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Nuclear factor NF-kappa-B p110 subunit (Rel-p110) (Relish protein) [Cleaved into: Nuclear factor NF-kappa-B p68 subunit (Rel-p68); Nuclear factor NF-kappa-B p49 subunit (Rel-p49)]

 NFKB1_DROME             Reviewed;         971 AA.
Q94527; A4V2K3; Q9U435; Q9U436; Q9U437; Q9U438; Q9U439; Q9U440;
Q9U6H3; Q9U6H4; Q9U6H5; Q9VHI0;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
18-JUL-2018, entry version 164.
RecName: Full=Nuclear factor NF-kappa-B p110 subunit;
AltName: Full=Rel-p110;
AltName: Full=Relish protein;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p68 subunit;
AltName: Full=Rel-p68;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p49 subunit;
AltName: Full=Rel-p49;
Name=Rel {ECO:0000312|FlyBase:FBgn0014018};
ORFNames=CG11992 {ECO:0000312|FlyBase:FBgn0014018};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL13493.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAJOR), FUNCTION, AND
DEVELOPMENTAL STAGE.
PubMed=8816802; DOI=10.1073/pnas.93.19.10343;
Dushay M.S., Asling B., Hultmark D.;
"Origins of immunity: Relish, a compound Rel-like gene in the
antibacterial defense of Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 93:10343-10347(1996).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS MAJOR AND MATERNAL),
FUNCTION, AND INDUCTION.
PubMed=10619029; DOI=10.1016/S1097-2765(00)80392-5;
Hedengren M., Asling B., Dushay M.S., Ando I., Ekengren S.,
Wihlborg M., Hultmark D.;
"Relish, a central factor in the control of humoral, but not cellular
immunity in Drosophila.";
Mol. Cell 4:827-837(1999).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MAJOR).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Head {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-880, AND VARIANTS SER-82;
LEU-110; ILE-699; GLY-845 AND ASN-862.
STRAIN=Zim1 {ECO:0000269|PubMed:10757765},
Zim2 {ECO:0000269|PubMed:10757765},
Zim3 {ECO:0000269|PubMed:10757765},
Zim5 {ECO:0000269|PubMed:10757765},
Zim7 {ECO:0000269|PubMed:10757765}, and
Zim8 {ECO:0000269|PubMed:10757765};
PubMed=10757765;
Begun D.J., Whitley P.;
"Adaptive evolution of relish, a Drosophila NF-kappaB/IkappaB
protein.";
Genetics 154:1231-1238(2000).
[7] {ECO:0000305}
PROTEIN SEQUENCE OF 546-553, FUNCTION, PROTEOLYTIC CLEAVAGE, AND
SUBCELLULAR LOCATION.
PubMed=11269501; DOI=10.1093/embo-reports/kvd072;
Stoeven S., Ando I., Kadalayil L., Engstrom Y., Hultmark D.;
"Activation of the Drosophila NF-kappaB factor Relish by rapid
endoproteolytic cleavage.";
EMBO Rep. 1:347-352(2000).
[8] {ECO:0000305}
DEVELOPMENTAL STAGE, INTERACTION WITH DREDD, AND MUTAGENESIS OF
ASP-545.
PubMed=11269502; DOI=10.1093/embo-reports/kvd073;
Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.;
"The Drosophila caspase Dredd is required to resist Gram-negative
bacterial infection.";
EMBO Rep. 1:353-358(2000).
[9] {ECO:0000305}
FUNCTION, AND PHOSPHORYLATION.
PubMed=11018014; DOI=10.1101/gad.817800;
Silverman N., Zhou R., Stoeven S., Pandey N., Hultmark D.,
Maniatis T.;
"A Drosophila IkappaB kinase complex required for Relish cleavage and
antibacterial immunity.";
Genes Dev. 14:2461-2471(2000).
[10] {ECO:0000305}
FUNCTION.
PubMed=11872802; DOI=10.1126/science.1070216;
Choe K.-M., Werner T., Stoeven S., Hultmark D., Anderson K.V.;
"Requirement for a peptidoglycan recognition protein (PGRP) in Relish
activation and antibacterial immune responses in Drosophila.";
Science 296:359-362(2002).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18000549; DOI=10.1371/journal.pone.0001178;
Ayyar S., Pistillo D., Calleja M., Brookfield A., Gittins K.,
Goldstone C., Simpson P.;
"NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila.";
PLoS ONE 2:E1178-E1178(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620 AND TYR-626, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
Akhouayri I., Turc C., Royet J., Charroux B.;
"Toll-8/Tollo negatively regulates antimicrobial response in the
Drosophila respiratory epithelium.";
PLoS Pathog. 7:E1002319-E1002319(2011).
