NFKB1_DROME
ID NFKB1_DROME Reviewed; 971 AA.
AC Q94527; A4V2K3; Q9U435; Q9U436; Q9U437; Q9U438; Q9U439; Q9U440; Q9U6H3;
AC Q9U6H4; Q9U6H5; Q9VHI0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Nuclear factor NF-kappa-B p110 subunit;
DE AltName: Full=Rel-p110;
DE AltName: Full=Relish protein;
DE Contains:
DE RecName: Full=Nuclear factor NF-kappa-B p68 subunit;
DE AltName: Full=Rel-p68;
DE Contains:
DE RecName: Full=Nuclear factor NF-kappa-B p49 subunit;
DE AltName: Full=Rel-p49;
GN Name=Rel {ECO:0000312|FlyBase:FBgn0014018};
GN ORFNames=CG11992 {ECO:0000312|FlyBase:FBgn0014018};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL13493.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAJOR), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=8816802; DOI=10.1073/pnas.93.19.10343;
RA Dushay M.S., Asling B., Hultmark D.;
RT "Origins of immunity: Relish, a compound Rel-like gene in the antibacterial
RT defense of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10343-10347(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS MAJOR AND MATERNAL), FUNCTION,
RP AND INDUCTION.
RX PubMed=10619029; DOI=10.1016/s1097-2765(00)80392-5;
RA Hedengren M., Asling B., Dushay M.S., Ando I., Ekengren S., Wihlborg M.,
RA Hultmark D.;
RT "Relish, a central factor in the control of humoral, but not cellular
RT immunity in Drosophila.";
RL Mol. Cell 4:827-837(1999).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MAJOR).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-880, AND VARIANTS SER-82; LEU-110;
RP ILE-699; GLY-845 AND ASN-862.
RC STRAIN=Zim1 {ECO:0000269|PubMed:10757765},
RC Zim2 {ECO:0000269|PubMed:10757765}, Zim3 {ECO:0000269|PubMed:10757765},
RC Zim5 {ECO:0000269|PubMed:10757765}, Zim7 {ECO:0000269|PubMed:10757765}, and
RC Zim8 {ECO:0000269|PubMed:10757765};
RX PubMed=10757765; DOI=10.1093/genetics/154.3.1231;
RA Begun D.J., Whitley P.;
RT "Adaptive evolution of relish, a Drosophila NF-kappaB/IkappaB protein.";
RL Genetics 154:1231-1238(2000).
RN [7] {ECO:0000305}
RP PROTEIN SEQUENCE OF 546-553, FUNCTION, PROTEOLYTIC CLEAVAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11269501; DOI=10.1093/embo-reports/kvd072;
RA Stoeven S., Ando I., Kadalayil L., Engstrom Y., Hultmark D.;
RT "Activation of the Drosophila NF-kappaB factor Relish by rapid
RT endoproteolytic cleavage.";
RL EMBO Rep. 1:347-352(2000).
RN [8] {ECO:0000305}
RP DEVELOPMENTAL STAGE, INTERACTION WITH DREDD, AND MUTAGENESIS OF ASP-545.
RX PubMed=11269502; DOI=10.1093/embo-reports/kvd073;
RA Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.;
RT "The Drosophila caspase Dredd is required to resist Gram-negative bacterial
RT infection.";
RL EMBO Rep. 1:353-358(2000).
RN [9] {ECO:0000305}
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11018014; DOI=10.1101/gad.817800;
RA Silverman N., Zhou R., Stoeven S., Pandey N., Hultmark D., Maniatis T.;
RT "A Drosophila IkappaB kinase complex required for Relish cleavage and
RT antibacterial immunity.";
RL Genes Dev. 14:2461-2471(2000).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=11872802; DOI=10.1126/science.1070216;
RA Choe K.-M., Werner T., Stoeven S., Hultmark D., Anderson K.V.;
RT "Requirement for a peptidoglycan recognition protein (PGRP) in Relish
RT activation and antibacterial immune responses in Drosophila.";
RL Science 296:359-362(2002).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18000549; DOI=10.1371/journal.pone.0001178;
RA Ayyar S., Pistillo D., Calleja M., Brookfield A., Gittins K., Goldstone C.,
RA Simpson P.;
RT "NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila.";
RL PLoS ONE 2:E1178-E1178(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620 AND TYR-626, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
RA Akhouayri I., Turc C., Royet J., Charroux B.;
RT "Toll-8/Tollo negatively regulates antimicrobial response in the Drosophila
RT respiratory epithelium.";
RL PLoS Pathog. 7:E1002319-E1002319(2011).
