XPO6_MOUSE
ID XPO6_MOUSE Reviewed; 1125 AA.
AC Q924Z6; Q3U3K7; Q6PEF3; Q9D0K9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Exportin-6;
DE Short=Exp6;
DE AltName: Full=Ran-binding protein 20;
GN Name=Xpo6; Synonyms=Ranbp20;
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] (ISOFORM 1).
RA Hartmann E., Goerlich D.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; THR-201; THR-204;
RP SER-208 AND SER-224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, 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).
RN [5]
RP FUNCTION.
RX PubMed=22323606; DOI=10.1073/pnas.1118880109;
RA Dopie J., Skarp K.P., Rajakyla E.K., Tanhuanpaa K., Vartiainen M.K.;
RT "Active maintenance of nuclear actin by importin 9 supports
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E544-E552(2012).
CC -!- FUNCTION: Mediates the nuclear export of actin and profilin-actin
CC complexes in somatic cells. {ECO:0000269|PubMed:22323606}.
CC -!- SUBUNIT: Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts
CC with ACTB. Interacts with ACTB in a RanGTP-dependent manner.
CC {ECO:0000250|UniProtKB:Q96QU8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96QU8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96QU8}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q96QU8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q924Z6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924Z6-2; Sequence=VSP_018467;
CC Name=3;
CC IsoId=Q924Z6-3; Sequence=VSP_018466, VSP_018468;
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY029528; AAK40296.1; -; mRNA.
DR EMBL; AK011324; BAB27545.1; -; mRNA.
DR EMBL; AK154709; BAE32778.1; -; mRNA.
DR EMBL; BC058090; AAH58090.1; -; mRNA.
DR CCDS; CCDS52396.1; -. [Q924Z6-2]
DR CCDS; CCDS80800.1; -. [Q924Z6-1]
DR RefSeq; NP_001298072.1; NM_001311143.1. [Q924Z6-1]
DR RefSeq; NP_083092.2; NM_028816.2. [Q924Z6-2]
DR AlphaFoldDB; Q924Z6; -.
DR SMR; Q924Z6; -.
DR STRING; 10090.ENSMUSP00000009344; -.
DR iPTMnet; Q924Z6; -.
DR PhosphoSitePlus; Q924Z6; -.
DR EPD; Q924Z6; -.
DR jPOST; Q924Z6; -.
DR MaxQB; Q924Z6; -.
DR PaxDb; Q924Z6; -.
DR PeptideAtlas; Q924Z6; -.
DR PRIDE; Q924Z6; -.
DR ProteomicsDB; 299720; -. [Q924Z6-1]
DR ProteomicsDB; 299721; -. [Q924Z6-2]
DR ProteomicsDB; 299722; -. [Q924Z6-3]
DR Antibodypedia; 26312; 65 antibodies from 19 providers.
DR DNASU; 74204; -.
DR Ensembl; ENSMUST00000009344; ENSMUSP00000009344; ENSMUSG00000000131. [Q924Z6-2]
DR Ensembl; ENSMUST00000168189; ENSMUSP00000130527; ENSMUSG00000000131. [Q924Z6-1]
DR GeneID; 74204; -.
DR KEGG; mmu:74204; -.
DR UCSC; uc009jqq.1; mouse. [Q924Z6-1]
DR UCSC; uc009jqr.1; mouse. [Q924Z6-2]
DR CTD; 23214; -.
DR MGI; MGI:2429950; Xpo6.
DR VEuPathDB; HostDB:ENSMUSG00000000131; -.
DR eggNOG; KOG2020; Eukaryota.
DR GeneTree; ENSGT00390000002810; -.
DR HOGENOM; CLU_004473_0_0_1; -.
DR InParanoid; Q924Z6; -.
DR OMA; DYQRRQW; -.
DR OrthoDB; 214523at2759; -.
DR PhylomeDB; Q924Z6; -.
DR TreeFam; TF323443; -.
