ID   REL_MELGA               Reviewed;         538 AA.
AC   P01125;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Proto-oncogene c-Rel;
DE   AltName: Full=p68;
DE   Flags: Fragment;
GN   Name=REL;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6090694; DOI=10.1128/jvi.52.1.172-182.1984;
RA   Wilhelmsen K.C., Eggleton K., Temin H.M.;
RT   "Nucleic acid sequences of the oncogene v-rel in reticuloendotheliosis
RT   virus strain T and its cellular homolog, the proto-oncogene c-rel.";
RL   J. Virol. 52:172-182(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 531-538.
RA   Temin H.M.;
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Proto-oncogene that may play a role in differentiation and
CC       lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which
CC       is present in almost all cell types and is involved in many biological
CC       processed such as inflammation, immunity, differentiation, cell growth,
CC       tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric
CC       complex formed by the Rel-like domain-containing proteins RELA/p65,
CC       RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at
CC       kappa-B sites in the DNA of their target genes and the individual
CC       dimers have distinct preferences for different kappa-B sites that they
CC       can bind with distinguishable affinity and specificity. Different dimer
CC       combinations act as transcriptional activators or repressors,
CC       respectively. NF-kappa-B is controlled by various mechanisms of post-
CC       translational modification and subcellular compartmentalization as well
CC       as by interactions with other cofactors or corepressors. NF-kappa-B
CC       complexes are held in the cytoplasm in an inactive state complexed with
CC       members of the NF-kappa-B inhibitor (I-kappa-B) family. In a
CC       conventional activation pathway, I-kappa-B is phosphorylated by I-
CC       kappa-B kinases (IKKs) in response to different activators,
CC       subsequently degraded thus liberating the active NF-kappa-B complex
CC       which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-
CC       c-Rel is a transcriptional activator (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex.
CC       Component of the NF-KAPPA-B p65-c-Rel complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; X03508; CAA27220.1; -; Genomic_DNA.
DR   EMBL; X03616; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03617; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03618; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03619; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03620; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03621; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03622; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; X03623; CAA27220.1; JOINED; Genomic_DNA.
DR   EMBL; K02455; AAA99433.1; -; Genomic_DNA.
DR   EMBL; K02447; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02448; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02449; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02450; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02451; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02452; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02453; AAA99433.1; JOINED; Genomic_DNA.
DR   EMBL; K02454; AAA99433.1; JOINED; Genomic_DNA.
DR   PIR; A01377; TVTK.
DR   AlphaFoldDB; P01125; -.
DR   SMR; P01125; -.
DR   InParanoid; P01125; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd01177; IPT_NFkappaB; 1.
DR   CDD; cd07933; RHD-n_c-Rel; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.340; -; 1.
DR   InterPro; IPR030505; c-Rel.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR033926; IPT_NFkappaB.
DR   InterPro; IPR000451; NFkB/Dor.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR042845; RHD-n_c-Rel.
DR   InterPro; IPR030492; RHD_CS.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR24169; PTHR24169; 1.
DR   PANTHER; PTHR24169:SF4; PTHR24169:SF4; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   PRINTS; PR00057; NFKBTNSCPFCT.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS01204; REL_1; 1.
DR   PROSITE; PS50254; REL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome.
FT   CHAIN           <1..>538
FT                   /note="Proto-oncogene c-Rel"
FT                   /id="PRO_0000205168"
FT   DOMAIN          5..294
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   REGION          401..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           287..292
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        401..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        6
FT                   /note="Y -> C (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="G -> R (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="G -> D (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="V -> M (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="E -> K (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="P -> L (in Ref. 1; AAA99433)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         538
SQ   SEQUENCE   538 AA;  60002 MW;  941ACF923E1EA6D4 CRC64;
     GISEPYIEIF EQPRQRGMRF RYKCEGRSAG SIPGEHSTDN NKTFPSIQIL NYFGKVKIRT
     TLVTKNEPYK PHPHDLVGKD CRDGYYEAEF GPERRVLSFQ NLGIQCVKKK DLKESISLRI
     SKKINPFNVP EEQLHNIDEY DLNVVRLCFQ AFLPDEHGNY TLALPPLISN PIYDNGAPNT
     AELRICRVNK NCGSVKGGDE IFLLCDKVQK DDIEVRFVLG NWEAKGSFSQ ADVHRQVAIV
     FRTPPFLRDI TEPITVKMQL RRPSDQEVSE PVDFRYLPDE EDSYGNKAKR QRSTLAWQKL
     IQDCGSAVTE RPKAAPIPTV NPEGKLIKKE PNMFSPTLML PGLGTLASSS QMYPACSQMP
     TQPAQLGPGK QDTLHSCWQQ LYSPSPSASS LLSMHSHNSF TAEVPQPGAQ GSSSLPAYHD
     NPLNWPDEKD SSFYRNFGNT HGMGAALVSA ADMQSVSSSS IVQGTHQASA TAASIMNMET
     NDMNCTSLNF EKYTQMLNVS NHRQQLHQVP ATCPPGSAWQ HSLSSQPNVA DRAVYSSF