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Q924C1 (XPO5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-5

Short name=Exp5
Alternative name(s):
Ran-binding protein 21
Gene names
Name:Xpo5
Synonyms:Kiaa1291, Ranbp21
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi) By similarity. Mediates nuclear export of ADAR/ADAR1 in a RanGTP-dependent manner By similarity.

Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP By similarity.

Subunit structure

Component of a nuclear export receptor complex composed of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, Ran and pre-miRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-dependent manner By similarity. Interacts with ADAR/ADAR1 (via DRBM domains) By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Shuttles between the nucleus and the cytoplasm By similarity.

Sequence similarities

Belongs to the exportin family.

Ontologies

Keywords
   Biological processProtein transport
RNA-mediated gene silencing
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
tRNA-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene silencing by RNA

Inferred from electronic annotation. Source: UniProtKB-KW

protein export from nucleus

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein transporter activity

Inferred from direct assay Ref.1. Source: MGI

tRNA binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q924C1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q924C1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-720: Missing.
     925-925: M → MPLSTPALVLSPQ
Isoform 3 (identifier: Q924C1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: K → V
     209-1204: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12041203Exportin-5
PRO_0000235300

Regions

Region2 – 108107Necessary for interaction with Ran By similarity
Region533 – 640108Necessary for interaction with ILF3 By similarity

Amino acid modifications

Modified residue3961N6-acetyllysine By similarity

Natural variations

Alternative sequence2 – 720719Missing in isoform 2.
VSP_018462
Alternative sequence2081K → V in isoform 3.
VSP_018463
Alternative sequence209 – 1204996Missing in isoform 3.
VSP_018464
Alternative sequence9251M → MPLSTPALVLSPQ in isoform 2.
VSP_018465

Experimental info

Sequence conflict481V → I in AAH55455. Ref.3
Sequence conflict1431F → S in AAH55455. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 23B3C27B68F71846

FASTA1,204136,973
        10         20         30         40         50         60 
MEMEQVNALC EELVKAVTVM MDPSSTQRYR LEALKFCEEF KEKCPICVPC GLKLAEKTQI 

        70         80         90        100        110        120 
AIVRHFGLQI LEHVVKFRWN SMSRLEKVYL KNSVMELIAN GTLRILEEEN HIKDVLSRIV 

       130        140        150        160        170        180 
VEMIKREWPQ HWPDMLMELD TLFRQGETQR ELVMFILLRL AEDVVTFQTL PTQRRRDIQQ 

       190        200        210        220        230        240 
TLTQNMERIL NFLLNTLQEN VNKYQQMKTD SSQEAEAQAN CRVSVAALNT LAGYIDWVSL 

       250        260        270        280        290        300 
NHITAENCKL VETLCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKRLMIL FGDVAMHYIL 

       310        320        330        340        350        360 
SAAQTADGGG LVEKHYLFLK RLCQVLCALG NLLCALLALD ANIQTPINFG MYLESFLAFT 

       370        380        390        400        410        420 
THPSQFLRSS THMTWGALFR HEVLSRDPAL LAVIPKYLRA SMTNLVKMGF PSKTDSPSCE 

       430        440        450        460        470        480 
YSRFDFDSDE DFNAFFNSSR AQHGEVVRCV CRLDPKTSFQ MAAEWLKYQL SASIDTGPVN 

       490        500        510        520        530        540 
SCSTAGTGEG GFCSIFSPSY VQWEAMTFFL ESVINQMFRT LDKEELPVSD GIELLQLVLN 

       550        560        570        580        590        600 
FEIKDPLVLS CVLTNVSALF PFVTYKPAFL PQVFSKLFSF VTFESVGESK APRTRAVRNV 

       610        620        630        640        650        660 
RRHACSSINK MCRDYPDLVL PNFDMLYSHV KQLLSNELLL TQMEKCALME ALVLVSNQFK 

