MP3K3_ARATH
ID MP3K3_ARATH Reviewed; 560 AA.
AC Q9M0T3; O81473; O82650; Q84W26;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 3 {ECO:0000303|PubMed:12119167};
DE Short=MAP kinase kinase kinase 3 {ECO:0000303|PubMed:12119167};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:P53778, ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=MAP3K beta 3 protein kinase {ECO:0000303|PubMed:10095117};
DE Short=MAP3K beta 3 {ECO:0000303|PubMed:10095117};
DE AltName: Full=MAPK/ERK kinase kinase 3 {ECO:0000303|PubMed:12119167};
DE Short=AtMEKK3 {ECO:0000303|PubMed:12119167};
GN Name=MEKK3 {ECO:0000303|PubMed:12119167};
GN Synonyms=MAP3Kb3 {ECO:0000303|PubMed:10095117}, MAPKKK10;
GN OrderedLocusNames=At4g08470 {ECO:0000312|Araport:AT4G08470};
GN ORFNames=T15F16.2 {ECO:0000312|EMBL:AAC28187.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-560, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10095117; DOI=10.1016/s0378-1119(99)00012-8;
RA Jouannic S., Hamal A., Leprince A.-S., Tregear J.W., Kreis M., Henry Y.;
RT "Characterisation of novel plant genes encoding MEKK/STE11 and RAF-related
RT protein kinases.";
RL Gene 229:171-181(1999).
RN [7]
RP NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20668060; DOI=10.1104/pp.110.159897;
RA Bush S.M., Krysan P.J.;
RT "iTILLING: a personalized approach to the identification of induced
RT mutations in Arabidopsis.";
RL Plant Physiol. 154:25-35(2010).
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 Evidence={ECO:0000250|UniProtKB:P53778};
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; Evidence={ECO:0000250|UniProtKB:P53778};
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, siliques,
CC leaves, seedlings and flower buds. {ECO:0000269|PubMed:10095117}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under standard growth
CC conditions. {ECO:0000269|PubMed:20668060}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF076275; AAC28187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161511; CAB77972.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82648.1; -; Genomic_DNA.
DR EMBL; BT004308; AAO42306.1; -; mRNA.
DR EMBL; BT021102; AAX12872.1; -; mRNA.
DR EMBL; AK228648; BAF00555.1; -; mRNA.
DR EMBL; AJ010092; CAA08996.1; -; mRNA.
DR PIR; D85084; D85084.
DR PIR; T01836; T01836.
DR PIR; T51736; T51736.
DR RefSeq; NP_192587.1; NM_116916.4.
DR AlphaFoldDB; Q9M0T3; -.
DR SMR; Q9M0T3; -.
DR IntAct; Q9M0T3; 3.
DR STRING; 3702.AT4G08470.1; -.
DR PaxDb; Q9M0T3; -.
DR PRIDE; Q9M0T3; -.
DR ProteomicsDB; 239067; -.
DR EnsemblPlants; AT4G08470.1; AT4G08470.1; AT4G08470.
DR GeneID; 826406; -.
DR Gramene; AT4G08470.1; AT4G08470.1; AT4G08470.
DR KEGG; ath:AT4G08470; -.
DR Araport; AT4G08470; -.
DR TAIR; locus:2133529; AT4G08470.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_486950_0_0_1; -.
DR InParanoid; Q9M0T3; -.
DR OrthoDB; 630495at2759; -.
DR PhylomeDB; Q9M0T3; -.
DR PRO; PR:Q9M0T3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0T3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..560
FT /note="Mitogen-activated protein kinase kinase kinase 3"
FT /id="PRO_0000441879"
FT DOMAIN 303..557
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 309..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 60
FT /note="L -> F (in Ref. 6; CAA08996)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> G (in Ref. 6; CAA08996)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> A (in Ref. 3; AAO42306 and 5; BAF00555)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> K (in Ref. 6; CAA08996)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="G -> R (in Ref. 6; CAA08996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 62308 MW; 01975D9911A69547 CRC64;
MDVTAIFAGD ILVQSREYLI PNDVVDVDGG IKAVRPPIIQ PPPGRKLPLI DFPGSSWDFL
TYFAPSKTVK RQSSSSSDNT SDKEEVETEE TRGMFVQLGD TAHEACPFAT NEADSSSTVS
IISPSYASRG SIVPSWLKRK FLGRVSLGFV YEGSSGSSVG SESTCSLMTP SLEFPDRISF
RKKDFSEKGP SRHVWEKRKL TRAKLIENFC NPEDIEPVTS WLKGQLLGEE SFASVYEAIS
DSSVGSESTC SLMTPSMEFP DRISFRKRDF SEEGPSGRVK EKRKLMRNKL IENFRKPEDI
TSWLKGQLLG RGSYASVYEA ISEDGDFFAV KEVSLLDKGI QAQECIQQLE GEIALLSQLQ
HQNIVRYRGT AKDVSKLYIF LELVTQGSVQ KLYERYQLSY TVVSLYTRQI LAGLNYLHDK
GFVHRDIKCA NMLVDANGTV KLADFGLAEA SKFNDIMSCK GTLFWMAPEV INRKDSDGNG
SPADIWSLGC TVLEMCTGQI PYSDLKPIQA AFKIGRGTLP DVPDTLSLDA RHFILTCLKV
NPEERPTAAE LLHHPFVINL
