ID XPO2_BOVIN Reviewed; 971 AA.
AC A5D785;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 08-NOV-2023, entry version 78.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) 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; BC140465; AAI40466.1; -; mRNA.
DR RefSeq; NP_001014933.2; NM_001014933.3.
DR AlphaFoldDB; A5D785; -.
DR SMR; A5D785; -.
DR STRING; 9913.ENSBTAP00000047927; -.
DR PaxDb; 9913-ENSBTAP00000047927; -.
DR PeptideAtlas; A5D785; -.
DR GeneID; 518622; -.
DR KEGG; bta:518622; -.
DR CTD; 1434; -.
DR eggNOG; KOG1992; Eukaryota.
DR InParanoid; A5D785; -.
DR OrthoDB; 178772at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
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; Leucine-rich Repeat Variant; 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 PANTHER; PTHR10997:SF8; EXPORTIN-2; 1.
DR PANTHER; PTHR10997; IMPORTIN-7, 8, 11; 1.
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; ARM repeat; 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_0000342152"
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; 110375 MW; 8188231B6322F3CA 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
LVTTGQEVKY DLLVSNAIQF LASVCERPHY KNLFEDQNTL TSICEKVIVP NMEFRAADEE
AFEDNSEEYI RRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLQEYAKNP
SVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLTEF FVNHILPDLK SANVNEFPVL
KADGIKYITI FRNQVPKEHL LVSIPLLINH LQAESIVVHT YAAHALERLF TMRGPNSATL
FTAAEIAPFV EILLTNLFKA LTLPGSSENE YIMKAIMRSF SLLQEAIIPY IPTLITQLTQ
KLLAVSKNPS KPHFNHYMFE AICLSIRITC KSNPAAVVNF 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
//
