ID A0A384B1B6_BALAS Unreviewed; 462 AA.
AC A0A384B1B6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Nuclear factor interleukin-3-regulated protein {ECO:0000256|ARBA:ARBA00018259, ECO:0000256|PIRNR:PIRNR019029};
GN Name=NFIL3 {ECO:0000313|RefSeq:XP_007193486.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007193486.1};
RN [1] {ECO:0000313|RefSeq:XP_007193486.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007193486.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR019029}.
CC -!- SUBUNIT: Homodimer. Binds DNA as a dimer.
CC {ECO:0000256|PIRNR:PIRNR019029}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR019029}.
CC -!- SIMILARITY: Belongs to the bZIP family. NFIL3 subfamily.
CC {ECO:0000256|ARBA:ARBA00006079, ECO:0000256|PIRNR:PIRNR019029}.
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DR RefSeq; XP_007193486.1; XM_007193424.2.
DR AlphaFoldDB; A0A384B1B6; -.
DR STRING; 310752.A0A384B1B6; -.
DR GeneID; 103014898; -.
DR KEGG; bacu:103014898; -.
DR CTD; 4783; -.
DR InParanoid; A0A384B1B6; -.
DR OrthoDB; 4467729at2759; -.
DR Proteomes; UP000261681; 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:UniProtKB-UniRule.
DR GO; GO:0006955; P:immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd14694; bZIP_NFIL3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR047229; NFIL3-like.
DR InterPro; IPR047106; NFIL3-like_bZIP.
DR InterPro; IPR016743; NFIL3/E4BP4.
DR InterPro; IPR010533; Vert_IL3-reg_TF.
DR PANTHER; PTHR15284; NUCLEAR FACTOR INTERLEUKIN-3-REGULATED PROTEIN; 1.
DR PANTHER; PTHR15284:SF1; NUCLEAR FACTOR INTERLEUKIN-3-REGULATED PROTEIN; 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; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|PIRNR:PIRNR019029};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108,
KW ECO:0000256|PIRNR:PIRNR019029};
KW DNA-binding {ECO:0000256|PIRNR:PIRNR019029};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR019029};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR019029};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR019029};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR019029}.
FT DOMAIN 73..123
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 188..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..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"
SQ SEQUENCE 462 AA; 51262 MW; AA798D478322151E CRC64;
MQLRKMQSIK KEQASLDAGS SVDKMMVLNS ALSEVSEDLT TGEELLLNEG SVGKNKSSAC
RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
SLKLKFGLIS SAAYAQEIQK LSNSTAVYFQ DYQTSKSTVS AFVDEHEPSM VASSCISVIK
HSPQSSLSDV SEVSSLEHSQ EGPGQSGCRS PESKFQVIKQ EPMELESYAR EPRDDPGAYR
AAVYQNYMGS SFPGYSHSPP LLQVNRSSSN SPRTSETDEG AVGKSSDGED EQQVPKGPIH
SPVELQRVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDHEFDGTQK LSSPVDMTSK
RHFELEKHNA PNLVHSSLTP FSVQVTNIQD WSLKSEHWHQ KELNGKTQNS YKTGVVEVKD
NGYKVSDPEN LFLKQGIANL SAEVVSLKRL IATHQISASD SG
//
