ID   XPO6A_XENLA             Reviewed;        1135 AA.
AC   Q53I77; Q5U4U2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Exportin-6-A;
GN   Name=xpo6-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN ACTIN AND PROFILIN-ACTIN COMPLEXES
RP   EXPORT, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Egg;
RX   PubMed=16489345; DOI=10.1038/ncb1357;
RA   Bohnsack M.T., Stueven T., Kuhn C., Cordes V.C., Goerlich D.;
RT   "A selective block of nuclear actin export stabilizes the giant nuclei of
RT   Xenopus oocytes.";
RL   Nat. Cell Biol. 8:257-263(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the nuclear export of actin and profilin-actin
CC       complexes in somatic cells. Oocyte nuclei lack active actin export.
CC       {ECO:0000269|PubMed:16489345}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16489345}. Cytoplasm
CC       {ECO:0000269|PubMed:16489345}. Note=Shuttles between the nucleus and
CC       the cytoplasm. {ECO:0000269|PubMed:16489345}.
CC   -!- TISSUE SPECIFICITY: Expressed during meiotic maturation 2 hours after
CC       germinal vesicle break down (GVBD) and in unfertilized and fertilized
CC       eggs, but not in oocytes (at protein level). Expressed in somatic
CC       cells, in oocytes, during meiotic maturation and in unfertilized and
CC       fertilized eggs. {ECO:0000269|PubMed:16489345}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 8, 12 and 30 hours post-
CC       fertilization (hpf). {ECO:0000269|PubMed:16489345}.
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR   EMBL; AJ865375; CAI26296.1; -; mRNA.
DR   EMBL; BC084952; AAH84952.1; -; mRNA.
DR   RefSeq; NP_001088605.1; NM_001095136.1.
DR   AlphaFoldDB; Q53I77; -.
DR   SMR; Q53I77; -.
DR   DNASU; 495496; -.
DR   GeneID; 495496; -.
DR   KEGG; xla:495496; -.
DR   CTD; 495496; -.
DR   Xenbase; XB-GENE-6253815; xpo6.S.
DR   OrthoDB; 214523at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 495496; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR040016; XPO6.
DR   PANTHER; PTHR21452; PTHR21452; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF08389; Xpo1; 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   Cytoplasm; Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1135
FT                   /note="Exportin-6-A"
FT                   /id="PRO_0000235303"
FT   DOMAIN          31..97
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   CONFLICT        790
FT                   /note="A -> V (in Ref. 2; AAH84952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1135 AA;  129849 MW;  00625E5C910A4A95 CRC64;
     MASEEASLRA LESLMSEFFH NGTSNERKRE IESLLNNFAQ QLGAWRFCFY FLSQSQNDYV
     LMYSLSVFEN MINKMWLGVP SQEKMEIRNS LPKLLLSQHK SLPSFICNKL CKVIVDMGRQ
     DWPMFYHDFF TNILQLIQTP STTPLGLIML KTASEELACP REDLIVARKE ELRKLLLEQV
     PTVLDLLTGV LESIWDKHSI TAATPPPSPT ASDTDDLLSN LIHTPNLTKQ LSQPPPSLEA
     ESERVCALAL ECLSHLFSWI PLSASITPSL LTTIFQFARL GCDARSRQTN SVTTNTTASV
     VNGRSSSPPT APARDLARLG VLAMSCINEL MCKNCVPLEF QEYLLRVCQQ TFYLLQRITR
     ETNAHSVRSR FEELDESYVE KFTDFLRLFV SVHLRRIESN AQFPLLEFLT LLFKYTFHQP
     TREGYLSCLD IWAQFLDYLT NKIRNRLEDR DAIIGRYEDA LVLLLNEVLN RIQFRYNQTQ
     LEELDDETLD DDQQTEWQRY LRHSLEVVAK IMDLLPTHAF SKLFAALQEN LNVYLGLQRC
     LVTNGNDQRL NVTAENDCRR LHCSLRDLSS LLQAVGRLAE YFIGDMFGAR FNDALTVVER
     LVEVTLYGSR IKLYNMETAV PSVLKPDLID VHAQSLAALQ AYSHWLARYY SEVQRQNPEQ
     FISIISTAME ALPPLISTKV QEKLLLSACH LLVSIATTVR PMFLLNIPSV QKVFSRVTDS
     SAQRLPEEAQ VLLCRALSNV LLLPWPNVPE GEQQWAERSS HHSNLLNALT RDYRLLKGSS
     LPQRKGQLEA TKRVICQTLG VLRDIVENIS GEGTKSRQIC YQSLQESAQL SLTLFPAYIH
     QSDVTEEMLS FFLALFQGLR VQMGAPFTEQ IIQTFLNMFT REQLAESILQ EGSAGCHVVE
     KFLKILQVVV QEPGQSFKPF LPSILSLCME QLYPIIAERP SPDVKAELFE LLFQLLHHNW
     RYFYRSSVLA SVHRDGSDEP MENQAQFIVV MQAFGQSFLQ PDIHIFRQNL SYLETLNSKH
     KLYHKKLFQT GMLPQFVSVL LQVLIHKSHD LLQEEIGIAV YNMASVDFST FFSTFLPEFL
     TGCQGLDTSQ KSVLARNFKM ERDLPSFTQS VHRLVNDLRY YRLCNDSLPP GTVKL