TF65_CHICK
ID TF65_CHICK Reviewed; 558 AA.
AC P98152;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transcription factor p65;
DE AltName: Full=Nuclear factor NF-kappa-B p65 subunit;
GN Name=RELA;
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], IDENTIFICATION IN THE NF-KAPPA-B P65-P50
RP COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX, IDENTIFICATION
RP IN THE NF-KAPPA-B P65-P105 COMPLEX, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in
CC almost all cell types and is the endpoint of a series of signal
CC transduction events that are initiated by a vast array of stimuli
CC related to many biological processes such as inflammation, immunity,
CC differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B
CC is a homo- or heterodimeric complex formed by the Rel-like domain-
CC containing proteins. The dimers bind at kappa-B sites in the DNA of
CC their target genes and the individual dimers have distinct preferences
CC for different kappa-B sites that they can bind with distinguishable
CC affinity and specificity. Different dimer combinations act as
CC transcriptional activators or repressors, respectively. NF-kappa-B is
CC controlled by various mechanisms of post-translational modification and
CC subcellular compartmentalization as well as by interactions with other
CC cofactors or corepressors. NF-kappa-B complexes are held in the
CC cytoplasm in an inactive state complexed with members of the NF-kappa-B
CC inhibitor (I-kappa-B) family. In a conventional activation pathway, I-
CC kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to
CC different activators, subsequently degraded thus liberating the active
CC NF-kappa-B complex which translocates to the nucleus. RELA shows a weak
CC DNA-binding site which could contribute directly to DNA binding in the
CC NF-kappa-B complex. {ECO:0000250|UniProtKB:Q04206}.
CC -!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of the
CC NF-kappa-B p65-c-Rel complex. Component of the NF-kappa-B p65-p105
CC complex. {ECO:0000269|PubMed:7916720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04207}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q04207}. Note=Nuclear, but also found in the
CC cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).
CC {ECO:0000250|UniProtKB:Q04206}.
CC -!- TISSUE SPECIFICITY: Spleen; lower level in brain.
CC {ECO:0000269|PubMed:7916720}.
CC -!- DOMAIN: The transcriptional activation domain 1/TA1 and the
CC transcriptional activation domain 2/TA2 have direct transcriptional
CC activation properties (By similarity). The 9aaTAD motif found within
CC the transcriptional activation domain 2 is a conserved motif present in
CC a large number of transcription factors that is required for their
CC transcriptional transactivation activity (By similarity).
CC {ECO:0000250|UniProtKB:Q04206, ECO:0000250|UniProtKB:Q04207}.
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; D13721; BAA02874.1; -; mRNA.
DR PIR; JC2004; JC2004.
DR RefSeq; NP_990460.1; NM_205129.1.
DR AlphaFoldDB; P98152; -.
DR SMR; P98152; -.
DR GeneID; 396027; -.
DR KEGG; gga:396027; -.
DR CTD; 5970; -.
DR VEuPathDB; HostDB:geneid_396027; -.
DR InParanoid; P98152; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; P98152; -.
DR Reactome; R-GGA-1227892; TRAF6 mediated NF-kB activation.
DR Reactome; R-GGA-434001; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
DR Reactome; R-GGA-434131; NFkB activation mediated by RIP1 complexed with activated TLR3.
DR PRO; PR:P98152; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071159; C:NF-kappaB complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
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:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
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:0002755; P:MyD88-dependent toll-like receptor signaling pathway; NAS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 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.
DR InterPro; IPR030495; RelA.
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; 2.
DR PANTHER; PTHR24169:SF1; PTHR24169:SF1; 2.
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 Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..558
FT /note="Transcription factor p65"
FT /id="PRO_0000205171"
FT DOMAIN 25..311
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 317..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..444
FT /note="Transcriptional activation domain 1"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT REGION 388..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..558
FT /note="Transcriptional activation domain 2"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT MOTIF 306..309
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 542..558
FT /note="9aaTAD"
FT /evidence="ECO:0000255"
FT COMPBIAS 325..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 558 AA; 60072 MW; 0528D159A4D47B36 CRC64;
MEPADLLPLY LQPEWGEQEP GGATPFVEIL EQPKQRGMRF RYKCEGRSAG SIPGEHSTDS
ARTHPTIRVN HYRGPGRVRV SLVTKDPPHG PHPHELVGRH CQHGYYEAEL SPERCVHSFQ
NLGIQCVKKR ELEAAVAERI RTNNNPFNVP MEERGAEYDL SAVRLCFQVW VNGPGGLCPL
PPVLSQPIYD NRAPSTAELR ILPGDRNSGS CQGGDEIFLL CDKVQKEDIE VRFWAEGWEA
KGSFAAADVH RQVAIVFRTP PFRERSLRHP VTVRMELQRP SDRQRSPPLD FRYLPHQGDL
QCIEEKRKRT RDTFRAFVQR APLPGLEPNP EPRPPRRIAV PSRPPPAPQQ PPSMVGAPPA
PLFPLGVPPA SSPTPEPLAE ALLQLQFDDG VGGSGPPPST TTTTTTTQCA LGGGIPDPGG
SPLDLGALLG DPPFDTIDAA ELQRLLGPPE TPPGGIGAGG GFGELLSLPT NFGDPPSSTA
ATFGPSPPML LSYPEAITRL VQCQTPGGSG GGGPPVGPPQ DLGGPLHPPG APPQPTEDSL
PSLGDLDFSA FLSQFPSS
