ILF3B_XENLA
ID ILF3B_XENLA Reviewed; 898 AA.
AC Q6DD04; Q91551;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Interleukin enhancer-binding factor 3-B;
DE AltName: Full=Double-stranded RNA-binding protein 4F.2 {ECO:0000303|PubMed:7922339};
DE Short=DsRNA-binding protein 4F.2 {ECO:0000312|EMBL:AAA19961.1};
GN Name=ilf3-b; Synonyms=ubp4 {ECO:0000303|PubMed:8631310};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAH77828.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH77828.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAA19961.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-898 (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000312|EMBL:AAA19961.1};
RX PubMed=7922339; DOI=10.1016/s0960-9822(00)00069-5;
RA Bass B.L., Hurst S.R., Singer J.D.;
RT "Binding properties of newly identified Xenopus proteins containing dsRNA-
RT binding motifs.";
RL Curr. Biol. 4:301-314(1994).
RN [3] {ECO:0000305}
RP IDENTIFICATION OF THE MRNA IN A RIBONUCLEOPROTEIN COMPLEX.
RX PubMed=8631310; DOI=10.1002/j.1460-2075.1996.tb00424.x;
RA Wormington M., Searfoss A.M., Hurney C.A.;
RT "Overexpression of poly(A) binding protein prevents maturation-specific
RT deadenylation and translational inactivation in Xenopus oocytes.";
RL EMBO J. 15:900-909(1996).
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 ECO:0000269|PubMed:8631310}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7922339}. 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 ECO:0000269|PubMed:7922339}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:7922339};
CC IsoId=Q6DD04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DD04-2; Sequence=VSP_053196, VSP_053197;
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in the oocyte (at protein
CC level). {ECO:0000269|PubMed:7922339}.
CC -!- PTM: Phosphorylated. Phosphorylation affects nuclear translocation (By
CC similarity). {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; BC077828; AAH77828.1; -; mRNA.
DR EMBL; U07156; AAA19961.1; -; mRNA.
DR PIR; I51653; I51653.
DR RefSeq; NP_001180330.1; NM_001193401.1. [Q6DD04-2]
DR AlphaFoldDB; Q6DD04; -.
DR SMR; Q6DD04; -.
DR DNASU; 398578; -.
DR GeneID; 398578; -.
DR KEGG; xla:398578; -.
DR CTD; 398578; -.
DR Xenbase; XB-GENE-6256032; ilf3.L.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398578; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA: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: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 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; Developmental protein;
KW DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..898
FT /note="Interleukin enhancer-binding factor 3-B"
FT /id="PRO_0000391690"
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 521..587
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 52..87
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 468..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..799
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 485..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 684..698
FT /note="QFYSNGGASGNAGGG -> DFFTDCYGYHDFASA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053196"
FT VAR_SEQ 699..898
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053197"
FT CONFLICT 137
FT /note="E -> K (in Ref. 2; AAA19961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 98702 MW; A4F256881111EFDC CRC64;
MRPMRIFLND DRHVMAKHSV VYPTQEELEA VQNMVSHTER ALKAVSDWID QQEKDSGIEQ
ENPEPEETET TEEGKDSEAK TGENPTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCRDKP
TISLLKRVAD NLVLQFETVS EDKYEVVQNI REASIVIKNT KEPPLTLHIR LTSPLVREEV
EKLSAGETLT VSDPPDVLDR HKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
PTWEPLRGWP LELLCEKAIG TANRPMGAGE ALRRVLECLS SGILMPDGPG LYDPCEKDAS
DALEHLERQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP TKMPKKTKIE IPIIDYTVQI
PPSTTYAMPA LKRPIEEDGE DKSPSKKKKK IQKKDEKSEP PQAMNALMRL NQLKPGLQYK
LISQTGPVHA PIFTMSVEVD DKTFEASGPS KKTAKLHVAV KVLQDMGLPT GIDEKEESVD
ESEEKPVLQT PSQTADSEQA DSSAGDQSES GKQQGPILTR HGKNPVMELN EKRRGLKYEL
ISETGGSHDK RFIMEVEVDG VKFQGNGSNK KVAKAYAALS ALEKLFPDYT TYTEAPKKKR
PPMMPRGGPK FAGKHNQGFG MMYNEVPPPQ VMRGRGRGGM NRGRGRGRGG FGGGNYGGYM
NSGGYGGGYG GNNYQTSATA GYSQFYSNGG ASGNAGGGGA GSGGYSSYYQ GEGYNAPTPP
KPFVKKPPPP QQQQQPPPQH ASNPPKPSYN QGYQGHQGGQ QQQQPQQQQQ QTYNQNQYSN
YGPPQKQKGG YNQGTQGAAS AGSYNYSNSY TGGTACRVRQ WRGCRRARRP ALTQRQALVT
TQGRTPAMVQ PAVPHRTKVT HSRTTIKVPP DRTTAALQII TSPLREEQEV MAGIQITT
