XPO1_RAT
ID XPO1_RAT Reviewed; 1071 AA.
AC Q80U96;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Exportin-1;
DE Short=Exp1;
DE AltName: Full=Chromosome region maintenance 1 protein homolog;
GN Name=Xpo1; Synonyms=Crm1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=11689633; DOI=10.1128/jvi.75.23.11515-11525.2001;
RA Hakata Y., Yamada M., Shida H.;
RT "Rat CRM1 is responsible for the poor activity of human T-cell leukemia
RT virus type 1 Rex protein in rat cells.";
RL J. Virol. 75:11515-11525(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448; SER-450 AND TYR-454, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-966, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates the nuclear export of cellular proteins (cargos)
CC bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the
CC nucleus, in association with RANBP3, binds cooperatively to the NES on
CC its target protein and to the GTPase Ran in its active GTP-bound form.
CC Docking of this complex to the nuclear pore complex (NPC) is mediated
CC through binding to nucleoporins. Upon transit of a nuclear export
CC complex into the cytoplasm, disassembling of the complex and hydrolysis
CC of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively)
CC cause release of the cargo from the export receptor. The directionality
CC of nuclear export is thought to be conferred by an asymmetric
CC distribution of the GTP- and GDP-bound forms of Ran between the
CC cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal
CC bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Component of a
CC nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1.
CC Found in a trimeric export complex with SNUPN, RAN and XPO1. Found in a
CC nuclear export complex with RANBP3 and RAN. Found in a 60S ribosomal
CC subunit export complex with NMD3, RAN, XPO1. Interacts with DDX3X,
CC NMD3, NUP42, NUP88, NUP214, RANBP3 and TERT. Interacts with NEMF (via
CC its N-terminus). Interacts with the monomeric form of BIRC5/survivin
CC deacetylated at 'Lys-129'. Interacts with DTNBP1 and SERTAD2; the
CC interactions translocate DTNBP1 and SERTAD2 out of the nucleus.
CC Interacts with ATF2. Interacts with SLC35G1 and STIM1. Interacts with
CC DCAF8. Interacts with CPEB3. Interacts with HAX1. Interacts with BOK;
CC translocates to the cytoplasm (By similarity). Interacts with HSP90AB1
CC (By similarity). {ECO:0000250|UniProtKB:O14980,
CC ECO:0000250|UniProtKB:Q6P5F9}.
CC -!- INTERACTION:
CC Q80U96; P0DJZ2: NS2; Xeno; NbExp=2; IntAct=EBI-9517348, EBI-9673535;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=Located in the nucleoplasm, Cajal bodies and
CC nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; AB105193; BAC65240.1; -; mRNA.
DR RefSeq; NP_445942.1; NM_053490.1.
DR RefSeq; XP_006251640.1; XM_006251578.3.
DR AlphaFoldDB; Q80U96; -.
DR SMR; Q80U96; -.
DR IntAct; Q80U96; 1.
DR STRING; 10116.ENSRNOP00000014062; -.
DR iPTMnet; Q80U96; -.
DR PhosphoSitePlus; Q80U96; -.
DR SwissPalm; Q80U96; -.
DR jPOST; Q80U96; -.
DR PaxDb; Q80U96; -.
DR PRIDE; Q80U96; -.
DR GeneID; 85252; -.
DR KEGG; rno:85252; -.
DR UCSC; RGD:620517; rat.
DR CTD; 7514; -.
DR RGD; 620517; Xpo1.
DR VEuPathDB; HostDB:ENSRNOG00000009935; -.
DR eggNOG; KOG2020; Eukaryota.
DR HOGENOM; CLU_011906_0_0_1; -.
DR InParanoid; Q80U96; -.
DR OMA; HNINTLC; -.
DR OrthoDB; 132850at2759; -.
DR PhylomeDB; Q80U96; -.
DR TreeFam; TF105695; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-RNO-9707616; Heme signaling.
DR PRO; PR:Q80U96; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000009935; Expressed in thymus and 20 other tissues.
DR Genevisible; Q80U96; RN.
DR GO; GO:0005642; C:annulate lamellae; ISO:RGD.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:RGD.
DR GO; GO:0006611; P:protein export from nucleus; IDA:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:RGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; ISO:RGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; ISO:RGD.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:RGD.
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; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; mRNA transport; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; RNA-binding; Transport.
FT CHAIN 1..1071
FT /note="Exportin-1"
FT /id="PRO_0000204707"
FT DOMAIN 46..112
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 217..240
FT /note="HEAT 1"
FT REPEAT 241..277
FT /note="HEAT 2"
FT REPEAT 354..472
FT /note="HEAT 3"
FT REPEAT 515..553
FT /note="HEAT 4"
FT REPEAT 560..597
FT /note="HEAT 5"
FT REPEAT 602..639
FT /note="HEAT 6"
FT REPEAT 775..813
FT /note="HEAT 7"
FT REPEAT 885..916
FT /note="HEAT 8"
FT REPEAT 917..954
FT /note="HEAT 9"
FT REPEAT 1002..1039
FT /note="HEAT 10"
FT REGION 327..450
FT /note="Necessary for interaction with Ran and nuclear
FT export complex formation"
FT /evidence="ECO:0000250"
FT REGION 411..481
FT /note="Necessary for interaction with RANBP3"
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 454
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 693
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
SQ SEQUENCE 1071 AA; 123039 MW; CFF018979B93F70D CRC64;
MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL THLKEHPDAW
TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE GIKKYVVGLI IKTSSDPTCV
EKEKVYIGKL NMILVQILKQ EWPKHWPTFI SDIVGASRTS ESLCQNNMVI LKLLSEEVFD
FSSGQITQVK AKHLKDSMCN EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY
IFETKLISTL IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFETLFTLT MMQLKQMLPL
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHGQLLEKR LNLREALMEA LHYMLLVSEV
EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF DIPPRRQLYL TVLSKVRLLM
VSRMAKPEEV LVVENDQGEV VREFMKDTDS INLYKNMRET LVYLTHLDYV DTEIIMTKKL
QNQVNGTEWS WKNLNTLCWA IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII
ASNIMYIVGQ YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ EHLIEKYMLL
PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK AVGHPFVIQL GRIYLDMLNV
YKCLSENISA AIQANGEMVT KQPLIRSMRT VKRETLKLIS GWVSRSNDPQ MVAENFVPPL
LDAVLIDYQR NVPAAREPEV LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE
YPEHRTNFFL LLQAVNSHCF PAFLAIPPAQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF NLVEEGKIST
PLNPGSPVSN QMFIQDYVAN LLKSAFPHLQ DAQVKLFVTG LFSLNQDIPA FKEHLRDFLV
QIKEFAGEDT SDLFLEERET ALRQAQEEKH KLQMSVPGIL NPHEIPEEMC D
