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RELB_CHICK
ID   RELB_CHICK              Reviewed;         549 AA.
AC   P51509; Q90721; Q9PWF4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Transcription factor RelB homolog;
GN   Name=RELB;
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 RELB-P50
RP   COMPLEX, AND IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
RC   TISSUE=Spleen;
RX   PubMed=11529676; DOI=10.1006/mcbr.2001.0290;
RA   Piffat K.A., Hrdlickova R., Nehyba J., Ikeda T., Liss A., Huang S., Sif S.,
RA   Gilmore T.D., Bose H.R. Jr.;
RT   "The chicken RelB transcription factor has transactivation sequences and a
RT   tissue-specific expression pattern that are distinct from mammalian RelB.";
RL   Mol. Cell Biol. Res. Commun. 4:266-275(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 151-424.
RC   TISSUE=Spleen;
RA   Ikeda T.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 150-479.
RA   Gilmore T.D., Piffat K.A., Huang S., Sif S.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor which is
CC       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. NF-kappa-B heterodimeric RelB-p50
CC       and RelB-p52 complexes are transcriptional activators. Stimulates
CC       promoter activity in the presence of p49- and p50-NF-kappa-B. Neither
CC       associates with DNA nor with p65-NF-kappa-B. May play a role in the
CC       regulation of the circadian clock (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component of the
CC       NF-kappa-B RelB-p52 complex. {ECO:0000269|PubMed:11529676}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; AF029260; AAD41539.1; -; mRNA.
DR   EMBL; D13794; BAA02947.1; -; mRNA.
DR   EMBL; U51737; AAA96827.1; -; mRNA.
DR   AlphaFoldDB; P51509; -.
DR   SMR; P51509; -.
DR   VEuPathDB; HostDB:geneid_396500; -.
DR   InParanoid; P51509; -.
DR   PhylomeDB; P51509; -.
DR   PRO; PR:P51509; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; IPR030496; RelB.
DR   InterPro; IPR032400; RelB_transact.
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:SF18; PTHR24169:SF18; 1.
DR   Pfam; PF16181; RelB_transactiv; 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   Activator; Biological rhythms; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..549
FT                   /note="Transcription factor RelB homolog"
FT                   /id="PRO_0000205175"
FT   DOMAIN          135..412
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   REGION          100..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        266
FT                   /note="G -> A (in Ref. 1; AAD41539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="A -> G (in Ref. 2; BAA02947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="G -> E (in Ref. 2; BAA02947)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="R -> A (in Ref. 3; AAA96827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        479
FT                   /note="S -> F (in Ref. 3; AAA96827)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  60193 MW;  1766BCF2C78BA37D CRC64;
     MFAPSLAAFR AMALPIPRLA PVMKSVQPAS FPVLGSMAAR LSTARGGRGL RAGRRPPGGP
     KGAAAAEEMA VPIGAALQDP NVGMAPVNDD LEIIEEVMKE DGFQPDPPPP GSPHDPPKLI
     PRGLGVPVGR RDPPRDPPRL IITEQPKKTG MRFRYECEGR SAGSILGESS TEASKTLPAI
     ELLNCQAIPE VQVTACLVWK DWPHRVHPHG LVGKDCSNGL CQVRLQPHAN PRHSFSNLGI
     QCVKKKEIEA AIEKKLQLGI DPFKAGSLKN HQEVDMNVVR ICFQASYRDG SGRTRQLSPV
     LSEPIFDKKS TNTSELRICR MNKESGPCTG GEELYLLCDK VQKEDIAVVF RKEPWEARAD
     FSQADVHRQG AIVLRTPPYR CVQLSEPVQV EVFLQRLTDR ARSRGCPYTY LPRERDAYGV
     KVKRKRGMPD LLEELSGADP YGIEAKRRKP PPGFMDHFAP LPAADEAFAL LADPLDPLSH
     LPPPSTPQIL WGRSYFRTPP PTETPTPPTA SWGPICSQGT SEGGGGRTSP RYRPPPPLKW
     GSQWAPPHQ
 
 
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