[14]
INTERACTION WITH DMAP1.
PubMed=24947515; DOI=10.1074/jbc.C114.553719;
Goto A., Fukuyama H., Imler J.L., Hoffmann J.A.;
"The chromatin regulator DMAP1 modulates activity of the nuclear
factor B (NF-B) transcription factor Relish in the Drosophila innate
immune response.";
J. Biol. Chem. 289:20470-20476(2014).
[15]
FUNCTION.
PubMed=25477468; DOI=10.1126/science.1258236;
Meyer S.N., Amoyel M., Bergantinos C., de la Cova C., Schertel C.,
Basler K., Johnston L.A.;
"An ancient defense system eliminates unfit cells from developing
tissues during cell competition.";
Science 346:1258236-1258236(2014).
-!- FUNCTION: Plays a key role in the humoral immune response
(PubMed:8816802, PubMed:10619029, PubMed:11269501,
PubMed:11872802, PubMed:22022271). Rel-p68 subunit translocates to
the nucleus where it binds to the promoter of the Cecropin A1 gene
and probably other antimicrobial peptide genes (PubMed:11269501).
I-kappa-B kinase complex (IKKbeta and key) and PGRP-LC are
essential signaling components in transmitting the
lipopolysaccharide (LPS) signal leading to cact degradation for
NF-kappa-B (rel) activation (PubMed:11872802, PubMed:11018014).
Part of a Toll-related receptor pathway that functions in the
apoptosis of unfit cells during cell competition
(PubMed:25477468). May be part of a NF-kappa-B and Tollo signaling
cascade that regulates development of the peripheral nervous
system (PubMed:18000549). Possibly post-transcriptionally
regulates the neuron-specific genes sc and ase, by promoting the
rapid turnover of their transcripts in the wing imaginal disk
(PubMed:18000549). {ECO:0000269|PubMed:10619029,
ECO:0000269|PubMed:11018014, ECO:0000269|PubMed:11269501,
ECO:0000269|PubMed:11872802, ECO:0000269|PubMed:18000549,
ECO:0000269|PubMed:25477468, ECO:0000269|PubMed:8816802}.
-!- SUBUNIT: Rel-p68 subunit interacts with Dredd (PubMed:11269502).
Interacts with DMAP1 (PubMed:24947515).
{ECO:0000269|PubMed:11269502, ECO:0000269|PubMed:24947515}.
-!- INTERACTION:
Q9VS59:akirin; NbExp=4; IntAct=EBI-869024, EBI-96644;
P98149:Dif; NbExp=4; IntAct=EBI-869024, EBI-188843;
P15330:dl; NbExp=2; IntAct=EBI-15786027, EBI-198375;
Q9VEZ5:IKKbeta; NbExp=2; IntAct=EBI-15786027, EBI-148871;
-!- SUBCELLULAR LOCATION: Nuclear factor NF-kappa-B p68 subunit:
Nucleus.
-!- SUBCELLULAR LOCATION: Nuclear factor NF-kappa-B p110 subunit:
Cytoplasm.
-!- SUBCELLULAR LOCATION: Nuclear factor NF-kappa-B p49 subunit:
Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Major {ECO:0000269|PubMed:10619029}; Synonyms=A
{ECO:0000269|PubMed:10619029}, B, C, p110
{ECO:0000269|PubMed:10619029};
IsoId=Q94527-1; Sequence=Displayed;
Name=Maternal {ECO:0000269|PubMed:10619029}; Synonyms=D
{ECO:0000269|PubMed:10619029}, p100 {ECO:0000269|PubMed:10619029};
IsoId=Q94527-2; Sequence=VSP_050089;
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:11269502, ECO:0000269|PubMed:8816802}.
-!- INDUCTION: By bacteria and fungi. {ECO:0000269|PubMed:10619029}.
-!- PTM: Phosphorylated by lipopolysaccharide (LPS)-activated I-kappa-
B kinase complex before being cleaved. Rel-p110 subunit is cleaved
within seconds of an immune challenge into Rel-p49 subunit and
Rel-p68 subunit. Rel-p110 subunit reappears after 45 minutes.
{ECO:0000269|PubMed:11018014, ECO:0000269|PubMed:11269501,
ECO:0000269|PubMed:18327897}.
