P14068 (XPO1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	1078 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Nucleus
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to caffeine Inferred from mutant phenotype PubMed 9211790. Source: PomBase cellular response to oxidative stress Inferred from mutant phenotype PubMed 12896976. Source: PomBase negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.3. Source: PomBase positive regulation of transcription factor import into nucleus Inferred from mutant phenotype PubMed 9585505. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nuclear periphery Inferred from direct assay Ref.1. Source: PomBase nuclear pore Inferred from sequence model. Source: PomBase
Molecular_function	GTP binding Non-traceable author statement. Source: PomBase nuclear export signal receptor activity Inferred from direct assay Ref.5. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1078	1078	Exportin-1		PRO_0000204709
Regions
	Domain	34 – 100	67	Importin N-terminal
Experimental info
	Mutagenesis	129	1	E → K in crm1-1R-9R. Ref.6
	Mutagenesis	299	1	E → K in crm1-14-R. Ref.6
	Mutagenesis	430	1	E → K in crm1-809; cold-sensitive and LMB hypersensitive. Ref.6
	Mutagenesis	503	1	G → D in crm1-N1. Ref.4
	Mutagenesis	529	1	C → S in crm1-K1; LMB resistant. Ref.5
	Mutagenesis	546	1	M → I in crm1-N1. Ref.4
	Mutagenesis	992	1	F → S in crm1-119; LMB resistant. Ref.6
	Sequence conflict	192 – 208	17	EIFQL…AQKPS → RFFNYAHKFSNVRKNLA no nucleotide entry Ref.3
	Sequence conflict	192 – 208	17	EIFQL…AQKPS → RFFNYAHKFSNVRKNLA in BAA03858. Ref.4
	Sequence conflict	484 – 485	2	IV → VI in AAG35722. Ref.6
	Sequence conflict	989	1	Missing no nucleotide entry Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P14068 [UniParc]. Last modified August 14, 2001. Version 3. Checksum: 6CFA6955F1DF9F6D	FASTA	1,078	123,567
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	D45029. T43511. T50137.
RefSeq	XP_001713070.1. XM_001713018.2.
3D structure databases
ProteinModelPortal	P14068.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4687292.
STRING	4896.SPAC1805.17-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1805.17.1; SPAC1805.17.1:pep; SPAC1805.17.
GeneID	3361487.
KEGG	spo:SPAC1805.17.
Organism-specific databases
PomBase	SPAC1805.17.
Phylogenomic databases
eggNOG	COG5101.
KO	K14290.
OMA	SAPENIS.
OrthoDB	EOG4MSH68.
Family and domain databases
Gene3D	1.25.10.10. 5 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR014877. CRM1_C_dom. IPR013598. Exportin-1/Importin-b-like. IPR001494. Importin-beta_N. [Graphical view]
Pfam	PF08767. CRM1_C. 1 hit. PF03810. IBN_N. 1 hit. PF08389. Xpo1. 1 hit. [Graphical view]
SMART	SM01102. CRM1_C. 1 hit. SM00913. IBN_N. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 2 hits.
PROSITE	PS50166. IMPORTIN_B_NT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20811530.

Entry information

Entry name

XPO1_SCHPO

Accession

Primary (citable) accession number: P14068
Secondary accession number(s): Q09197 , Q9HF66, Q9URF4, Q9UTF9, Q9UTG0, Q9UUL0, Q9UUL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	August 14, 2001
Last modified:	May 29, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program