XPO1_SCHPO
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 25-MAY-2022, entry version 177.
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}.
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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; 4896.SPAC1805.17.1; -.
DR MaxQB; P14068; -.
DR PaxDb; P14068; -.
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; HNINTLC; -.
DR PhylomeDB; P14068; -.
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; ISO:PomBase.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 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; PTHR11223; 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; SSF48371; 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