-!- DISRUPTION PHENOTYPE: Larvae infected with Gram-negative bacteria
fail to activate tracheal expression of the antibacterial peptide
gene Drs (PubMed:22022271). Ectopic bristles develop on the
dorsocentral, scutellar and lateral regions of the noctum, with
one or more ectopic bristles per hemi-notum (PubMed:18000549).
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EMBL; U62005; AAB17264.1; -; mRNA.
EMBL; AF186073; AAF07931.1; -; Genomic_DNA.
EMBL; AF186073; AAF07932.1; -; Genomic_DNA.
EMBL; AF186077; AAF07086.1; -; Genomic_DNA.
EMBL; AF186078; AAF07087.2; -; Genomic_DNA.
EMBL; AE014297; AAF54333.2; -; Genomic_DNA.
EMBL; AE014297; AAS65130.1; -; Genomic_DNA.
EMBL; AE014297; AAS65131.1; -; Genomic_DNA.
EMBL; AE014297; AAS65132.1; -; Genomic_DNA.
EMBL; AY058264; AAL13493.1; -; mRNA.
EMBL; AF204284; AAF20132.1; -; Genomic_DNA.
EMBL; AF204285; AAF20133.1; -; Genomic_DNA.
EMBL; AF204286; AAF20134.1; -; Genomic_DNA.
EMBL; AF204287; AAF20135.1; -; Genomic_DNA.
EMBL; AF204288; AAF20136.1; -; Genomic_DNA.
EMBL; AF204289; AAF20137.1; -; Genomic_DNA.
RefSeq; NP_477094.1; NM_057746.4. [Q94527-1]
RefSeq; NP_996187.1; NM_206465.1. [Q94527-2]
RefSeq; NP_996188.1; NM_206466.1. [Q94527-1]
RefSeq; NP_996189.1; NM_206467.1. [Q94527-1]
UniGene; Dm.4154; -.
ProteinModelPortal; Q94527; -.
SMR; Q94527; -.
BioGrid; 66255; 118.
DIP; DIP-60434N; -.
IntAct; Q94527; 6.
MINT; Q94527; -.
STRING; 7227.FBpp0088375; -.
iPTMnet; Q94527; -.
PaxDb; Q94527; -.
PRIDE; Q94527; -.
EnsemblMetazoa; FBtr0089338; FBpp0088375; FBgn0014018. [Q94527-1]
EnsemblMetazoa; FBtr0089339; FBpp0088973; FBgn0014018. [Q94527-1]
EnsemblMetazoa; FBtr0089340; FBpp0088971; FBgn0014018. [Q94527-1]
EnsemblMetazoa; FBtr0089341; FBpp0088972; FBgn0014018. [Q94527-2]
GeneID; 41087; -.
KEGG; dme:Dmel_CG11992; -.
CTD; 5966; -.
FlyBase; FBgn0014018; Rel.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00500000044765; -.
InParanoid; Q94527; -.
KO; K02580; -.
OMA; HEQMFHL; -.
OrthoDB; EOG091G05R7; -.
PhylomeDB; Q94527; -.
Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
Reactome; R-DME-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-DME-202424; Downstream TCR signaling.
Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
Reactome; R-DME-209560; NF-kB is activated and signals survival.
Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
Reactome; R-DME-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-DME-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-9020702; Interleukin-1 signaling.
Reactome; R-DME-933542; TRAF6 mediated NF-kB activation.
SignaLink; Q94527; -.
GenomeRNAi; 41087; -.
PRO; PR:Q94527; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0014018; -.
Genevisible; Q94527; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0005719; C:nuclear euchromatin; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:FlyBase.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:FlyBase.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006955; P:immune response; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; IDA:FlyBase.
GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
GO; GO:0006967; P:positive regulation of antifungal peptide biosynthetic process; IMP:FlyBase.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:FlyBase.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0045088; P:regulation of innate immune response; IMP:FlyBase.
GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:FlyBase.
GO; GO:0008063; P:Toll signaling pathway; TAS:FlyBase.
CDD; cd00204; ANK; 1.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 2.
Pfam; PF12796; Ank_2; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00248; ANK; 6.
SMART; SM00429; IPT; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; Direct protein sequencing; Immunity; Innate immunity;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 971 Nuclear factor NF-kappa-B p110 subunit.
{ECO:0000269|PubMed:11269501}.
/FTId=PRO_0000030318.
