REL_MOUSE
ID REL_MOUSE Reviewed; 587 AA.
AC P15307;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 25-MAY-2022, entry version 160.
DE RecName: Full=Proto-oncogene c-Rel;
GN Name=Rel;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=2654811;
RA Grumont R.J., Gerondakis S.;
RT "Structure of a mammalian c-rel protein deduced from the nucleotide
RT sequence of murine cDNA clones.";
RL Oncogene Res. 4:1-8(1989).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2204017;
RA Grumont R.J., Gerondakis S.;
RT "The murine c-rel proto-oncogene encodes two mRNAs the expression of which
RT is modulated by lymphoid stimuli.";
RL Oncogene Res. 5:245-254(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2204816; DOI=10.1128/mcb.10.10.5473-5485.1990;
RA Bull P., Morley K.L., Hoekstra M.F., Hunter T., Verma I.M.;
RT "The mouse c-rel protein has an N-terminal regulatory domain and a C-
RT terminal transcriptional transactivation domain.";
RL Mol. Cell. Biol. 10:5473-5485(1990).
RN [4]
RP INTERACTION WITH NFKBIB.
RX PubMed=8816457; DOI=10.1128/mcb.16.10.5444;
RA Suyang H., Phillips R.J., Douglas I., Ghosh S.;
RT "Role of unphosphorylated, newly synthesized IkappaB beta in persistent
RT activation of NF-kappaB.";
RL Mol. Cell. Biol. 16:5444-5449(1996).
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 processes 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: Component of the NF-kappa-B p65-c-Rel complex. Component of
CC the NF-kappa-B p50-c-Rel complex. Component of the NF-kappa-B p52-c-Rel
CC complex. Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex.
CC Interacts with NKIRAS1. Interacts with NFKBIB. Interacts with NFKBIE
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P15307; Q60778: Nfkbib; NbExp=5; IntAct=EBI-5323778, EBI-644469;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; X15842; CAA33843.1; ALT_SEQ; mRNA.
DR EMBL; X60271; CAA42817.1; -; mRNA.
DR PIR; A60367; A60367.
DR AlphaFoldDB; P15307; -.
DR SMR; P15307; -.
DR DIP; DIP-59241N; -.
DR IntAct; P15307; 7.
DR STRING; 10090.ENSMUSP00000099928; -.
DR iPTMnet; P15307; -.
DR PhosphoSitePlus; P15307; -.
DR EPD; P15307; -.
DR jPOST; P15307; -.
DR MaxQB; P15307; -.
DR PaxDb; P15307; -.
DR PRIDE; P15307; -.
DR ProteomicsDB; 253217; -.
DR MGI; MGI:97897; Rel.
DR eggNOG; ENOG502QQS6; Eukaryota.
DR InParanoid; P15307; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR ChiTaRS; Rel; mouse.
DR PRO; PR:P15307; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P15307; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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; ISO:MGI.
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:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
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 Acetylation; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04864"
FT CHAIN 2..587
FT /note="Proto-oncogene c-Rel"
FT /id="PRO_0000205166"
FT DOMAIN 8..297
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 403..468
FT /note="Transcriptional transactivator"
FT MOTIF 291..296
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q04864"
FT MOD_RES 267
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="G -> E (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="G -> P (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..154
FT /note="CVFMF -> LCFQV (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="D -> H (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="S -> SS (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64960 MW; 98FC237B6D140416 CRC64;
MASSGYNPYV EIIEQPRQRG MRFRYKCEGR SAGSIPGERS TDNNRTYPSV QIMNYYGKGK
IRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGPERRPL FFQNLGIRCV KKKEVKGAII
LRISAGINPF NVGEQQLLDI EDCDLNVVRC VFMFFLPDED GNFTTALPPI VSNPIYDNRA
PNTAELRICR VNKNCGSVRG GDEIFLLCDK VQKDDIEVRF VLNDWEARGV FSQADVHRQV
AIVFKTPPYC KAILEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDAYGNK SKKQKTTLIF
QKLLQDCGHF TEKPRTAPLG STGEGRFIKK ESNLFSHGTV LPEMPRSSGV PGQAEPYYSS
CGSISSGLPH HPPAIPSVAH QPTSWPPVTH PTSHPVSTNT LSTFSAGTLS SNSQGILPFL
EGPGVSDLSA SNSCLYNPDD LARMETPSMS PTDLYSISDV NMLSTRPLSV MAPSTDGMGD
TDNPRLVSIN LENPSCNARL GPRDLRQLHQ MSPASLSAGT SSSSVFVSQS DAFDRSNFSC
VDNGLMNEPG LSDDANNPTF VQSSHYSVNT LQSEQLSDPF TYGFFKI
