NFIL3_BOVIN
ID NFIL3_BOVIN Reviewed; 462 AA.
AC Q08D88;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein;
GN Name=NFIL3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily. {ECO:0000305}.
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DR EMBL; BC123885; AAI23886.1; -; mRNA.
DR RefSeq; NP_001068708.1; NM_001075240.1.
DR RefSeq; XP_005210477.1; XM_005210420.2.
DR RefSeq; XP_015328138.1; XM_015472652.1.
DR AlphaFoldDB; Q08D88; -.
DR SMR; Q08D88; -.
DR STRING; 9913.ENSBTAP00000023618; -.
DR PaxDb; Q08D88; -.
DR PRIDE; Q08D88; -.
DR GeneID; 506097; -.
DR KEGG; bta:506097; -.
DR CTD; 4783; -.
DR eggNOG; KOG3119; Eukaryota.
DR HOGENOM; CLU_052045_0_0_1; -.
DR InParanoid; Q08D88; -.
DR OrthoDB; 1450431at2759; -.
DR TreeFam; TF328374; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001779; P:natural killer cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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_0000292666"
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 189..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
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 394
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"
SQ SEQUENCE 462 AA; 51436 MW; 3509D4F8CEC52079 CRC64;
MQLRKMQSIK KEQASLDAGT NVDKMMVLNS ALTEVSEDLT TGEELLLNEG SVGKNKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ DYQTSKSTVS AFVDEHEPSM VASSCISVIK
HSPQSSLSDV SEVSSLEHSQ EGPVQNGCRS PESKFQVIKQ EPMELESYAR EPRDDRGAYR
GAVYQNYMGN SFPGYSHSPP LLQVNRSSSN SPRTSETDEG AVGKSSDGED EQQVPKGPIH
SPVELQRVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDHEFDGTQK LSSPVDMTSK
RHFELEKHTT PNLVHSSLTP FSVQVTNIQD WSLKSEHWHQ KELNGKTQSS FKTGVVEVKD
SGYKVSDPEN LFLKQGIANL SAEVVSLKRL IATHQISASD SG