RN [14]
RP INTERACTION WITH AKIRIN.
RX PubMed=25180232; DOI=10.15252/embj.201488456;
RA Bonnay F., Nguyen X.H., Cohen-Berros E., Troxler L., Batsche E.,
RA Camonis J., Takeuchi O., Reichhart J.M., Matt N.;
RT "Akirin specifies NF-kappaB selectivity of Drosophila innate immune
RT response via chromatin remodeling.";
RL EMBO J. 33:2349-2362(2014).
RN [15]
RP INTERACTION WITH DMAP1.
RX PubMed=24947515; DOI=10.1074/jbc.c114.553719;
RA Goto A., Fukuyama H., Imler J.L., Hoffmann J.A.;
RT "The chromatin regulator DMAP1 modulates activity of the nuclear factor B
RT (NF-B) transcription factor Relish in the Drosophila innate immune
RT response.";
RL J. Biol. Chem. 289:20470-20476(2014).
RN [16]
RP FUNCTION.
RX PubMed=25477468; DOI=10.1126/science.1258236;
RA Meyer S.N., Amoyel M., Bergantinos C., de la Cova C., Schertel C.,
RA Basler K., Johnston L.A.;
RT "An ancient defense system eliminates unfit cells from developing tissues
RT during cell competition.";
RL Science 346:1258236-1258236(2014).
RN [17]
RP FUNCTION.
RX PubMed=29934091; DOI=10.1016/j.chom.2018.05.022;
RA Liu Y., Gordesky-Gold B., Leney-Greene M., Weinbren N.L., Tudor M.,
RA Cherry S.;
RT "Inflammation-induced, STING-dependent autophagy restricts Zika virus
RT infection in the Drosophila brain.";
RL Cell Host Microbe 24:57-68(2018).
RN [18]
RP FUNCTION.
RX PubMed=29924997; DOI=10.1016/j.celrep.2018.05.029;
RA Martin M., Hiroyasu A., Guzman R.M., Roberts S.A., Goodman A.G.;
RT "Analysis of Drosophila STING reveals an evolutionarily conserved
RT antimicrobial function.";
RL Cell Rep. 23:3537-3550(2018).
RN [19]
RP FUNCTION.
RX PubMed=30119996; DOI=10.1016/j.immuni.2018.07.013;
RA Goto A., Okado K., Martins N., Cai H., Barbier V., Lamiable O., Troxler L.,
RA Santiago E., Kuhn L., Paik D., Silverman N., Holleufer A., Hartmann R.,
RA Liu J., Peng T., Hoffmann J.A., Meignin C., Daeffler L., Imler J.L.;
RT "The kinase IKKbeta regulates a STING- and NF-kappaB-dependent antiviral
RT response pathway in Drosophila.";
RL Immunity 49:225-234(2018).
RN [20]
RP FUNCTION.
RX PubMed=33262294; DOI=10.1126/scisignal.abc4537;
RA Cai H., Holleufer A., Simonsen B., Schneider J., Lemoine A., Gad H.H.,
RA Huang J., Huang J., Chen D., Peng T., Marques J.T., Hartmann R.,
RA Martins N.E., Imler J.L.;
RT "2'3'-cGAMP triggers a STING- and NF-kappaB-dependent broad antiviral
RT response in Drosophila.";
RL Sci. Signal. 13:0-0(2020).
RN [21]
RP FUNCTION.
