGNTLIPA 

       790        800        810        820        830        840 
LFEAVLLDYL QNVPDARDAE VLNLITTIVN QLSELLTDKI PLVLDAVFGC TLEMISKDFS 

       850        860        870        880        890        900 
EYPEHRAAFF QLLRAINLNC FPALLNIPAP QFKLVINSIV WSFKHVSRDI QETGLNILLE 

       910        920        930        940        950        960 
LINNMASMGP DVSNAFFQTY YISLLQDILY VLTDSDHKSG FKLQSLILAR LFYLVESNQI 

       970        980        990       1000       1010       1020 
TVPLYDPSQF PQEMNNQLFL RQYIMNLLVT AFPHLQPIQI QEFVQTVLAL NQDSIKFKLA 

      1030       1040       1050       1060       1070 
LRDFLIQLKE FGGDNAELYL EEKEQELAAQ QKAQLEKAMT VPGMIKPVDM PTMEEEEL 

« Hide

References

« Hide 'large scale' references
[1]"Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein preferentially localized in the nucleus and its periphery."
Adachi Y., Yanagida M.
J. Cell Biol. 108:1195-1207(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Adachi Y.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Fission yeast pap1-dependent transcription is negatively regulated by an essential nuclear protein, crm1."
Toda T., Shimanuki M., Saka Y., Yamano H., Adachi Y., Shirakawa M., Kyogoku Y., Yanagida M.
Mol. Cell. Biol. 12:5474-5484(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression."
Nishi K., Yoshida M., Fujiwara D., Nishikawa M., Horinouchi S., Beppu T.
J. Biol. Chem. 269:6320-6324(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-503 AND MET-546.
Strain: LM102.
[5]"Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region."
Kudo N., Matsumori N., Taoka H., Fujiwara D., Schreiner E.P., Wolff B., Yoshida M., Horinouchi S.
Proc. Natl. Acad. Sci. U.S.A. 96:9112-9117(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-529.
Strain: AC1 and FN41.
[6]"Sequence of Crm1/exportin 1 mutant alleles reveals critical sites associated with multidrug resistance."
Carobbio S., Realini C., Norbury C.J., Toda T., Cavalli F., Spataro V.
Curr. Genet. 39:2-9(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-129; GLU-299; GLU-430 AND PHE-992.
Strain: 972 / HM123.
[7]"Cloning of caf1+, caf2+ and caf4+ from Schizosaccharomyces pombe: their involvement in multidrug resistance, UV and pH sensitivity."
Benko Z., Sipiczki M., Carr A.M.
Mol. Gen. Genet. 260:434-443(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[9]"Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1."
Mercier A., Labbe S.
J. Biol. Chem. 284:20249-20262(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHP4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15482 Genomic DNA. Translation: CAB40824.2.
D16355 Genomic DNA. Translation: BAA03858.1.
AB027496 Genomic DNA. Translation: BAA83345.1.
AB027497 Genomic DNA. Translation: BAA83346.1.
AF208056 Genomic DNA. Translation: AAG35722.1.
CU329670 Genomic DNA. Translation: CAB55858.1.
PIRD45029.
T43511.
T50137.
RefSeqXP_001713070.1. XM_001713018.2.

3D structure databases

ProteinModelPortalP14068.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280563. 11 interactions.
MINTMINT-4687292.
STRING4896.SPAC1805.17-1.

Proteomic databases

MaxQBP14068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1805.17.1; SPAC1805.17.1:pep; SPAC1805.17.
GeneID3361487.
KEGGspo:SPAC1805.17.

Organism-specific databases

PomBaseSPAC1805.17.

Phylogenomic databases

eggNOGCOG5101.
KOK14290.
OMAILKQAWP.
OrthoDBEOG7MWH56.
PhylomeDBP14068.

Family and domain databases

Gene3D1.25.10.10. 5 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08767. CRM1_C. 1 hit.
PF03810. IBN_N. 1 hit.
PF08389. Xpo1. 1 hit.
[Graphical view]
SMARTSM01102. CRM1_C. 1 hit.
SM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20811530.
PROP14068.

Entry information

Entry nameXPO1_SCHPO
AccessionPrimary (citable) accession number: P14068
Secondary accession number(s): Q09197 expand/collapse secondary AC list , Q9HF66, Q9URF4, Q9UTF9, Q9UTG0, Q9UUL0, Q9UUL1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 14, 2001
Last modified: July 9, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names