NEMO_DROME
ID NEMO_DROME Reviewed; 387 AA.
AC Q9GYV5; Q9W105;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=NF-kappa-B essential modulator;
DE AltName: Full=Inhibitor of nuclear factor kappa B kinase subunit gamma;
DE Short=DmIKKgamma;
DE AltName: Full=NEMO homolog;
GN Name=key; Synonyms=IKKGAMMA; ORFNames=CG16910;
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:AAF47273.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND INTERACTION WITH IKKBETA.
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 [2] {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 [3] {ECO:0000305}
RP GENOME REANNOTATION.
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {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).
CC -!- FUNCTION: Essential signaling component in transmitting the
CC lipopolysaccharide (LPS) signal leading to cact degradation, which is
CC required for NF-kappa-B (Rel) activation. Required for antibacterial
CC immune response. {ECO:0000269|PubMed:11018014}.
CC -!- SUBUNIT: Interacts with IKKbeta to form the I-kappa-B kinase complex.
CC {ECO:0000269|PubMed:11018014}.
CC -!- INTERACTION:
CC Q9GYV5; Q9VEZ5: IKKbeta; NbExp=3; IntAct=EBI-113108, EBI-148871;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; AF294396; AAG02486.1; -; mRNA.
DR EMBL; AE013599; AAF47273.2; -; Genomic_DNA.
DR EMBL; AY061242; AAL28790.1; -; mRNA.
DR RefSeq; NP_523856.2; NM_079132.4.
DR AlphaFoldDB; Q9GYV5; -.
DR SMR; Q9GYV5; -.
DR BioGRID; 63537; 116.
DR IntAct; Q9GYV5; 2.
DR STRING; 7227.FBpp0296952; -.
DR PaxDb; Q9GYV5; -.
DR PeptideAtlas; Q9GYV5; -.
DR EnsemblMetazoa; FBtr0072428; FBpp0072333; FBgn0041205.
DR GeneID; 37967; -.
DR KEGG; dme:Dmel_CG16910; -.
DR UCSC; CG16910-RA; d. melanogaster.
DR CTD; 37967; -.
DR FlyBase; FBgn0041205; key.
DR VEuPathDB; VectorBase:FBgn0041205; -.
DR eggNOG; ENOG502S6HT; Eukaryota.
DR InParanoid; Q9GYV5; -.
DR PhylomeDB; Q9GYV5; -.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
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 SignaLink; Q9GYV5; -.
DR BioGRID-ORCS; 37967; 0 hits in 3 CRISPR screens.
DR ChiTaRS; key; fly.
DR GenomeRNAi; 37967; -.
DR PRO; PR:Q9GYV5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0041205; Expressed in embryonic/larval hemocyte (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q9GYV5; baseline and differential.
DR Genevisible; Q9GYV5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR InterPro; IPR032419; CC2-LZ_dom.
DR InterPro; IPR034735; NEMO_ZF.
DR Pfam; PF16516; CC2-LZ; 1.
DR PROSITE; PS51801; ZF_CCHC_NOA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..387
FT /note="NF-kappa-B essential modulator"
FT /id="PRO_0000096781"
FT ZN_FING 355..385
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT REGION 302..332
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT REGION 324..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..331
FT /evidence="ECO:0000255"
FT COMPBIAS 324..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT CONFLICT 36
FT /note="E -> K (in Ref. 2; AAF47273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43879 MW; 1D0038A61786091A CRC64;
MSDEESFVIL GSSPCSSLMP DSSLRSDVCG NAQEAEETVA STSTQPPTVN CIPVSITASQ
QQHKSLDSGS SQQQSLATSF IMGEIQSDVL KNSVYSQFPS LCSLQGSAEE VVKLQNMMTE
YLALKSTLDK VNQTMLNYHN LTQQWRQEAA DREHQYKEHV KECQAQIAIL RVENQELKRD
LETKIEQIEG VHTIRLKEQD ELRKSVSEKQ SLIDNMRVEI DKLKQLNHSF EFVPEYATES
KSQELIKKMQ LDINELKARD IQKQEVIKGL QIQNDIYRRD FEMERADREK NAGEKDQYLM
DLRSLQRRNQ ELIEALAESH KASKACSTAS PLSSSRSNLR EEQRPILDPT GASSRTSDTT
LRCPICSKSF NALSVLQSHV NDCLDKN
