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Database: UniProt
Entry: A0A087RHC9_APTFO
LinkDB: A0A087RHC9_APTFO
Original site: A0A087RHC9_APTFO 
ID   A0A087RHC9_APTFO        Unreviewed;       458 AA.
AC   A0A087RHC9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Nuclear factor interleukin-3-regulated protein {ECO:0000256|ARBA:ARBA00018259, ECO:0000256|PIRNR:PIRNR019029};
GN   ORFNames=AS27_03603 {ECO:0000313|EMBL:KFM12883.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM12883.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM12883.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM12883.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a transcriptional regulator of a number of
CC       proteins of the circadian clock. {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   EMBL; KL226361; KFM12883.1; -; Genomic_DNA.
DR   RefSeq; XP_009285471.1; XM_009287196.2.
DR   AlphaFoldDB; A0A087RHC9; -.
DR   STRING; 9233.A0A087RHC9; -.
DR   GeneID; 103905515; -.
DR   KEGG; afor:103905515; -.
DR   CTD; 4783; -.
DR   OrthoDB; 4467729at2759; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
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:UP000053286};
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..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..214
FT                   /note="Polar residues"
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        256..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"
SQ   SEQUENCE   458 AA;  51269 MW;  F0A0C3046083DF92 CRC64;
     MQLRKMQTLK KEHGPVDAGS NVDKIMVLKS TLAEVSEELS TNEDILLTEA SSGKSKSSAC
     RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV LENKLIALGE ENATLKAELL
     SLKLKFGLIS SAAYAQEIQK LSSSTTVYFQ DYQSSKSNIN SFVDEHEPSI VGSSCISVIK
     HSPQSSMSDV SEISSVEHTQ PNRIQSNCRS PENKFQIIKQ EPMELEREPR DDRGSYKASI
     YPNYMGTTFN VYSHSPPLLQ VNRSSSNSPR TSETDDGVVG KSSDGEDEQQ VPKGPIHSPV
     EHKNVHATVK VPEVNSSALP HKLRIKAKAM QVKVEAMDND YDATQKLSSP IDMSSKRHFE
     LEKHGAQNLV HSSHTPFSVQ VTNIQDWSLK PELWHQKELN VKIQSGCKTG VVEIKDNIYN
     VSESENLYLK QGIANLSAEV ASLKRLITTQ QISASDSG
//
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