ID   XPO1_SCHPO              Reviewed;        1078 AA.
AC   P14068; Q09197; Q9HF66; Q9URF4; Q9UTF9; Q9UTG0; Q9UUL0; Q9UUL1;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 3.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Exportin-1;
DE   AltName: Full=Caffeine resistance protein 2;
DE   AltName: Full=Chromosome region maintenance protein 1;
GN   Name=xpo1; Synonyms=caf2, crm1; ORFNames=SPAC1805.17, SPAC1B2.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2647765; DOI=10.1083/jcb.108.4.1195;
RA   Adachi Y., Yanagida M.;
RT   "Higher order chromosome structure is affected by cold-sensitive mutations
RT   in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein
RT   preferentially localized in the nucleus and its periphery.";
RL   J. Cell Biol. 108:1195-1207(1989).
RN   [2]
RP   SEQUENCE REVISION.
RA   Adachi Y.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1448080; DOI=10.1128/mcb.12.12.5474-5484.1992;
RA   Toda T., Shimanuki M., Saka Y., Yamano H., Adachi Y., Shirakawa M.,
RA   Kyogoku Y., Yanagida M.;
RT   "Fission yeast pap1-dependent transcription is negatively regulated by an
RT   essential nuclear protein, crm1.";
RL   Mol. Cell. Biol. 12:5474-5484(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-503 AND MET-546.
RC   STRAIN=LM102;
RX   PubMed=8119981; DOI=10.1016/s0021-9258(17)37374-x;
RA   Nishi K., Yoshida M., Fujiwara D., Nishikawa M., Horinouchi S., Beppu T.;
RT   "Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear
RT   protein, involved in control of higher order chromosome structure and gene
RT   expression.";
RL   J. Biol. Chem. 269:6320-6324(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-529.
RC   STRAIN=AC1, and FN41;
RX   PubMed=10430904; DOI=10.1073/pnas.96.16.9112;
RA   Kudo N., Matsumori N., Taoka H., Fujiwara D., Schreiner E.P., Wolff B.,
RA   Yoshida M., Horinouchi S.;
RT   "Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a
RT   cysteine residue in the central conserved region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:9112-9117(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLU-129; GLU-299;
RP   GLU-430 AND PHE-992.
RC   STRAIN=972 / HM123;
RX   PubMed=11318103; DOI=10.1007/s002940000170;
RA   Carobbio S., Realini C., Norbury C.J., Toda T., Cavalli F., Spataro V.;
RT   "Sequence of Crm1/exportin 1 mutant alleles reveals critical sites
RT   associated with multidrug resistance.";
RL   Curr. Genet. 39:2-9(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9894913; DOI=10.1007/s004380050914;
RA   Benko Z., Sipiczki M., Carr A.M.;
RT   "Cloning of caf1+, caf2+ and caf4+ from Schizosaccharomyces pombe: their
RT   involvement in multidrug resistance, UV and pH sensitivity.";
RL   Mol. Gen. Genet. 260:434-443(1998).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH PHP4.
RX   PubMed=19502236; DOI=10.1074/jbc.m109.009563;
RA   Mercier A., Labbe S.;
RT   "Both Php4 function and subcellular localization are regulated by iron via
RT   a multistep mechanism involving the glutaredoxin Grx4 and the exportin
RT   Crm1.";
RL   J. Biol. Chem. 284:20249-20262(2009).
CC   -!- FUNCTION: Receptor for the leucine-rich nuclear export signal (NES).
CC       {ECO:0000269|PubMed:19502236}.
CC   -!- SUBUNIT: Interacts with php4. {ECO:0000269|PubMed:19502236}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Localized in the nucleus and at its
CC       periphery.
CC   -!- MISCELLANEOUS: Cellular target of leptomycin B (LMB), a nuclear export
CC       inhibitor. LMB alkylates Cys-529 leading to CRM1 inactivation.
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15482; CAB40824.2; -; Genomic_DNA.
DR   EMBL; D16355; BAA03858.1; -; Genomic_DNA.
DR   EMBL; AB027496; BAA83345.1; -; Genomic_DNA.
DR   EMBL; AB027497; BAA83346.1; -; Genomic_DNA.
DR   EMBL; AF208056; AAG35722.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB55858.1; -; Genomic_DNA.
DR   PIR; D45029; D45029.
DR   PIR; T43511; T43511.
DR   PIR; T50137; T50137.
DR   RefSeq; XP_001713070.1; XM_001713018.2.
DR   AlphaFoldDB; P14068; -.
DR   SMR; P14068; -.
DR   BioGRID; 280563; 21.
DR   STRING; 284812.P14068; -.
DR   MaxQB; P14068; -.
DR   PaxDb; 4896-SPAC1805-17-1; -.
DR   EnsemblFungi; SPAC1805.17.1; SPAC1805.17.1:pep; SPAC1805.17.
DR   PomBase; SPAC1805.17; -.
DR   VEuPathDB; FungiDB:SPAC1805.17; -.
DR   eggNOG; KOG2020; Eukaryota.
DR   HOGENOM; CLU_011906_0_0_1; -.
DR   InParanoid; P14068; -.
DR   OMA; WAFKHNN; -.
DR   PhylomeDB; P14068; -.
DR   Reactome; R-SPO-5687128; MAPK6/MAPK4 signaling.
