M3K3_ARATH
ID M3K3_ARATH Reviewed; 651 AA.
AC O22042; Q9SFG7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 3;
DE EC=2.7.11.25;
DE AltName: Full=Arabidopsis NPK1-related protein kinase 3;
GN Name=ANP3; OrderedLocusNames=At3g06030; ORFNames=F24F17.1, F2O10.1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9263451; DOI=10.1046/j.1365-313x.1997.12010039.x;
RA Nishihama R., Banno H., Kawahara E., Irie K., Machida Y.;
RT "Possible involvement of differential splicing in regulation of the
RT activity of Arabidopsis ANP1 that is related to mitogen-activated protein
RT kinase kinase kinases (MAPKKKs).";
RL Plant J. 12:39-48(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-108 AND LYS-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION.
RX PubMed=20215588; DOI=10.1105/tpc.109.071746;
RA Beck M., Komis G., Mueller J., Menzel D., Samaj J.;
RT "Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2 and 3
RT and mitogen-activated protein kinase 4 are essential for microtubule
RT organization.";
RL Plant Cell 22:755-771(2010).
RN [7]
RP INTERACTION WITH NACK2 AND MKK6.
RX PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x;
RA Zeng Q., Chen J.G., Ellis B.E.;
RT "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis.";
RL Plant J. 67:895-906(2011).
CC -!- FUNCTION: Involved in cortical microtubules organization and
CC stabilization by regulating the phosphorylation state of microtubule-
CC associated proteins such as MAP65-1. {ECO:0000269|PubMed:20215588}.
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 -!- SUBUNIT: Interacts with NACK2 and MKK6. {ECO:0000269|PubMed:21575092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:9263451}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB000799; BAA21857.1; -; mRNA.
DR EMBL; AC013454; AAF23214.1; -; Genomic_DNA.
DR EMBL; AC068073; AAF66131.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74332.1; -; Genomic_DNA.
DR EMBL; AY069917; AAL47465.1; -; mRNA.
DR EMBL; BT001024; AAN46778.1; -; mRNA.
DR RefSeq; NP_187254.1; NM_111477.4.
DR AlphaFoldDB; O22042; -.
DR SMR; O22042; -.
DR BioGRID; 5109; 4.
DR IntAct; O22042; 2.
DR STRING; 3702.AT3G06030.1; -.
DR iPTMnet; O22042; -.
DR PaxDb; O22042; -.
DR PRIDE; O22042; -.
DR ProteomicsDB; 250819; -.
DR EnsemblPlants; AT3G06030.1; AT3G06030.1; AT3G06030.
DR GeneID; 819774; -.
DR Gramene; AT3G06030.1; AT3G06030.1; AT3G06030.
DR KEGG; ath:AT3G06030; -.
DR Araport; AT3G06030; -.
DR TAIR; locus:2080394; AT3G06030.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_020952_1_0_1; -.
DR InParanoid; O22042; -.
DR OMA; KSGVPCD; -.
DR OrthoDB; 361120at2759; -.
DR PhylomeDB; O22042; -.
DR PRO; PR:O22042; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22042; baseline and differential.
DR Genevisible; O22042; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
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; HDA:TAIR.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase;
KW Microtubule; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..651
FT /note="Mitogen-activated protein kinase kinase kinase 3"
FT /id="PRO_0000086272"
FT DOMAIN 68..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 573..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..130
FT /evidence="ECO:0000255"
FT COILED 618..641
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 651 AA; 71654 MW; E8FDF683C7E31268 CRC64;
MQDILGSVRR SLVFRSSLAG DDGTSGGGLS GFVGKINSSI RSSRIGLFSK PPPGLPAPRK
EEAPSIRWRK GELIGCGAFG RVYMGMNLDS GELLAIKQVL IAPSSASKEK TQGHIRELEE
EVQLLKNLSH PNIVRYLGTV RESDSLNILM EFVPGGSISS LLEKFGSFPE PVIIMYTKQL
LLGLEYLHNN GIMHRDIKGA NILVDNKGCI RLADFGASKK VVELATVNGA KSMKGTPYWM
APEVILQTGH SFSADIWSVG CTVIEMATGK PPWSEQYQQF AAVLHIGRTK AHPPIPEDLS
PEAKDFLMKC LHKEPSLRLS ATELLQHPFV TGKRQEPYPA YRNSLTECGN PITTQGMNVR
SSINSLIRRS TCSGLKDVCE LGSLRSSIIY PQKSNNSGFG WRDGDSDDLC QTDMDDLCNI
ESVRNNVLSQ STDLNKSFNP MCDSTDNWSC KFDESPKVMK SKSNLLSYQA SQLQTGVPCD
EETSLTFAGG SSVAEDDYKG TELKIKSFLD EKAQDLKRLQ TPLLEEFHNA MNPGIPQGAL
GDTNIYNLPN LPSISKTPKR LPSRRLSAIS DAMPSPLKSS KRTLNTSRVM QSGTEPTQVN
ESTKKGVNNS RCFSEIRRKW EEELYEELER HRENLRHAGA GGKTPLSGHK G
