XPO2_MOUSE
ID XPO2_MOUSE Reviewed; 971 AA.
AC Q9ERK4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Exportin-2;
DE Short=Exp2;
DE AltName: Full=Chromosome segregation 1-like protein;
DE AltName: Full=Importin-alpha re-exporter;
GN Name=Cse1l; Synonyms=Xpo2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cJ;
RX PubMed=11564884; DOI=10.1128/mcb.21.20.7020-7024.2001;
RA Bera T.K., Bera J., Brinkmann U., Tessarollo L., Pastan I.;
RT "Cse1l is essential for early embryonic growth and development.";
RL Mol. Cell. Biol. 21:7020-7024(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Export receptor for importin-alpha. Mediates importin-alpha
CC re-export from the nucleus to the cytoplasm after import substrates
CC (cargos) have been released into the nucleoplasm. In the nucleus binds
CC cooperatively to importin-alpha and to the GTPase Ran in its active
CC GTP-bound form. Docking of this trimeric complex to the nuclear pore
CC complex (NPC) is mediated through binding to nucleoporins. Upon transit
CC of a nuclear export complex into the cytoplasm, disassembling of the
CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and
CC RANGAP1, respectively) cause release of the importin-alpha from the
CC export receptor. CSE1L/XPO2 then return to the nuclear compartment and
CC mediate another round of transport. The directionality of nuclear
CC export is thought to be conferred by an asymmetric distribution of the
CC GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
CC {ECO:0000250|UniProtKB:P55060}.
CC -!- SUBUNIT: Found in a complex with CSE1L/XPO2, Ran and KPNA2. Binds with
CC high affinity to importin-alpha only in the presence of RanGTP. The
CC complex is dissociated by the combined action of RanBP1 and RanGAP1.
CC Interacts with CFTR. {ECO:0000250|UniProtKB:P55060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55060}. Nucleus
CC {ECO:0000250|UniProtKB:P55060}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:P55060}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in embryos from 5 to 17 dpc.
CC Highly expressed in adult testis, heart, brain, lung, liver, skeletal
CC muscle, spleen and kidney. {ECO:0000269|PubMed:11564884}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality at around 5.5 dpc.
CC {ECO:0000269|PubMed:11564884}.
CC -!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
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DR EMBL; AF301152; AAG24636.1; -; mRNA.
DR CCDS; CCDS17092.1; -.
DR RefSeq; NP_076054.1; NM_023565.3.
DR AlphaFoldDB; Q9ERK4; -.
DR SMR; Q9ERK4; -.
DR BioGRID; 225874; 34.
DR IntAct; Q9ERK4; 7.
DR MINT; Q9ERK4; -.
DR STRING; 10090.ENSMUSP00000002790; -.
DR iPTMnet; Q9ERK4; -.
DR PhosphoSitePlus; Q9ERK4; -.
DR SwissPalm; Q9ERK4; -.
DR EPD; Q9ERK4; -.
DR jPOST; Q9ERK4; -.
DR MaxQB; Q9ERK4; -.
DR PaxDb; Q9ERK4; -.
DR PeptideAtlas; Q9ERK4; -.
DR PRIDE; Q9ERK4; -.
DR ProteomicsDB; 300007; -.
DR Antibodypedia; 28372; 553 antibodies from 40 providers.
DR DNASU; 110750; -.
DR Ensembl; ENSMUST00000002790; ENSMUSP00000002790; ENSMUSG00000002718.
DR GeneID; 110750; -.
DR KEGG; mmu:110750; -.
DR UCSC; uc008nys.2; mouse.
DR CTD; 1434; -.
DR MGI; MGI:1339951; Cse1l.
DR VEuPathDB; HostDB:ENSMUSG00000002718; -.
DR eggNOG; KOG1992; Eukaryota.
DR GeneTree; ENSGT00550000074884; -.
DR HOGENOM; CLU_009614_0_0_1; -.
DR InParanoid; Q9ERK4; -.
DR OMA; YRYEFKS; -.
DR OrthoDB; 1248958at2759; -.
DR PhylomeDB; Q9ERK4; -.
DR TreeFam; TF300473; -.
DR BioGRID-ORCS; 110750; 30 hits in 70 CRISPR screens.
DR ChiTaRS; Cse1l; mouse.
DR PRO; PR:Q9ERK4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ERK4; protein.
DR Bgee; ENSMUSG00000002718; Expressed in embryonic post-anal tail and 88 other tissues.
DR ExpressionAtlas; Q9ERK4; baseline and differential.
DR Genevisible; Q9ERK4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR005043; XPO2_C.
DR InterPro; IPR013713; XPO2_central.
DR Pfam; PF03378; CAS_CSE1; 1.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 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 Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..971
FT /note="Exportin-2"
FT /id="PRO_0000117288"
FT DOMAIN 29..102
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55060"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55060"
FT MOD_RES 574
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55060"
FT MOD_RES 824
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55060"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55060"
SQ SEQUENCE 971 AA; 110455 MW; 041335E17593F3F2 CRC64;
MELSDANLQT LTEYLKKTLD PDPAIRRPAE KFLESVEGNQ NYPLLLLTLL EKSQDNVIKV
CASVTFKNYI KRNWRIVEDE PNKICEADRV AIKANIVHLM LSSPEQIQKQ LSDAISIIGR
EDFPQKWPDL LTEMVNRFQS GDFHVINGVL RTAHSLFKRY RHEFKSNELW TEIKLVLDAF
ALPLTNLFKA TIELCSTHAN DASALRILFS SLILISKLFY SLNFQDLPEF FEDNMETWMN
NFHTLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQRYL PRFVTAIWNL
LVTTGREVKY DLLVSNAIQF LASVCERPHY KNLFEDQNTL TSICEKVIVP NMEFRAADEE
AFEDNSEEYI RRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLQEYAKNP
SVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLTEF FVNHILPDLK SNNVNEFPVL
KADGIKYIMI FRNQVPKEHL LVSIPLLISH LEAESIVVHT YAAHALERLF TMRGSNNTTL
FTAAEIAPFV EILLTNLFKA LTLPGSSENE YIMKAIMRSF SLLQEAIIPY IPTLITQLTQ
KLLAVSKNPS KPHFNHYMFE AICLSIRITC KANPAAVVNF EEALFLVFTE ILQNDVQEFI
PYVFQVMSLL LETHKNDIPS SYMALFPHLL QPVLWERTGN IPALVRLLQA FLERGSSTIA
TAAADKIPGL LGVFQKLIAS KANDHQGFYL LNSIIEHMPP ESVDQYRKQI FILLFQRLQN
SKTTKFIKSF LVFINLYCIK YGALALQEIF DGIQPKMFGM VLEKIIIPEI QKVSGNVEKK
ICAVGITKLL TECPPMMDTE YTKLWTPLLQ SLIGLFELPE DDSIPDEEHF IDIEDTPGYQ
TAFSQLAFAG KKEHDPVGQM VNNPKIHLAQ SLHKLSTACP GRVPSMVSTS LNAEALQYLQ
GYLQAASVTL L
