ID   TF65_XENLA              Reviewed;         527 AA.
AC   Q04865;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative transcription factor p65 homolog;
DE   AltName: Full=XRel1;
GN   Name=rela; Synonyms=rel1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=2011580; DOI=10.1073/pnas.88.7.2697;
RA   Kao K.R., Hopwood N.D.;
RT   "Expression of a mRNA related to c-rel and dorsal in early Xenopus laevis
RT   embryos.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2697-2701(1991).
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   -!- 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: Predominantly in the animal hemisphere of the
CC       oocyte; all tissues of early embryo. {ECO:0000269|PubMed:2011580}.
CC   -!- DEVELOPMENTAL STAGE: Oocyte and early embryo.
CC       {ECO:0000269|PubMed:2011580}.
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}.
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DR   EMBL; M60785; AAA49945.1; -; mRNA.
DR   PIR; A38631; A38631.
DR   RefSeq; NP_001081048.1; NM_001087579.1.
DR   AlphaFoldDB; Q04865; -.
DR   SMR; Q04865; -.
DR   BioGRID; 98955; 1.
DR   PRIDE; Q04865; -.
DR   DNASU; 394353; -.
DR   GeneID; 394353; -.
DR   KEGG; xla:394353; -.
DR   CTD; 394353; -.
DR   Xenbase; XB-GENE-946512; rela.L.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 394353; Expressed in lung and 19 other tissues.
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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..527
FT                   /note="Putative transcription factor p65 homolog"
FT                   /id="PRO_0000205172"
FT   DOMAIN          18..306
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   REGION          381..444
FT                   /note="Transcriptional activation domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q04207"
FT   REGION          494..527
FT                   /note="Transcriptional activation domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q04207"
FT   MOTIF           301..304
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           513..521
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         276
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   527 AA;  59059 MW;  320E1CF5BC546B79 CRC64;
     MDGFHWTDIV SSMPPSIPPV EIIEQPKQRG MRFRYKCEGR SAGSIPGERS TDTSKTHPTI
     KINNYQGPAR IRISLVTKDS PHKPHPHELV GKDCKDGYYE AELSPDRSIH SFQNLGIQCV
     KKREVEDAVA HRIRTNNNPF NVSPEELKAD YDLNTVCLCF QVFIPDQAAG RMLPLPFVVS
     QPIYDNRAPN TAELKICRVN KNSGSCLGGD EIFLLCDKVQ KEDIEVIFGL GNWEARGIFS
     QADVHRQVAI VFRTPAFQDT KIRQSVKVQM QLRRPSDKEV SEPMEFQYLP DEGDPHHIDE
     KRKRTLDNFK HYVKNNPFAG GETRPQRRIA VANRNVPTKS EPIRPSIPVP NPVVSCLPFS
     MPVLKAENVT SPSTLLSTVN ISDFSNLGFS SQPPSQSDHD RLESMLNYPS FPGDANLDLV
     EMLPHENESR CTSLSSIDNS DFSQLLSESQ SSGTLSAALQ EPGTSQGTFM AYPESIARLM
     TNRPNEDEGG ERIDSGLING MFDISREEIH LTSLFELDFS SLLSNMK