NFIL3_RAT
ID NFIL3_RAT Reviewed; 462 AA.
AC Q6IMZ0; Q923M2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein;
DE AltName: Full=E4 promoter-binding protein 4;
GN Name=Nfil3;
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 [MRNA], AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11262393; DOI=10.1074/jbc.m010332200;
RA Nishimura Y., Tanaka T.;
RT "Calcium-dependent activation of nuclear factor regulated by interleukin
RT 3/adenovirus E4 promoter-binding protein gene expression by
RT calcineurin/nuclear factor of activated T cells and calcium/calmodulin-
RT dependent protein kinase signaling.";
RL J. Biol. Chem. 276:19921-19928(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as a transcriptional regulator that recognizes and binds
CC to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many
CC cellular and viral promoters. Represses transcription from promoters
CC with activating transcription factor (ATF) sites. Represses promoter
CC activity in osteoblasts. Represses transcriptional activity of PER1.
CC Represses transcriptional activity of PER2 via the B-site on the
CC promoter. Activates transcription from the interleukin-3 promoter in T-
CC cells. Competes for the same consensus-binding site with PAR DNA-
CC binding factors (DBP, HLF and TEF). Component of the circadian clock
CC that acts as a negative regulator for the circadian expression of PER2
CC oscillation in the cell-autonomous core clock. Protects pro-B cells
CC from programmed cell death (By similarity). Represses the transcription
CC of CYP2A5 (By similarity). Positively regulates the expression and
CC activity of CES2 by antagonizing the repressive action of NR1D1 on CES2
CC (By similarity). Required for the development of natural killer cell
CC precursors (By similarity). {ECO:0000250|UniProtKB:O08750,
CC ECO:0000250|UniProtKB:Q16649}.
CC -!- SUBUNIT: Homodimer (By similarity). Binds DNA as a dimer (By
CC similarity). Interacts with CRY2, DR1 and PER2 (By similarity).
CC Interacts with NR0B2 (By similarity). Interacts with MYSM1 (By
CC similarity). {ECO:0000250|UniProtKB:O08750,
CC ECO:0000250|UniProtKB:Q16649}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- INDUCTION: Up-regulated by dexamethasone and thapsigargin.
CC {ECO:0000269|PubMed:11262393}.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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DR EMBL; AY004663; AAF86615.1; -; mRNA.
DR EMBL; BC072527; AAH72527.1; -; mRNA.
DR RefSeq; NP_446179.2; NM_053727.2.
DR RefSeq; XP_006253729.1; XM_006253667.3.
DR RefSeq; XP_006253731.1; XM_006253669.2.
DR RefSeq; XP_006253732.1; XM_006253670.3.
DR AlphaFoldDB; Q6IMZ0; -.
DR SMR; Q6IMZ0; -.
DR STRING; 10116.ENSRNOP00000015525; -.
DR iPTMnet; Q6IMZ0; -.
DR PhosphoSitePlus; Q6IMZ0; -.
DR PaxDb; Q6IMZ0; -.
DR PRIDE; Q6IMZ0; -.
DR Ensembl; ENSRNOT00000015525; ENSRNOP00000015525; ENSRNOG00000011668.
DR Ensembl; ENSRNOT00000096237; ENSRNOP00000093138; ENSRNOG00000011668.
DR Ensembl; ENSRNOT00000096697; ENSRNOP00000090522; ENSRNOG00000011668.
DR Ensembl; ENSRNOT00000112357; ENSRNOP00000089110; ENSRNOG00000011668.
DR GeneID; 114519; -.
DR KEGG; rno:114519; -.
DR CTD; 4783; -.
DR RGD; 620972; Nfil3.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000160540; -.
DR HOGENOM; CLU_052045_0_0_1; -.
DR InParanoid; Q6IMZ0; -.
DR OMA; KNVHATV; -.
DR OrthoDB; 1450431at2759; -.
DR PhylomeDB; Q6IMZ0; -.
DR TreeFam; TF328374; -.
DR PRO; PR:Q6IMZ0; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000011668; Expressed in liver and 18 other tissues.
DR Genevisible; Q6IMZ0; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Activator; Biological rhythms; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..462
FT /note="Nuclear factor interleukin-3-regulated protein"
FT /id="PRO_0000292669"
FT DOMAIN 73..136
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 314
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CROSSLNK 448
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16649"
FT CONFLICT 45
FT /note="L -> P (in Ref. 1; AAF86615)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="S -> P (in Ref. 1; AAF86615)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="N -> S (in Ref. 1; AAF86615)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> V (in Ref. 1; AAF86615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50781 MW; 1D7365C2F4B017EF CRC64;
MQLRKMQAIK KEPASLDPTG SSDKMLLLNS ALAEVAEDLA SGEDLLLNEG SMGKNKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS STVYAQEIQK LSNSTAVYFQ DYQTSKAAVS SYVDEHEPAM VAGSCISVIK
HSPQSSLSDV SEVSSVEHTQ ESPAQGGCRS PENKFPVIKQ EPVELESFAR ESREERGAYS
ASIYQSYMGS SFSTYSHSPP LLQVHGSTSN SPRTSEADEG VVGKSSDGED EQQVPKGPIH
SPVELQRVHA TVVKVPEVNP SALPHKLRIK AKAMQVKVEA LDSEFEGMQK LSSPADALAK
RHFDLEKHGA SGTAHSSLPP FSVQVTNIQD WSLRSEHWHH KELGGKTQGT FKTGVVEVKD
SGYKVSEAEN LYLKQGVANL SAEVVSLKRF IATQPISASD SR
