ID   XPO2_DANRE              Reviewed;         971 AA.
AC   Q7SZC2; G1K2H9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 106.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|Ensembl:ENSDARP00000022858, ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Ensembl:ENSDARP00000022858,
RC   ECO:0000312|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, INTERACTION WITH CFTR, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=20933420; DOI=10.1016/j.cub.2010.09.012;
RA   Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S.,
RA   Gabriel S., Mostov K., Huisken J., Stainier D.Y.;
RT   "Cse1l is a negative regulator of CFTR-dependent fluid secretion.";
RL   Curr. Biol. 20:1840-1845(2010).
CC   -!- FUNCTION: Export receptor for importin alpha. Mediates importin-alpha
CC       re-export from the nucleus to the cytoplasm after import substrates
CC       have been released into the nucleoplasm (By similarity). Negatively
CC       regulates fluid secretion and plays a role in fluid homeostasis by
CC       down-regulating cftr activity (PubMed:20933420).
CC       {ECO:0000250|UniProtKB:P55060, ECO:0000269|PubMed:20933420}.
CC   -!- SUBUNIT: Interacts with cftr (PubMed:20933420).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20933420}. Nucleus
CC       {ECO:0000250|UniProtKB:P55060}. Apical cell membrane
CC       {ECO:0000269|PubMed:20933420}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:20933420}. Basal cell membrane
CC       {ECO:0000269|PubMed:20933420}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:20933420}. Lateral cell membrane
CC       {ECO:0000269|PubMed:20933420}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:20933420}. Note=Shuttles between the nucleus and
CC       the cytoplasm. {ECO:0000250|UniProtKB:P55060}.
CC   -!- TISSUE SPECIFICITY: Detected in larval gut, liver, exocrine pancreas
CC       and part of the brain and retina at 96 hpf.
CC       {ECO:0000269|PubMed:20933420}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes strong
CC       expansion of the gut lumen, due to excessive fluid accumulation.
CC       {ECO:0000269|PubMed:20933420}.
CC   -!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
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DR   EMBL; CR559931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052479; AAH52479.1; -; mRNA.
DR   EMBL; BC066737; AAH66737.1; -; mRNA.
DR   RefSeq; NP_958858.1; NM_201450.1.
DR   AlphaFoldDB; Q7SZC2; -.
DR   SMR; Q7SZC2; -.
DR   BioGRID; 78862; 1.
DR   STRING; 7955.ENSDARP00000022858; -.
DR   PaxDb; Q7SZC2; -.
DR   PRIDE; Q7SZC2; -.
DR   Ensembl; ENSDART00000013203; ENSDARP00000022858; ENSDARG00000006963.
DR   GeneID; 30707; -.
DR   KEGG; dre:30707; -.
DR   CTD; 1434; -.
DR   ZFIN; ZDB-GENE-990603-1; cse1l.
DR   eggNOG; KOG1992; Eukaryota.
DR   GeneTree; ENSGT00550000074884; -.
DR   InParanoid; Q7SZC2; -.
DR   OMA; YRYEFKS; -.
DR   OrthoDB; 1248958at2759; -.
DR   PhylomeDB; Q7SZC2; -.
DR   TreeFam; TF300473; -.
DR   PRO; PR:Q7SZC2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 11.
DR   Bgee; ENSDARG00000006963; Expressed in mature ovarian follicle and 32 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
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:0007589; P:body fluid secretion; IMP:ZFIN.
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   Cell membrane; Cytoplasm; Membrane; Nucleus; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..971
FT                   /note="Exportin-2"
FT                   /id="PRO_0000237680"
FT   DOMAIN          29..102
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   CONFLICT        48
FT                   /note="A -> T (in Ref. 2; AAH52479/AAH66737)"
SQ   SEQUENCE   971 AA;  110028 MW;  632AFF088108925D CRC64;
     MELNDGNLQT LTEYLQKTLS ADPAVRRPAE KFLESVEGNQ NYPILLLAVL EKSQNEVIRV
     CSAVTFKNYI KRNWRIVEDE PNKISDPDRT AIKANIVNLM LTSPEQIQKQ LSDAISIIGR
     EDFPLKWPDL LTEMVNRFQS GDFHIINGVL RTAHSLFKRY RHEFKSNELW SEIKLVLDTF
     AQPLTELFKA TIELCQTHAT DINALKVLFS SLTLISKLFY SLNFQDLPEF FEDNMETWMT
     NFHNLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQPYL PRFVTAIWNL
     LVTTGQEVKY DLLVSNAIQF LASVCERPHY KHLFEDQNVL TSICEKVIVP NMEFRSADEE
     AFEDNSEEYI IRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLAEYAKNP
     GVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLSEF FLNHILIDLK SPNVNEFPVL
     KSDAIKYVMT FRSQLPKEQL LQAVPLLVSH LQAESIVQHT YAAHALERLF TMRGGNNTTL
     ITPTEMAPFT EQLLNHLFKA LAIPGSSENE YIMKAIMRSF SLLQEAIVPY IPTLIGQLTH
     KLLLVSKNPS KPHFNHYLFE SLCLSIRITC KANPDTVSSF EEALFPVFTE ILQNDVQEFV
     PYVFQVMSLL LEIHSNSIPS SYMALFPHLL QPVLWERTGN IPPLVRLLQA YLEKGAAAIA
     NTASDKIPGL LGVFQKLIAS KANDHQGFYL LNSIVEHMPA EAITQYRKQI FILLFQRLQS
     SKTTKFVKSF LVFINLYSVK YGAIALQEIF DDIQPKMFGM VVEKIVIPEV QKVSGQVEKK
     ICAVGIIKIL TECPAMMDTE YTKLWAPLLQ ALIGLFELPE DDSIPDDEHF IDIEDTPGYQ
     TAFSQLAFAG KKEHDPIGDA VSNPKILLAQ SLHKLSTACP GRVPSMLSTS LPTEALQFLQ
     GYLQAATVQL V