M3K7_DROME
ID M3K7_DROME Reviewed; 678 AA.
AC Q9V3Q6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 7;
DE EC=2.7.11.25;
DE AltName: Full=TGF-beta-activated kinase 1;
DE AltName: Full=dTAK1;
GN Name=Tak1; ORFNames=CG18492;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Ovary;
RX PubMed=10757786; DOI=10.1128/mcb.20.9.3015-3026.2000;
RA Takatsu Y., Nakamura M., Stapleton M., Danos M.C., Matsumoto K.,
RA O'Connor M.B., Shibuya H., Ueno N.;
RT "TAK1 participates in c-Jun N-terminal kinase signaling during Drosophila
RT development.";
RL Mol. Cell. Biol. 20:3015-3026(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP FUNCTION.
RX PubMed=14519762; DOI=10.1074/jbc.m304802200;
RA Silverman N., Zhou R., Erlich R.L., Hunter M., Bernstein E., Schneider D.,
RA Maniatis T.;
RT "Immune activation of NF-kappaB and JNK requires Drosophila TAK1.";
RL J. Biol. Chem. 278:48928-48934(2003).
RN [6]
RP FUNCTION.
RX PubMed=15037551; DOI=10.1101/gad.1168104;
RA Park J.M., Brady H., Ruocco M.G., Sun H., Williams D., Lee S.J.,
RA Kato T. Jr., Richards N., Chan K., Mercurio F., Karin M., Wasserman S.A.;
RT "Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK-
RT mediated immune response in Drosophila.";
RL Genes Dev. 18:584-594(2004).
CC -!- FUNCTION: Component of a protein kinase signal transduction cascade.
CC Mediator of TGF-beta signal transduction. Responsible for activation of
CC the JNK MAPK pathway (basket, bsk and hemipterous, hep) in response to
CC LPS. Component of the NF-kappa-B pathway; relish-mediated JNK
CC inhibition involves proteasomal degradation of Tak1; certain targets of
CC Relish that are induced during immune responses may facilitate
CC destruction of Tak1 and switch off the JNK cascade. Participates in
CC diverse roles such as control of cell shape and regulation of
CC apoptosis. {ECO:0000269|PubMed:10757786, ECO:0000269|PubMed:14519762,
CC ECO:0000269|PubMed:15037551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AF199466; AAF06815.1; -; mRNA.
DR EMBL; AE014298; AAF50895.1; -; Genomic_DNA.
DR EMBL; AY051953; AAK93377.1; -; mRNA.
DR RefSeq; NP_524080.1; NM_079356.3.
DR AlphaFoldDB; Q9V3Q6; -.
DR SMR; Q9V3Q6; -.
DR BioGRID; 64981; 156.
DR STRING; 7227.FBpp0077011; -.
DR PaxDb; Q9V3Q6; -.
DR PRIDE; Q9V3Q6; -.
DR EnsemblMetazoa; FBtr0077319; FBpp0077011; FBgn0026323.
DR GeneID; 39659; -.
DR KEGG; dme:Dmel_CG18492; -.
DR CTD; 39659; -.
DR FlyBase; FBgn0026323; Tak1.
DR VEuPathDB; VectorBase:FBgn0026323; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000160233; -.
DR HOGENOM; CLU_000288_7_41_1; -.
DR InParanoid; Q9V3Q6; -.
DR OMA; NNPLFHM; -.
DR OrthoDB; 635654at2759; -.
DR PhylomeDB; Q9V3Q6; -.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
DR SignaLink; Q9V3Q6; -.
DR BioGRID-ORCS; 39659; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39659; -.
DR PRO; PR:Q9V3Q6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026323; Expressed in oviduct (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q9V3Q6; baseline and differential.
DR Genevisible; Q9V3Q6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IMP:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IMP:FlyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IGI:FlyBase.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; 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:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007254; P:JNK cascade; IGI:FlyBase.
DR GO; GO:0048802; P:notum morphogenesis; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; 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; TAS:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IGI:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017421; MAPKKK7.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46716; PTHR46716; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Immunity; Innate immunity; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..678
FT /note="Mitogen-activated protein kinase kinase kinase 7"
FT /id="PRO_0000086254"
FT DOMAIN 19..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 678 AA; 75675 MW; 87EBA80CDB8CDE45 CRC64;
MATASLDALQ AAYVDFSEIT LREKVGHGSY GVVCKAVWRD KLVAVKEFFA SAEQKDIEKE
VKQLSRVKHP NIIALHGISS YQQATYLIME FAEGGSLHNF LHGKVKPAYS LAHAMSWARQ
CAEGLAYLHA MTPKPLIHRD VKPLNLLLTN KGRNLKICDF GTVADKSTMM TNNRGSAAWM
APEVFEGSKY TEKCDIFSWA IVLWEVLSRK QPFKGIDNAY TIQWKIYKGE RPPLLTTCPK
RIEDLMTACW KTVPEDRPSM QYIVGVMHEI VKDYTGADKA LEYTFVNQQI VTKESDGTVA
AQPDSLSSQE GELSPSSTQL TPTTAANANV NAIAISKTTT SSMTENTSST SSDITPTNSG
QLDNNPLFYM VTNRWDAIPE EESNESRNDS FNLTSSAEAT QRLETIRNGM ILMACKPMEQ
LTLDVEANGF DLSPSESSSS STNAKSDGRE RLTVTDTKPV MMTTDLSNNN GGIHAHSNGL
LSHANGWQAR DEELQEQEHE QEIVNSLDVD VDPDEDENDG TEQSLAEILD PELQPEPPIP
NDAESQLIYR DHRHMAKEYL SVDTNLYYAQ DFKDKLIVQM DRTEREQKQE LLRKMKDKEG
LQSLYNNLQQ QYASRQLAAG HHPQPHPHPH PNQLQHPHSH PPMHFLQDEG CGLLPGSVCG
GSESVEEGWV VIPPHHNA