DR   PRO; PR:P14068; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; ISM:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005525; F:GTP binding; NAS:PomBase.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IDA:PomBase.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006611; P:protein export from nucleus; IMP:PomBase.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR041123; CRM1_repeat.
DR   InterPro; IPR041235; Exp1_repeat_2.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR045065; XPO1/5.
DR   InterPro; IPR014877; XPO1_C_dom.
DR   InterPro; IPR040485; XPO1_repeat_3.
DR   PANTHER; PTHR11223; EXPORTIN 1/5; 1.
DR   PANTHER; PTHR11223:SF2; EXPORTIN-1; 1.
DR   Pfam; PF08767; CRM1_C; 1.
DR   Pfam; PF18777; CRM1_repeat; 1.
DR   Pfam; PF18784; CRM1_repeat_2; 1.
DR   Pfam; PF18787; CRM1_repeat_3; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF08389; Xpo1; 1.
DR   SMART; SM01102; CRM1_C; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1078
FT                   /note="Exportin-1"
FT                   /id="PRO_0000204709"
FT   DOMAIN          34..100
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   MUTAGEN         129
FT                   /note="E->K: In crm1-1R-9R."
FT                   /evidence="ECO:0000269|PubMed:11318103"
FT   MUTAGEN         299
FT                   /note="E->K: In crm1-14-R."
FT                   /evidence="ECO:0000269|PubMed:11318103"
FT   MUTAGEN         430
FT                   /note="E->K: In crm1-809; cold-sensitive and LMB
FT                   hypersensitive."
FT                   /evidence="ECO:0000269|PubMed:11318103"
FT   MUTAGEN         503
FT                   /note="G->D: In crm1-N1."
FT                   /evidence="ECO:0000269|PubMed:8119981"
FT   MUTAGEN         529
FT                   /note="C->S: In crm1-K1; LMB resistant."
FT                   /evidence="ECO:0000269|PubMed:10430904"
FT   MUTAGEN         546
FT                   /note="M->I: In crm1-N1."
FT                   /evidence="ECO:0000269|PubMed:8119981"
FT   MUTAGEN         992
FT                   /note="F->S: In crm1-119; LMB resistant."
FT                   /evidence="ECO:0000269|PubMed:11318103"
FT   CONFLICT        192..208
FT                   /note="EIFQLCSQILERAQKPS -> RFFNYAHKFSNVRKNLA (in Ref. 3;
FT                   no nucleotide entry and 4; BAA03858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484..485
FT                   /note="IV -> VI (in Ref. 6; AAG35722)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        989
FT                   /note="Missing (in Ref. 3; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1078 AA;  123567 MW;  6CFA6955F1DF9F6D CRC64;
     MEGILAFDRE LDVALLDRVV QTFYQGVGAE QQQAQQVLTQ FQAHPDAWSQ AYSILEKSEY
     PQTKYIALSV LDKLITTRWK MLPKEQRLGI RNYIVAVMIK NSSDETVLQQ QKTFLNKLDL
     TLVQILKQEW PHNWPNFIPE IVQASKTNLS LCENNMIVLR LLSEEIFDYS AEQMTQLKTK
     NLKNQMCGEF AEIFQLCSQI LERAQKPSLI KATLGTLLRF LNWIPLGYIF ETNIVELITN
     RFLNVPDFRN VTIECLTEIA SLTSQPQYND KFVTMFNLVM TSVNSMLPLQ TDFREAYEES
     STNEQDFIQN LALFLCAFFS SHLRPLENPE NQEVLLNAHS YLLNISRINE REIFKICLEY
     WSKLVAQLYE EMQQIPMSEM NPLLNLSSPT SLISSNPNML ANLPLRKHIY KDILSTLRLV
     MIENMVKPEE VLIVENDEGE IVREFVKETD TITLYKSMRE VLVYLTHLDV VDTEIVMTEK
     LARIVVGTEW SWQNLNTLCW AIGSISGAMN EEMEKRFLVN VIKDLLGLCE MKRGKDNKAV
     VASNIMYVVG QYPRFLKAHW KFLKTVVNKL FEFMHEYHEG VQDMACDTFI KIAQKCRRHF
     VAQQLGETEP FINEIIRNLA KTTEDLTPQQ THTFYEACGY MISAQPQKHL QERLIFDLMA
     LPNQAWENIV AQAAQNAQVL GDPQTVKILA NVLKTNVAAC TSIGSGFYPQ IAKNYVDMLG
     LYKAVSGLIS EVVAAQGNIA TKTPHVRGLR TIKKEILKLV DAYISRAEDL ELVGNTLIPA
     LFEAVLLDYL QNVPDARDAE VLNLITTIVN QLSELLTDKI PLVLDAVFGC TLEMISKDFS
     EYPEHRAAFF QLLRAINLNC FPALLNIPAP QFKLVINSIV WSFKHVSRDI QETGLNILLE
     LINNMASMGP DVSNAFFQTY YISLLQDILY VLTDSDHKSG FKLQSLILAR LFYLVESNQI
     TVPLYDPSQF PQEMNNQLFL RQYIMNLLVT AFPHLQPIQI QEFVQTVLAL NQDSIKFKLA
     LRDFLIQLKE FGGDNAELYL EEKEQELAAQ QKAQLEKAMT VPGMIKPVDM PTMEEEEL
//