ID REL_CHICK Reviewed; 598 AA. AC P16236; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 04-NOV-2026, entry version 161. DE RecName: Full=Proto-oncogene c-Rel; DE AltName: Full=p68; GN Name=REL; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=2179815; RA Capobianco A.J., Simmons D.L., Gilmore T.D.; RT "Cloning and expression of a chicken c-rel cDNA: unlike p59v-rel, p68c-rel RT is a cytoplasmic protein in chicken embryo fibroblasts."; RL Oncogene 5:257-265(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-7. RX PubMed=2167440; DOI=10.1128/mcb.10.9.4788-4794.1990; RA Kabrun N., Bumstead N., Hayman M.J., Enrietto P.J.; RT "Characterization of a novel promoter insertion in the c-rel locus."; RL Mol. Cell. Biol. 10:4788-4794(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-598. RX PubMed=2555689; DOI=10.1128/mcb.9.10.4323-4336.1989; RA Hannink M., Temin H.M.; RT "Transactivation of gene expression by nuclear and cytoplasmic rel RT proteins."; RL Mol. Cell. Biol. 9:4323-4336(1989). RN [4] RP IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX. RX PubMed=7916720; DOI=10.1016/0378-1119(93)90645-j; RA Ikeda T., Honjo K., Hirota Y., Onodera T.; RT "Isolation of the chicken NF-kappa B p65 subunit-encoding cDNA and RT characterization of its products."; RL Gene 133:237-242(1993). RN [5] RP IDENTIFICATION, AND MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=16287166; DOI=10.1002/pmic.200402056; RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J., RA Schneider J., Palomar M.A., Linares R.; RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of RT development."; RL Proteomics 5:4946-4957(2005). RN [6] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH IL2 DNA. RX PubMed=11587641; DOI=10.1016/s0969-2126(01)00635-9; RA Huang D.B., Chen Y.Q., Ruetsche M., Phelps C.B., Ghosh G.; RT "X-ray crystal structure of proto-oncogene product c-Rel bound to the CD28 RT response element of IL-2."; RL Structure 9:669-678(2001). 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. CC {ECO:0000269|PubMed:11587641, ECO:0000269|PubMed:7916720}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MASS SPECTROMETRY: Mass=63513; Mass_error=3; Method=MALDI; CC Evidence={ECO:0000269|PubMed:16287166}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52193; CAA36439.1; -; mRNA. DR EMBL; M26381; AAA48721.1; -; mRNA. DR PIR; A34098; TVCHRL. DR PIR; S10893; S10893. DR RefSeq; NP_001161198.2; NM_001167726.2. DR PDB; 1GJI; X-ray; 2.85 A; A/B=7-281. DR AlphaFoldDB; P16236; -. DR SMR; P16236; -. DR FunCoup; P16236; 516. DR STRING; 9031.ENSGALP00000039504; -. DR iPTMnet; P16236; -. DR PaxDb; 9031-ENSGALP00000039504; -. DR GeneID; 396500; -. DR KEGG; gga:396500; -. DR CTD; 5966; -. DR VEuPathDB; HostDB:geneid_396500; -. DR eggNOG; ENOG502QQS6; Eukaryota. DR InParanoid; P16236; -. DR OMA; ACPIKQS; -. DR OrthoDB; 7881762at2759; -. DR PhylomeDB; P16236; -. DR EvolutionaryTrace; P16236; -. DR PRO; PR:P16236; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; TAS:AgBase. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; TAS:AgBase. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:AgBase. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006309; P:apoptotic DNA fragmentation; IDA:AgBase. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central. DR CDD; cd01177; IPT_NFkappaB; 1. DR CDD; cd07933; RHD-n_c-Rel; 1. DR FunFam; 2.60.40.340:FF:000003; NFkB p65 transcription factor; 1. DR FunFam; 2.60.40.10:FF:000046; Nuclear factor NF-kappa-B p105 subunit; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1. 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_sf. 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; NUCLEAR FACTOR NF-KAPPA-B PROTEIN; 1. DR PANTHER; PTHR24169:SF4; PROTO-ONCOGENE C-REL; 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; SSF81296; E set domains; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome. FT CHAIN 1..598 FT /note="Proto-oncogene c-Rel" FT /id="PRO_0000205167" FT DOMAIN 7..296 FT /note="RHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265" FT REGION 391..426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 289..294 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOD_RES 266 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000255" FT CONFLICT 74 FT /note="H -> L (in Ref. 3; AAA48721)" FT /evidence="ECO:0000305" FT CONFLICT 205 FT /note="I -> L (in Ref. 3; AAA48721)" FT /evidence="ECO:0000305" FT CONFLICT 317 FT /note="A -> T (in Ref. 3; AAA48721)" FT /evidence="ECO:0000305" FT CONFLICT 410 FT /note="G -> N (in Ref. 3; AAA48721)" FT /evidence="ECO:0000305" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:1GJI" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 114..122 FT /evidence="ECO:0007829|PDB:1GJI" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 133..137 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 146..156 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:1GJI" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 202..208 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:1GJI" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 256..264 FT /evidence="ECO:0007829|PDB:1GJI" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:1GJI" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:1GJI" SQ SEQUENCE 598 AA; 66847 MW; 74B38AE57A8B5CD3 CRC64; MAGISEPYIE IFEQPRQRGM RFRYKCEGRS AGSIPGEHST DNNKTFPSIQ ILNYFGKVKI RTTLVTKNEP YKPHPHDLVG KDCRDGYYEA EFGPERRVLS FQNLGIQCVK KKDLKESISL RISKKINPFN VPEEQLHNID EYDLNVVRLC FQAFLPDEHG NYTLALPPLI SNPIYDNRAP NTAELRICRV NKNCGSVKGG DEIFILCDKV QKDDIEVRFV LDNWEAKGSF SQADVHRQVA IVFRTPPFLR DITEPITVKM QLRRPSDQEV SEPMDFRYLP DEKDPYGNKA KRQRSTLAWQ KLIQDCGSAV TERPKAAPIP TVNPEGKLIK KEPNMFSPTL MLPGLGTLTS SSQMYPPCSQ MPHQPAQLGP GKQDTLPSCW QQLFSSSPSA SSLLSMHPHN SFTAEVPQPG AQGSSSLPAF HDNPLNWPDE KDSSFYRNFG STNGMGAAMV SAADMQSASS NSIVHATHQA SATAASIVNM ETNDMNCTSL NFEKYTQVLN VSNHRQQLHQ APAACPPVAA PGSTPFSSQP NLADTAVYNS FLDQEVISDS RLSTNPLQNH QNSLTLTDNQ FYDTDGVHTD ELYQSFQLDT NILQSYNH //