RX PubMed=34261127; DOI=10.1038/s41586-021-03743-5;
RA Slavik K.M., Morehouse B.R., Ragucci A.E., Zhou W., Ai X., Chen Y., Li L.,
RA Wei Z., Baehre H., Koenig M., Seifert R., Lee A.S.Y., Cai H., Imler J.L.,
RA Kranzusch P.J.;
RT "cGAS-like receptors sense RNA and control 3'2'-cGAMP signaling in
RT Drosophila.";
RL Nature 597:109-113(2021).
RN [22]
RP FUNCTION.
RX PubMed=34261128; DOI=10.1038/s41586-021-03800-z;
RA Holleufer A., Winther K.G., Gad H.H., Ai X., Chen Y., Li L., Wei Z.,
RA Deng H., Liu J., Frederiksen N.A., Simonsen B., Andersen L.L.,
RA Kleigrewe K., Dalskov L., Pichlmair A., Cai H., Imler J.L., Hartmann R.;
RT "Two cGAS-like receptors induce antiviral immunity in Drosophila.";
RL Nature 597:114-118(2021).
CC -!- FUNCTION: Transcription factor that plays a key role in the humoral
CC immune response as part of the peptidoglycan recognition protein (IMD)
CC signaling pathway (PubMed:10619029, PubMed:8816802, PubMed:11269501,
CC PubMed:11872802, PubMed:22022271, PubMed:29924997). Rel-p68 subunit
CC translocates to the nucleus where it binds to the promoter of the
CC Cecropin A1 gene and probably other antimicrobial peptide genes
CC (PubMed:11269501, PubMed:29924997). I-kappa-B kinase complex (IKKbeta
CC and key) and PGRP-LC are essential signaling components in transmitting
CC the lipopolysaccharide (LPS) signal leading to cact degradation for NF-
CC kappa-B (rel) activation (PubMed:11018014, PubMed:11872802). Part of a
CC Toll-related receptor pathway that functions in the apoptosis of unfit
CC cells during cell competition (PubMed:25477468). Also part of some
CC antiviral immunity: activated downstream of Sting signaling, which
CC detects double-stranded RNA (dsRNA) from viruses, and promotes
CC expression of antiviral effector genes (PubMed:29934091,
CC PubMed:30119996, PubMed:33262294, PubMed:34261127, PubMed:34261128).
CC May be part of a NF-kappa-B and Tollo signaling cascade that regulates
CC development of the peripheral nervous system (PubMed:18000549).
CC Possibly post-transcriptionally regulates the neuron-specific genes sc
CC and ase, by promoting the rapid turnover of their transcripts in the
CC wing imaginal disk (PubMed:18000549). {ECO:0000269|PubMed:10619029,
CC ECO:0000269|PubMed:11018014, ECO:0000269|PubMed:11269501,
CC ECO:0000269|PubMed:11872802, ECO:0000269|PubMed:18000549,
CC ECO:0000269|PubMed:22022271, ECO:0000269|PubMed:25477468,
CC ECO:0000269|PubMed:29924997, ECO:0000269|PubMed:29934091,
CC ECO:0000269|PubMed:30119996, ECO:0000269|PubMed:33262294,
CC ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128,
CC ECO:0000269|PubMed:8816802}.
CC -!- SUBUNIT: Rel-p68 subunit interacts with Dredd (PubMed:11269502).
CC Interacts with DMAP1 (PubMed:24947515). Interacts with akirin;
CC interaction is immune stimulation-dependent; activates selected rel
CC target gene promoters (PubMed:25180232). {ECO:0000269|PubMed:11269502,
CC ECO:0000269|PubMed:24947515, ECO:0000269|PubMed:25180232}.
