NFIL3_CHICK
ID NFIL3_CHICK Reviewed; 458 AA.
AC Q90Z72;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein;
DE AltName: Full=E4 promoter-binding protein 4;
DE Short=cE4BP4 protein;
DE AltName: Full=bZIP protein E4BP4;
GN Name=NFIL3; Synonyms=E4BP4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX PubMed=11427718; DOI=10.1073/pnas.141090998;
RA Doi M., Nakajima Y., Okano T., Fukada Y.;
RT "Light-induced phase-delay of the chicken pineal circadian clock is
RT associated with the induction of cE4bp4, a potential transcriptional
RT repressor of cPer2 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8089-8094(2001).
RN [2]
RP FUNCTION, INTERACTION WITH CSNK1E, PHOSPHORYLATION AT SER-182, MUTAGENESIS
RP OF SER-182; SER-298 AND SER-349, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15182670; DOI=10.1016/j.cub.2004.05.043;
RA Doi M., Okano T., Yujnovsky I., Sassone-Corsi P., Fukada Y.;
RT "Negative control of circadian clock regulator E4BP4 by casein kinase
RT Iepsilon-mediated phosphorylation.";
RL Curr. Biol. 14:975-980(2004).
CC -!- FUNCTION: Acts as a transcriptional regulator (By similarity).
CC Represses PER2 transcription through a recognition sequence in the
CC promoter (PubMed:11427718, PubMed:15182670). Component of the circadian
CC clock that may contribute to the rhythmic expression of PER2 gene in a
CC light-dependent and time-of-day-dependent manner (PubMed:11427718,
CC PubMed:15182670). {ECO:0000250|UniProtKB:O08750,
CC ECO:0000269|PubMed:11427718, ECO:0000269|PubMed:15182670}.
CC -!- SUBUNIT: Homodimer (By similarity). Binds DNA as a dimer (By
CC similarity). {ECO:0000250|UniProtKB:Q16649}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15182670}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15182670}.
CC -!- INDUCTION: Expression is regulated by light and circadian rhythms in
CC the pineal gland (at protein level). {ECO:0000269|PubMed:11427718,
CC ECO:0000269|PubMed:15182670}.
CC -!- PTM: Phosphorylated. Phosphorylated on Ser-182. Phosphorylation may
CC require prime phosphorylation(s). Phosphorylation takes place at
CC specific times of the day. Phosphorylation leads to its down-regulation
CC through proteasome-dependent degradation.
CC {ECO:0000269|PubMed:15182670}.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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DR EMBL; AF335427; AAK72227.1; -; mRNA.
DR RefSeq; NP_989949.1; NM_204618.2.
DR RefSeq; XP_015135721.1; XM_015280235.1.
DR AlphaFoldDB; Q90Z72; -.
DR SMR; Q90Z72; -.
DR STRING; 9031.ENSGALP00000024495; -.
DR iPTMnet; Q90Z72; -.
DR PaxDb; Q90Z72; -.
DR PRIDE; Q90Z72; -.
DR GeneID; 395326; -.
DR KEGG; gga:395326; -.
DR CTD; 4783; -.
DR VEuPathDB; HostDB:geneid_395326; -.
DR eggNOG; KOG3119; Eukaryota.
DR InParanoid; Q90Z72; -.
DR OrthoDB; 1450431at2759; -.
DR PhylomeDB; Q90Z72; -.
DR PRO; PR:Q90Z72; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016743; NFIL3/E4BP4.
DR InterPro; IPR010533; Vert_IL3-reg_TF.
DR PANTHER; PTHR15284:SF1; PTHR15284:SF1; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR Pfam; PF06529; Vert_IL3-reg_TF; 1.
DR PIRSF; PIRSF019029; bZIP_E4BP4; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..458
FT /note="Nuclear factor interleukin-3-regulated protein"
FT /id="PRO_0000292670"
FT DOMAIN 73..136
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..95
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 99..106
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine; by CSNK1E"
FT /evidence="ECO:0000269|PubMed:15182670"
FT MUTAGEN 182
FT /note="S->A: Induces a strong decrease in its
FT electrophoretic retardation."
FT /evidence="ECO:0000269|PubMed:15182670"
FT MUTAGEN 298
FT /note="S->A: Does not induce a strong decrease in its
FT electrophoretic retardation."
FT /evidence="ECO:0000269|PubMed:15182670"
FT MUTAGEN 349
FT /note="S->A: Does not induce a strong decrease in its
FT electrophoretic retardation."
FT /evidence="ECO:0000269|PubMed:15182670"
SQ SEQUENCE 458 AA; 51351 MW; CDAC9416BB5A2621 CRC64;
MQLRKMQTLK KEHGSVDTSS NVDKIMVLKS TLAEVSEELS TNEDILLTEA SSGKSKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS SASYAQEIQK LSSSTTVYFQ DYQSSKPNIN SFVDEHEPSV VGSSCISVIK
HSPQSSMSDM SEMPSVEHTQ GSRIQSNCRS PENKFQIIKQ EPIELEREPR DDRGSYKASI
YPNYMGTTFN MYSHSPPLLQ VNRSSSNSPR TSETDDGVVG KSSDGEDEQQ VPKGPIHSPV
EHKNVHATVK VPEVNSSALP HKLRIKAKAM QVKVEAMDND YDATQKLSSP IDMSSKRHFE
LEKHGAQNLV HSSHTPFSVQ VTNIQDWSLK PELWHQKELN VKIQNGCKTG VVEIKDNVYN
VSESENLYLK QGIANLSAEV ASLKRLITTQ QISASDSG
