ID   XPO2_PONAB              Reviewed;         971 AA.
AC   Q5R9J2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
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DR   EMBL; CR859395; CAH91568.1; -; mRNA.
DR   RefSeq; NP_001125921.1; NM_001132449.2.
DR   AlphaFoldDB; Q5R9J2; -.
DR   SMR; Q5R9J2; -.
DR   STRING; 9601.ENSPPYP00000023647; -.
DR   GeneID; 100172855; -.
DR   KEGG; pon:100172855; -.
DR   CTD; 1434; -.
DR   eggNOG; KOG1992; Eukaryota.
DR   InParanoid; Q5R9J2; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..971
FT                   /note="Exportin-2"
FT                   /id="PRO_0000237679"
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;  110328 MW;  2036A4405D1D9C43 CRC64;
     MELSDANLQT PTEYLKKTLD PDPAIRRPAE KFLESVEGNQ NYPLLLLTLL EKSQDNVIKV
     CASVTFKNYI KRNWRIVEDE PNKICEADRV AIKANIVHLM LSSPEQIQKQ LSDAISIIGR
     EDFPQKWPDL LTEMVNRFQS GDFHVINGVL RTAHSLFKRY RHEFKSNELW TETKLVLDAF
     ALPLTNLFKA TIELCSTHAN DASALRILFS SLILISKLFY SLNFQDLPEF FEDNMETWMN
     NFHTLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQRYL PRFVTAIWNL
     LVTTGQEVKY DLLVSNAIQF LASVCERPHY KNLFEDQNTL TSICEKVIVP NMEFRAADEE
     AFEDNSEEYI RRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLQEYAKNP
     SVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLTEF FVNHILPDLK SANVNEFPVL
     KADGIKYIMI FRNQVPKEHL LVSIPLLINH LQAESIVVHT YAAHALERLF TMRGPNNATL
     FTAAEIAPFV EILLTNLFKA LTLPGSSENE YIMKAIMRSF SLLQEAIIPY IPTLITQLTQ
     KLLAVSKNPS KPHFNHYMSE AICLSIRITC KANPAAVVNF EEALFLVFTE ILQNDVQEFI
     PYVFQVMSLL LETHKNDIPS SYMALFPHLL QPVLWERTGN IPALVRLLQA FLERGSNTIA
     SAAADKIPGL LGVFQKLIAS KANDHQGFYL LNSIIEHMPP ESVDQYRKQI FILLFQRLQN
     SKTTKFIKSF LVFINLYCIK YGALALQEIF DGIQPKMFGM VLEKIIIPEI QKVSGNVEKK
     ICAVGITKLL TECPPMMDTE YTKLWTPLLQ SLIGLFELPE DDTIPDEEHF IDIEDTPGYQ
     TAFSQLAFAG KKEHDPVGQM VNNPKIHLAQ SLHKLSTACP GRVPSMVSTS LNAEALQYLQ
     GYLQAASVTL L