ILF3_XENTR
ID ILF3_XENTR Reviewed; 698 AA.
AC Q6GL57;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Interleukin enhancer-binding factor 3 {ECO:0000312|EMBL:AAH74653.1};
GN Name=ilf3 {ECO:0000312|EMBL:AAH74653.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH74653.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH74653.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that plays an essential role in the
CC biogenesis of circular RNAs (circRNAs) which are produced by back-
CC splicing circularization of pre-mRNAs. Within the nucleus, promotes
CC circRNAs processing by stabilizing the regulatory elements residing in
CC the flanking introns of the circularized exons. Plays thereby a role in
CC the back-splicing of a subset of circRNAs. As a consequence,
CC participates in a wide range of transcriptional and post-
CC transcriptional processes. Binds to poly-U elements and AU-rich
CC elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon
CC viral infection, ILF3 accumulates in the cytoplasm and participates in
CC the innate antiviral response. Mechanistically, ILF3 becomes
CC phosphorylated and activated by the double-stranded RNA-activated
CC protein kinase/PKR which releases ILF3 from cellular mature circRNAs.
CC In turn, unbound ILF3 molecules are able to interact with and thus
CC inhibit viral mRNAs. Has a cytoplasmic role early in development as
CC part of a ribonucleoprotein (mRNP) complex which may regulate mRNA
CC transport and/or translation. Following nuclear localization at the
CC mid-blastula transition, acts as a transcription factor and binds the
CC 5'-CCAAT-3' promoter sequence to regulate transcription of the gata2
CC gene as a subunit of the CCAAT box transcription factor (CBTF). Its
CC role as an mRNP component negatively regulates its activity as a
CC transcription factor by precluding its nuclear localization.
CC {ECO:0000250|UniProtKB:Q12906, ECO:0000250|UniProtKB:Q91550}.
CC -!- SUBUNIT: A component of a ybx2/frgy2-containing mRNA-ribonucleoprotein
CC (mRNP) complex. Also a component of the CCAAT box transcription factor
CC (CBTF) complex. {ECO:0000250|UniProtKB:Q91550}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91550}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91550}. Note=Cytoplasmic in fertilized eggs,
CC then translocates to the nucleus prior to gastrulation. RNA-binding is
CC required for cytoplasmic retention during early development, and
CC nuclear translocation at the mid-blastula transition (MBT) is probably
CC coupled to the degradation of maternal mRNA that occurs at that stage
CC (By similarity). {ECO:0000250|UniProtKB:Q91550}.
CC -!- PTM: Phosphorylated. Phosphorylation affects nuclear translocation.
CC {ECO:0000250|UniProtKB:Q91550}.
CC -!- PTM: Methylated by protein arginine N-methyltransferase 1 (prmt1b) in
CC the RGG-rich domain. Methylation decreases DNA-binding and thereby
CC decreases transcription of the gata2 gene, but does not regulate dsRNA
CC binding or subcellular localization. {ECO:0000250|UniProtKB:Q91550}.
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; BC074653; AAH74653.1; -; mRNA.
DR RefSeq; NP_001005648.1; NM_001005648.1.
DR AlphaFoldDB; Q6GL57; -.
DR SMR; Q6GL57; -.
DR STRING; 8364.ENSXETP00000026522; -.
DR Ensembl; ENSXETT00000049660; ENSXETP00000049660; ENSXETG00000011651.
DR GeneID; 448121; -.
DR KEGG; xtr:448121; -.
DR CTD; 3609; -.
DR Xenbase; XB-GENE-494367; ilf3.
DR InParanoid; Q6GL57; -.
DR OrthoDB; 612611at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011651; Expressed in gastrula and 25 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 2.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR033099; ILF3/NF90.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR45762:SF4; PTHR45762:SF4; 3.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51703; DZF; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; Developmental protein; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..698
FT /note="Interleukin enhancer-binding factor 3"
FT /id="PRO_0000391691"
FT DOMAIN 5..379
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT DOMAIN 399..468
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 520..586
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..390
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 374..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 77078 MW; 470617B45A1E1E5A CRC64;
MRPMRIFLND DRHVMAKHSV VYPTQEELEA VQNMVSHTER ALKAVSDWID QQEKDCSGEQ
EQPEPEEPET TEEGKDSEGK TGENPTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCRDKP
TISLLKRVAD NLVLQFETVS EDKYEVIQNI REASIVIKNT KEPPLTLNIR LTSPLVREEM
EKLSAGETLT VSDPPDVLDR HKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
PTWEPLRGWP LELLCEKAIG TANRPMGAGE ALRRVLECLS SGILMPDGPG LYDPCEKEAS
DALEHLERQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP TKIPKKTKVE TPTIDYTVQI
PPSTTYAMPA LKRPMEEDGE DKSPSKKKKK IQKKDEKSEP PQAMNALMRL NQLKPGLQYK
LISQTGPVHA PIFTMSVEVD EKTFEASGPS KKTAKLHVAV KVLQDMGLPT GMEEKEEATD
ESEQKPVVQT PAQPADSTQT DSAADQAESA KQQGPILTKH GKNPVMELNE KRRGLKYELI
SETGGSHDKR FVMEVEVDGV KFQGSGSNKK VAKAYAALAA LEKLFPDYTT YAEAPKKKRP
PMMPRGGPKF AGKHNQGFGM MYNEVPPPQA MRGRGRGGMN RGRGRGRGGF GGGNHGGYMN
SGGYGGGYGG NYNYQTSATA GYSDFFTDCY GYHDFASA
