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Q9JIL3 (ILF3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin enhancer-binding factor 3
Gene names
Name:Ilf3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length897 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA By similarity. Can regulate protein arginine N-methyltransferase 1 activity. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication By similarity.

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with FUS and SMN proteins and with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346 By similarity. Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2 By similarity.

Subcellular location

Nucleusnucleolus By similarity. Cytoplasm By similarity. Nucleus By similarity. Note: TThe unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.

Post-translational modification

Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication By similarity.

Methylated by protein arginine N-methyltransferase 1.

Sequence similarities

Contains 2 DRBM (double-stranded RNA-binding) domains.

Contains 1 DZF domain.

Ontologies

Keywords
   Biological processAntiviral defense
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of viral genome replication

Inferred from sequence or structural similarity. Source: UniProtKB

protein methylation

Inferred from direct assay Ref.1. Source: MGI

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction Ref.1. Source: RGD

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Prmt1Q630092EBI-78714,EBI-78708

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JIL3-1)

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: Q9JIL3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALYHHHFITRRRR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 897897Interleukin enhancer-binding factor 3
PRO_0000126072

Regions

Domain5 – 378374DZF
Domain398 – 46770DRBM 1
Domain524 – 59067DRBM 2
Region609 – 897289Interaction with PRMT1
Motif371 – 38919Bipartite nuclear localization signal Potential
Compositional bias385 – 3895Poly-Lys
Compositional bias634 – 6374Poly-Pro
Compositional bias640 – 65920Arg/Gly-rich
Compositional bias701 – 71010Poly-Gly
Compositional bias796 – 8005Poly-Gly

Amino acid modifications

Modified residue1001N6-acetyllysine By similarity
Modified residue1881Phosphothreonine; by PKR By similarity
Modified residue1901Phosphoserine By similarity
Modified residue3151Phosphothreonine; by PKR By similarity
Modified residue3821Phosphoserine By similarity
Modified residue3841Phosphoserine By similarity
Modified residue4601N6-acetyllysine By similarity
Modified residue4761Phosphoserine By similarity
Modified residue4821Phosphoserine By similarity
Modified residue6091Omega-N-methylated arginine By similarity
Modified residue7941Phosphoserine By similarity
Modified residue8141Phosphoserine By similarity

Natural variations

Alternative sequence11M → MALYHHHFITRRRR in isoform 2.
VSP_013409

Sequences

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

Last modified April 12, 2005. Version 2.
Checksum: ACD800D1858539BB

FASTA89795,935
        10         20         30         40         50         60 
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGNSELS 

        70         80         90        100        110        120 
EAENMDTPPD DESKEGAGEQ KAEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP 

       130        140        150        160        170        180 
TTALLDKVAD NLAIQLTTVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM 

       190        200        210        220        230        240 
EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV 

       250        260        270        280        290        300 
PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT 

       310        320        330        340        350        360 
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP 

       370        380        390        400        410        420 
PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP QAMNALMRLN QLKPGLQYKL 

       430        440        450        460        470        480 
ISQTGPVHAP IFTMSVEVDG STFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE 

       490        500        510        520        530        540 
DSAEESDGKP AVVAPPPVVE AVSNPSSVFP SDATTEQGPI LTKHGKNPVM ELNEKRRGLK 

       550        560        570        580        590        600 
YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DAPLALEANK 

       610        620        630        640        650        660 
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEAPPPPNIR GRGRGGNIRG RGRGRGFGGT 

       670        680        690        700        710        720 
NHGGGYMNAG AGYGSYGYSS NSATAGYSQF YSNGGHYGNA GGGGSGGGGG SSSYSSYYQG 

       730        740        750        760        770        780 
DSYNSPVPPK HAGKKPLHGG QQKPSYSSGY QSHQGQQQPY NQSQYSSYGT PQGKQKGYGH 

       790        800        810        820        830        840 
GQGSYSSYSN SYNSPGGGGG SDYSYDSKFN YSGSGGRSGG NSYGSSGSSY NTGSHGGYGA 

       850        860        870        880        890 
GSGGSSSYQG KQGGYSSQSN YSSPGSSQSY SGPASSYQSS QGGYSRNTEH SMNYQYR 

« Hide

Isoform 2 [UniParc].

Checksum: D6AB97A4B52E442A
Show »

FASTA91097,680

References

« Hide 'large scale' references
[1]"Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3."
Tang J., Kao P.N., Herschman H.R.
J. Biol. Chem. 275:19866-19876(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF220102 mRNA. Translation: AAF31446.1.
AABR03063190 Genomic DNA. No translation available.
AABR03065470 Genomic DNA. No translation available.
RefSeqNP_445864.1. NM_053412.1.
UniGeneRn.203881.

3D structure databases

ProteinModelPortalQ9JIL3.
SMRQ9JIL3. Positions 403-470, 525-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249972. 1 interaction.
IntActQ9JIL3. 1 interaction.
STRING10116.ENSRNOP00000062871.

PTM databases

PhosphoSiteQ9JIL3.

Proteomic databases

PaxDbQ9JIL3.
PRIDEQ9JIL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID84472.
KEGGrno:84472.
UCSCRGD:619734. rat. [Q9JIL3-1]

Organism-specific databases

CTD3609.
RGD619734. Ilf3.

Phylogenomic databases

eggNOGNOG307678.
HOGENOMHOG000232164.
HOVERGENHBG069915.
InParanoidQ9JIL3.
KOK13090.
PhylomeDBQ9JIL3.

Gene expression databases

GenevestigatorQ9JIL3.

Family and domain databases

Gene3D3.30.160.20. 2 hits.
InterProIPR014720. dsRNA-bd_dom.
IPR006561. DZF.
[Graphical view]
PfamPF00035. dsrm. 2 hits.
PF07528. DZF. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 2 hits.
SM00572. DZF. 1 hit.
[Graphical view]
PROSITEPS50137. DS_RBD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio616960.
PROQ9JIL3.

Entry information

Entry nameILF3_RAT
AccessionPrimary (citable) accession number: Q9JIL3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: April 12, 2005
Last modified: April 16, 2014
This is version 101 of the entry and version 2 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