CHAIN 1 545 Nuclear factor NF-kappa-B p68 subunit.
{ECO:0000269|PubMed:11269501}.
/FTId=PRO_0000030319.
CHAIN 546 971 Nuclear factor NF-kappa-B p49 subunit.
{ECO:0000269|PubMed:11269501}.
/FTId=PRO_0000030320.
DOMAIN 147 339 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 640 669 ANK 1. {ECO:0000305}.
REPEAT 673 702 ANK 2. {ECO:0000305}.
REPEAT 710 740 ANK 3. {ECO:0000305}.
REPEAT 745 775 ANK 4. {ECO:0000305}.
REPEAT 783 812 ANK 5. {ECO:0000305}.
MOTIF 452 457 Nuclear localization signal.
{ECO:0000255}.
SITE 545 546 Cleavage (when cotranslationally
processed).
{ECO:0000269|PubMed:11269501}.
MOD_RES 431 431 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 620 620 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 626 626 Phosphotyrosine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 950 950 Phosphoserine.
{ECO:0000250|UniProtKB:P25799}.
VAR_SEQ 1 112 Missing (in isoform Maternal).
{ECO:0000303|PubMed:10619029}.
/FTId=VSP_050089.
VARIANT 82 82 N -> S (in strain: Zim2).
{ECO:0000269|PubMed:10757765}.
VARIANT 110 110 F -> L (in strain: Zim3).
{ECO:0000269|PubMed:10757765}.
VARIANT 699 699 T -> I (in strain: Zim8).
{ECO:0000269|PubMed:10757765}.
VARIANT 845 845 E -> G (in strain: Zim1).
{ECO:0000269|PubMed:10757765}.
VARIANT 862 862 S -> N (in strain: Zim8).
{ECO:0000269|PubMed:10757765}.
MUTAGEN 545 545 D->A: Completely resistant to cleavage.
{ECO:0000269|PubMed:11269502}.
CONFLICT 114 114 Missing (in Ref. 2; AAF07086).
{ECO:0000305}.
SEQUENCE 971 AA; 109775 MW; EAF607357381AD32 CRC64;
MNMNQYYDLD NGKNVMFMND ASSTSGYSSS TSPNSTNRSF SPAHSPKTME LQTDFANLNL
PGGNSPHQPP MANSPYQNQL LNNGGICQLG ATNLINSTGV SFGVANVTSF GNMYMDHQYF
VPAPATVPPS QNFGYHQNGL ASDGDIKHVP QLRIVEQPVE KFRFRYKSEM HGTHGSLNGA
NSKRTPKTFP EVTLCNYDGP AVIRCSLFQT NLDSPHSHQL VVRKDDRDVC DPHDLHVSKE
RGYVAQFINM GIIHTAKKYI FEELCKKKQD RLVFQMNRRE LSHKQLQELH QETEREAKDM
NLNQVRLCFE AFKIEDNGAW VPLAPPVYSN AINNRKSAQT GELRIVRLSK PTGGVMGNDE
LILLVEKVSK KNIKVRFFEE DEDGETVWEA YAKFRESDVH HQYAIVCQTP PYKDKDVDRE
VNVYIELIRP SDDERSFPAL PFRYKPRSVI VSRKRRRTGS SANSSSSGTE SSNNSLDLPK
TLGLAQPPNG LPNLSQHDQT ISEEFGREKH LNEFIASEDF RKLIEHNSSD LEKICQLDMG
ELQHDGHNRA EVPSHRNRTI KCLDDLFEIY KQDRISPIKI SHHKVEKWFI EHALNNYNRD
TLLHEVISHK KDKLKLAIQT IQVMNYFNLK DVVNSTLNAD GDSALHVACQ QDRAHYIRPL
LGMGCNPNLK NNAGNTPLHV AVKEEHLSCV ESFLNGVPTV QLDLSLTNDD GLTPLHMAIR
QNKYDVAKKL ISYDRTSISV ANTMDGNNAL HMAVLEQSVE LLVLILDAQN ENLTDILQAQ
NAAGHTPLEL AERKANDRVV QLLKNVYPEK GELAMTWIPC KVKEEIDSSS DESSDAGQLE
IKSEEMDIET KDEDSVELDL SSGPRRQKDE SSRDTEMDNN KLQLLLKNKF IYDRLCSLLN
QPLGHGSDPQ DRKWMQLARQ THLKQFAFIW LGAEDLLDHV KRKGASVEFS TFARALQAVD
PQAYALLVNP T


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