ILF3_DANRE
ID ILF3_DANRE Reviewed; 833 AA.
AC Q6NXA4; Q802W3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Interleukin enhancer-binding factor 3 homolog;
GN Name=ilf3; ORFNames=zgc:77030;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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. {ECO:0000250|UniProtKB:Q12906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q12906}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12906}. Nucleus {ECO:0000250|UniProtKB:Q12906}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47175.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC047175; AAH47175.1; ALT_SEQ; mRNA.
DR EMBL; BC067172; AAH67172.1; -; mRNA.
DR RefSeq; NP_997764.1; NM_212599.1.
DR AlphaFoldDB; Q6NXA4; -.
DR SMR; Q6NXA4; -.
DR STRING; 7955.ENSDARP00000019087; -.
DR iPTMnet; Q6NXA4; -.
DR PaxDb; Q6NXA4; -.
DR GeneID; 321868; -.
DR KEGG; dre:321868; -.
DR CTD; 321868; -.
DR ZFIN; ZDB-GENE-030131-587; ilf3b.
DR eggNOG; KOG3792; Eukaryota.
DR InParanoid; Q6NXA4; -.
DR OrthoDB; 612611at2759; -.
DR PhylomeDB; Q6NXA4; -.
DR PRO; PR:Q6NXA4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.460.10; -; 1.
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 Antiviral defense; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..833
FT /note="Interleukin enhancer-binding factor 3 homolog"
FT /id="PRO_0000126073"
FT DOMAIN 11..379
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT DOMAIN 402..471
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 527..593
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 218
FT /note="F -> Y (in Ref. 1; AAH47175)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="G -> V (in Ref. 1; AAH47175)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="T -> A (in Ref. 1; AAH67172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 90436 MW; 4E4F44B7DC839347 CRC64;
MPPPLRHRSM RIFVNDDRHV MAKHSAIYPT QEELEGVQNM VSHTERALKL VSDWLDDQEK
GNAKVNALDT DGEGDKETEP STGEQATRSL RGVMRVGLVA KGLLLKGDLD LELVLLCKEK
PTITLLKKVS DNLAVQLKQL VTEEKYDVKP CIRDATIVIK NAKEPPLTLT IHLTSPLVRE
EVEKQAAGET LSVIDPPDVL DRQKCLTALA SLRHAKWFQA RANGLRSCVI VIRILRDLCA
RVPTWSPLRG WPLELLCEKA IGTGNRPMGA GEALRRVLEC LASGILMADG SGICDPCEKE
LTDAISHVDR QQREDITQSA QHALRLSAFG QLHKVLGMDP LPSKMPRKPR SDTPIDYTVQ
IPPSTTYVPP MKRPIEEEST DEKNPNKKKK KLQKKSPDEK AEPAQAMNAL MRLNQLKPGL
QYKLISQTGP VHVPVFTMSV EVDGKNFEAS GPSKRTAKLH VAVKVLQDMG LPTGMDQKTT
ELMKVDEPVS TQETLPPVIK MEPEPVPITE TPTDENARQQ GPILTKHGKN PVMELNEKRR
GLKYELISET GGSHDKRFVM EVEIDGQKFQ GTGSNKKVAK AYAALAALEK LFPEGSNSEV
NKKKKMPPMH TGFGMVSGPP SDMMPNPRGR GRGRGRGRGR GFNNGGGFNQ GGYGTYGYGG
NNSGYNFYNN GGSNGGSVAS NQGTNQSSGG AAATGGFGSY YQSDSSYTSP APTPKPVGKK
PPMHQNTKPQ APGVGQGGSY GQYNQGYGQK KNFGQTQGGG GAAAGGGGNF NYSTAYPSQV
TGGQEYNYEG YSNQSNYNSQ GGANQNFGGN SAPYNSGQAG YGRGDPNMNY QYR
