REL_CHICK
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 03-AUG-2022, entry version 148.
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 (2.85 ANGSTROMS) OF 7-281 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};
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DR EMBL; X52193; CAA36439.1; -; mRNA.
DR EMBL; M26381; AAA48721.1; -; mRNA.
DR PIR; A34098; TVCHRL.
DR PIR; S10893; S10893.
DR RefSeq; NP_001161198.1; NM_001167726.1.
DR PDB; 1GJI; X-ray; 2.85 A; A/B=7-281.
DR PDBsum; 1GJI; -.
DR AlphaFoldDB; P16236; -.
DR SMR; P16236; -.
DR STRING; 9031.ENSGALP00000039504; -.
DR iPTMnet; P16236; -.
DR PaxDb; P16236; -.
DR PRIDE; P16236; -.
DR GeneID; 396500; -.
DR KEGG; gga:396500; -.
DR CTD; 5966; -.
DR VEuPathDB; HostDB:geneid_396500; -.
DR eggNOG; ENOG502QQS6; Eukaryota.
DR InParanoid; P16236; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; P16236; -.
DR EvolutionaryTrace; P16236; -.
DR PRO; PR:P16236; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; TAS:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006357; P: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 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 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 COMPBIAS 391..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 STRAND 256..263
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