DR BioGRID-ORCS; 74204; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Xpo6; mouse.
DR PRO; PR:Q924Z6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q924Z6; protein.
DR Bgee; ENSMUSG00000000131; Expressed in embryonic post-anal tail and 263 other tissues.
DR ExpressionAtlas; Q924Z6; baseline and differential.
DR Genevisible; Q924Z6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006611; P:protein export from nucleus; IMP: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 Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96QU8"
FT CHAIN 2..1125
FT /note="Exportin-6"
FT /id="PRO_0000235302"
FT DOMAIN 31..97
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96QU8"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..879
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018466"
FT VAR_SEQ 482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018467"
FT VAR_SEQ 880..928
FT /note="HEGSTGCRVVEKFLKILQVVVQEPGQVFKPFLPSIIALCMEQVYPIIAE ->
FT MAQGLLHGKWQKCGWDMSTGYCLAPLRLLWWPPPSCMEGRCSVVWISLQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018468"
FT CONFLICT 483
FT /note="Missing (in Ref. 2; AAH58090)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="A -> S (in Ref. 2; BAE32778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="S -> R (in Ref. 2; BAE32778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1125 AA; 128664 MW; CA808BDB172A84B9 CRC64;
MASEEASLRA LESLMTEFFH DCTTNERKRE IEELLNNFAQ QVGAWRFCLY FLSSTRNDYV
MMYSLTVFEN LINKMWLGVP SQDKMEIRSC LPKLLLAHHK TLPYFIRNKL CKVIVDIGRQ
DWPMFYHDFF TNILQLIQSP VTTPLGLIML KTTSEELACP REDLSVARKE ELRKLLLDQV
QTVLGLLTGI LETVWDKHSV TAATPPPSPT SGESGDLLSN LLQSPSSAKL LHQPIPILDV
ESEYVCSLAL ECLAHLFSWI PLSASITPSL LTTIFHFARF GCDTRARKMA SVNGSSQNCV
LGQERGRLGV LAMSCINELM SKNCVPMEFE EYLLRMFQQT FYLLQKITKD NNAHTVKSRL
EELDESYIEK FTDFLRLFVS VHLRRIESYS QFPVVEFLTL LFKYTFHQPT HEGYFSCLDI
WTLFLDYLTS KIKSRLGDKE AVLNRYEDAL VLLLTEVLNR IQFRYNQAQL EELDDETLDD
DQQTEWQRYL RQSLEVVAKV MELLPTHAFS TLFPVLQDNL EVYLGLQQFV VTSGSGHRLN
ITAENDCRRL HCSLRDLSSL LQAVGRLAEY FIGDVFAARF NDALTVVERL VKVTLYGSQI
KLYNIETAVP SVLKPDLIDV HAQSLAALQA YSHWLAQYCG EAHRQNTQQF VTLISTTMDA
ITPLISTKVQ DKLLLSACHL LVSLATTVRP VFLISIPAVQ KVFNSIIDAS AQRLTDKAQV
LVCRALSNTL LLPWPNLPES EQQWPLRSIN HASLISALSR DYHSLKPSAT APQRKVPLGD
TKVIIHQTLS VLEDIVENIS GESTKSRQIC YQSLQESVQV SLALFPAFIH QSDVTDEMLS
FFLTLFRGLR VQMGVPFTEQ IIQTFLNMFT REQLAESILH EGSTGCRVVE KFLKILQVVV
QEPGQVFKPF LPSIIALCME QVYPIIAERP SPDVKAELFE LLFRTLHHNW RYFFKSTVLA
SVQRGIAEEQ MENEPQFSAI MQAFGQSFLQ PDIHLFKQNL FYLETLNTKQ KLYHKKIFRT
TMLFQFVNVL LQVLVHKSHD LLQEEIGIAI YNMASVDFDG FFAAFLPEFL TSCDGVDANQ
KNVLGRNFKM DRDLPSFTQN VHRLVNDLRY YRLCNDSLPP GTVKL