       670        680        690        700        710        720 
DYERQKLFLE ELMAPVVNIW LSEEMCRALS DIDSFIAYVG ADLKSCDPAV EDPCGLNRAR 

       730        740        750        760        770        780 
MSFCVYSILG VMRRTSWPSD LEEAKAGGFV VGYTPSGNPI FRNPCTEQIL RLLDNLLALV 

       790        800        810        820        830        840 
RTHNTLYTPE MLTKMAEPFT KALDIVESEK TAILGLPQPL LEFNDHPVYR TTLERMQRFF 

       850        860        870        880        890        900 
GILYENCYHI LGKAGPSMQQ DFYTVEDLAS QLLGSAFVNL NNIPDFRLRS MLRVFVKPLV 

       910        920        930        940        950        960 
LFCPSEHYET LISPILGPLF TYLHMRLSQK WHVINQRSIL CGEDEIAEDN PESQEMLEEQ 

       970        980        990       1000       1010       1020 
LVRMLTREAM DLIMACCVSK KTADHTAAPT ADGDDEEMMA TEVAPSSVVE LTDLGKCLMK 

      1030       1040       1050       1060       1070       1080 
HEDVCTALLI TAFNSLTWKD TLSCQRATTQ LCWPLLKQVM SGTLLADAVT WLFTSVLKGL 

      1090       1100       1110       1120       1130       1140 
QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE INKESLDQFD CKLLNPSLQK 

      1150       1160       1170       1180       1190       1200 
AADKRRKDHF KRLIAGCIGK PLGEQFRKEV HIKNLPWLFK KPKPMLETEV LDSEEGGLAT 


IFEP 

« Hide

Isoform 2 [UniParc].

Checksum: F33B026ABE3C32EA
Show »

FASTA49756,259
Isoform 3 [UniParc].

Checksum: 7C32C64C229DA26C
Show »

FASTA20824,728

References

« Hide 'large scale' references
[1]"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: FVB/N.
Tissue: Mammary gland.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-521 AND 959-1204.
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF343581 mRNA. Translation: AAK68050.1.
AK122486 mRNA. Translation: BAC65768.1.
BC055455 mRNA. Translation: AAH55455.1.
BC131661 mRNA. Translation: AAI31662.1.
AK010389 mRNA. Translation: BAB26904.1.
AK011190 mRNA. Translation: BAB27455.1.
RefSeqNP_082474.1. NM_028198.2.
UniGeneMm.275039.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215307. 1 interaction.

PTM databases

PhosphoSiteQ924C1.

Proteomic databases

PaxDbQ924C1.
PRIDEQ924C1.

Protocols and materials databases

DNASU72322.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087031; ENSMUSP00000084257; ENSMUSG00000067150. [Q924C1-1]
GeneID72322.
KEGGmmu:72322.
UCSCuc008crz.1. mouse. [Q924C1-3]
uc008csa.1. mouse. [Q924C1-1]
uc012aun.1. mouse. [Q924C1-2]

Organism-specific databases

CTD57510.
MGIMGI:1913789. Xpo5.
RougeSearch...

Phylogenomic databases

eggNOGNOG296759.
GeneTreeENSGT00390000013979.
HOGENOMHOG000236267.
HOVERGENHBG056281.
InParanoidA2RRJ5.
KOK14289.
OMALISNHFC.
OrthoDBEOG7MWGW1.
PhylomeDBQ924C1.
TreeFamTF323382.

Gene expression databases

BgeeQ924C1.
CleanExMM_XPO5.
GenevestigatorQ924C1.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08389. Xpo1. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSXPO5. mouse.
NextBio336012.
PMAP-CutDBQ924C1.
PROQ924C1.
SOURCESearch...

Entry information

Entry nameXPO5_MOUSE
AccessionPrimary (citable) accession number: Q924C1
Secondary accession number(s): A2RRJ5 expand/collapse secondary AC list , Q7TMP2, Q80TF9, Q9CRI9, Q9CT48
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot