ILF2_RAT
ID ILF2_RAT Reviewed; 463 AA.
AC Q7TP98;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Interleukin enhancer-binding factor 2;
DE AltName: Full=Liver regeneration-related protein LRRG031;
GN Name=Ilf2; ORFNames=Ab1-143;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chromatin-interacting protein that forms a stable heterodimer
CC with interleukin enhancer-binding factor 3/ILF3 and plays a role in
CC several biological processes including transcription, innate immunity
CC or cell growth. Essential for the efficient reshuttling of ILF3
CC (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms
CC an RNA-binding complex that is required for mitotic progression and
CC cytokinesis by regulating the expression of a cluster of mitotic genes.
CC Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Plays
CC also a role in the inhibition of various viruses including Japanese
CC encephalitis virus or enterovirus 71. {ECO:0000250|UniProtKB:Q12905}.
CC -!- SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also
CC bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7
CC and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a
CC complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified
CC in a IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Interacts with IGF2BP1. Interacts with CRBN; this interaction
CC promotes ubiquitination and subsequent degradation of ILF2.
CC {ECO:0000250|UniProtKB:Q12905}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q12905}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12905}. Nucleus {ECO:0000250|UniProtKB:Q12905}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:Q12905}.
CC -!- PTM: Ubiquitinated at Lys-166 by CRBN with polyubiquitin chains by the
CC CUL4-RING E3 ligase (CRL4-CRBN) and then degraded by the proteasome.
CC {ECO:0000250|UniProtKB:Q12905}.
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DR EMBL; AY325142; AAP92543.1; -; mRNA.
DR RefSeq; NP_001041351.1; NM_001047886.1.
DR AlphaFoldDB; Q7TP98; -.
DR SMR; Q7TP98; -.
DR BioGRID; 259671; 5.
DR CORUM; Q7TP98; -.
DR IntAct; Q7TP98; 2.
DR MINT; Q7TP98; -.
DR STRING; 10116.ENSRNOP00000045539; -.
DR jPOST; Q7TP98; -.
DR PaxDb; Q7TP98; -.
DR PRIDE; Q7TP98; -.
DR GeneID; 310612; -.
DR KEGG; rno:310612; -.
DR UCSC; RGD:1305734; rat.
DR CTD; 3608; -.
DR RGD; 1305734; Ilf2.
DR eggNOG; KOG3793; Eukaryota.
DR HOGENOM; CLU_589956_0_0_1; -.
DR InParanoid; Q7TP98; -.
DR OrthoDB; 1145212at2759; -.
DR PhylomeDB; Q7TP98; -.
DR TreeFam; TF320194; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q7TP98; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q7TP98; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR043519; NT_sf.
DR Pfam; PF07528; DZF; 2.
DR SMART; SM00572; DZF; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51703; DZF; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..463
FT /note="Interleukin enhancer-binding factor 2"
FT /id="PRO_0000126066"
FT DOMAIN 108..444
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT REGION 424..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CXY6"
FT MOD_RES 94
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 145
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
SQ SEQUENCE 463 AA; 51381 MW; C33E6F88C9FC2195 CRC64;
MVSTHLTSTT LPDCYRSLIV NSELGSSALM DLNSPSFLYP LLHTPADKGT LCTYQAALGK
VYASLEVIGV GDDKLQAVHG LNGGKPHRDI LGSRITRPTG IKPLCLPRHI LAYDWLAQSL
LGIVIGSISL AYNELLMMEK LKGFRPFVPH IPFDFYLCEM AFPRVKPAPD ETSFSEALLK
RNQDLAPNSA EQQIEEVRQV GSYKKGTMTT GHNVADLVVI LKILPTFLTM LTNETGFEIS
SSDATVKILI TTVPPNLRKL DPELHLDIKV LQSALAAIRH ARWFEENASQ STVKVLIRLL
KDLRIRFPGF EPLTPWILDL LGHYAVMNNP TRQPLALNVA YRRCLQILAA GLFLPGSVGI
TDPCESGNFR VHTVMTLEQQ DMVCYTAQTL VRILSHGGFR KILGQEGDAS YLASEISTWD
GVIVTPSEKA YEKPPEKKEG EEEEENTEEP PQGEEEESME TQE