CC -!- INTERACTION:
CC Q94527; Q9VS59: akirin; NbExp=4; IntAct=EBI-869024, EBI-96644;
CC Q94527; Q7YU81: chn; NbExp=3; IntAct=EBI-869024, EBI-164494;
CC Q94527; P98149: Dif; NbExp=3; IntAct=EBI-869024, EBI-188843;
CC Q94527; P13002: grh; NbExp=3; IntAct=EBI-869024, EBI-497032;
CC Q94527; Q9VDZ3: sqz; NbExp=3; IntAct=EBI-869024, EBI-2565022;
CC Q94527-1; P98149: Dif; NbExp=2; IntAct=EBI-15786027, EBI-188843;
CC Q94527-1; P15330: dl; NbExp=2; IntAct=EBI-15786027, EBI-198375;
CC Q94527-1; Q9VEZ5: IKKbeta; NbExp=2; IntAct=EBI-15786027, EBI-148871;
CC Q94527-1; Q94527-1: Rel; NbExp=2; IntAct=EBI-15786027, EBI-15786027;
CC -!- SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p68 subunit]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p110 subunit]:
CC Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Nuclear factor NF-kappa-B p49 subunit]:
CC Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Major {ECO:0000269|PubMed:10619029}; Synonyms=A
CC {ECO:0000269|PubMed:10619029}, B, C, p110
CC {ECO:0000269|PubMed:10619029};
CC IsoId=Q94527-1; Sequence=Displayed;
CC Name=Maternal {ECO:0000269|PubMed:10619029}; Synonyms=D
CC {ECO:0000269|PubMed:10619029}, p100 {ECO:0000269|PubMed:10619029};
CC IsoId=Q94527-2; Sequence=VSP_050089;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11269502, ECO:0000269|PubMed:8816802}.
CC -!- INDUCTION: By bacteria and fungi. {ECO:0000269|PubMed:10619029}.
CC -!- PTM: Phosphorylated by lipopolysaccharide (LPS)-activated I-kappa-B
CC kinase complex before being cleaved. Rel-p110 subunit is cleaved within
CC seconds of an immune challenge into Rel-p49 subunit and Rel-p68
CC subunit. Rel-p110 subunit reappears after 45 minutes.
CC {ECO:0000269|PubMed:11018014, ECO:0000269|PubMed:11269501,
CC ECO:0000269|PubMed:18327897}.
CC -!- DISRUPTION PHENOTYPE: Larvae infected with Gram-negative bacteria fail
CC to activate tracheal expression of the antibacterial peptide gene Drs
CC (PubMed:22022271). Ectopic bristles develop on the dorsocentral,
CC scutellar and lateral regions of the noctum, with one or more ectopic
CC bristles per hemi-notum (PubMed:18000549).
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DR EMBL; U62005; AAB17264.1; -; mRNA.
DR EMBL; AF186073; AAF07931.1; -; Genomic_DNA.
DR EMBL; AF186073; AAF07932.1; -; Genomic_DNA.
DR EMBL; AF186077; AAF07086.1; -; Genomic_DNA.
DR EMBL; AF186078; AAF07087.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF54333.2; -; Genomic_DNA.
DR EMBL; AE014297; AAS65130.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65131.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65132.1; -; Genomic_DNA.
DR EMBL; AY058264; AAL13493.1; -; mRNA.
DR EMBL; AF204284; AAF20132.1; -; Genomic_DNA.
DR EMBL; AF204285; AAF20133.1; -; Genomic_DNA.
DR EMBL; AF204286; AAF20134.1; -; Genomic_DNA.
DR EMBL; AF204287; AAF20135.1; -; Genomic_DNA.
DR EMBL; AF204288; AAF20136.1; -; Genomic_DNA.
DR EMBL; AF204289; AAF20137.1; -; Genomic_DNA.
DR RefSeq; NP_477094.1; NM_057746.4. [Q94527-1]
DR RefSeq; NP_996187.1; NM_206465.1. [Q94527-2]
DR RefSeq; NP_996188.1; NM_206466.1. [Q94527-1]
DR RefSeq; NP_996189.1; NM_206467.1. [Q94527-1]
DR AlphaFoldDB; Q94527; -.
DR SMR; Q94527; -.
DR BioGRID; 66255; 259.
DR DIP; DIP-60434N; -.
DR IntAct; Q94527; 137.
DR MINT; Q94527; -.
DR STRING; 7227.FBpp0088375; -.
DR iPTMnet; Q94527; -.
DR PaxDb; Q94527; -.
DR PRIDE; Q94527; -.
DR DNASU; 41087; -.
DR EnsemblMetazoa; FBtr0089338; FBpp0088375; FBgn0014018. [Q94527-1]
DR EnsemblMetazoa; FBtr0089339; FBpp0088973; FBgn0014018. [Q94527-1]
DR EnsemblMetazoa; FBtr0089340; FBpp0088971; FBgn0014018. [Q94527-1]
DR EnsemblMetazoa; FBtr0089341; FBpp0088972; FBgn0014018. [Q94527-2]
DR GeneID; 41087; -.
DR KEGG; dme:Dmel_CG11992; -.
DR CTD; 5966; -.
DR FlyBase; FBgn0014018; Rel.
DR VEuPathDB; VectorBase:FBgn0014018; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000164992; -.
DR InParanoid; Q94527; -.
DR OMA; MTWIPRK; -.
DR PhylomeDB; Q94527; -.
DR Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-DME-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-DME-202424; Downstream TCR signaling.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-209560; NF-kB is activated and signals survival.
DR Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
DR Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-DME-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-DME-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9020702; Interleukin-1 signaling.
DR Reactome; R-DME-933542; TRAF6 mediated NF-kB activation.
DR SignaLink; Q94527; -.
DR BioGRID-ORCS; 41087; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41087; -.
DR PRO; PR:Q94527; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0014018; Expressed in embryonic/larval hemocyte (Drosophila) and 47 other tissues.
DR ExpressionAtlas; Q94527; baseline and differential.
DR Genevisible; Q94527; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:FlyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006955; P:immune response; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0006967; P:positive regulation of antifungal peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:FlyBase.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:FlyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR24169; PTHR24169; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ANK repeat; Antiviral defense; Cytoplasm;
KW Direct protein sequencing; Immunity; Innate immunity; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..971
FT /note="Nuclear factor NF-kappa-B p110 subunit"
FT /evidence="ECO:0000269|PubMed:11269501"
FT /id="PRO_0000030318"
FT CHAIN 1..545
FT /note="Nuclear factor NF-kappa-B p68 subunit"
FT /evidence="ECO:0000269|PubMed:11269501"
FT /id="PRO_0000030319"
FT CHAIN 546..971
FT /note="Nuclear factor NF-kappa-B p49 subunit"
FT /evidence="ECO:0000269|PubMed:11269501"
FT /id="PRO_0000030320"
FT DOMAIN 147..339
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REPEAT 640..669
FT /note="ANK 1"
FT /evidence="ECO:0000305"
FT REPEAT 673..702
FT /note="ANK 2"
FT /evidence="ECO:0000305"
FT REPEAT 710..740
FT /note="ANK 3"
FT /evidence="ECO:0000305"
FT REPEAT 745..775
FT /note="ANK 4"
FT /evidence="ECO:0000305"
FT REPEAT 783..812
FT /note="ANK 5"
FT /evidence="ECO:0000305"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 452..457
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 455..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 545..546
FT /note="Cleavage (when cotranslationally processed)"
FT /evidence="ECO:0000269|PubMed:11269501"
FT MOD_RES 431
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 620
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 626
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25799"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform Maternal)"
FT /evidence="ECO:0000303|PubMed:10619029"
FT /id="VSP_050089"
FT VARIANT 82
FT /note="N -> S (in strain: Zim2)"
FT /evidence="ECO:0000269|PubMed:10757765"
FT VARIANT 110
FT /note="F -> L (in strain: Zim3)"
FT /evidence="ECO:0000269|PubMed:10757765"
FT VARIANT 699
FT /note="T -> I (in strain: Zim8)"
FT /evidence="ECO:0000269|PubMed:10757765"
FT VARIANT 845
FT /note="E -> G (in strain: Zim1)"
FT /evidence="ECO:0000269|PubMed:10757765"
FT VARIANT 862
FT /note="S -> N (in strain: Zim8)"
FT /evidence="ECO:0000269|PubMed:10757765"
FT MUTAGEN 545
FT /note="D->A: Completely resistant to cleavage."
FT /evidence="ECO:0000269|PubMed:11269502"
FT CONFLICT 114
FT /note="Missing (in Ref. 2; AAF07086)"
FT /evidence="ECO:0000305"
SQ 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
