M3KE1_ARATH
ID M3KE1_ARATH Reviewed; 1368 AA.
AC Q9LJD8; O81809;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=MAP3K epsilon protein kinase 1 {ECO:0000303|PubMed:11489177};
DE Short=AtM3KE1 {ECO:0000303|PubMed:11489177};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A0A078CGE6};
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7 {ECO:0000305};
GN Name=M3KE1 {ECO:0000303|PubMed:11489177}; Synonyms=MAPKKK7 {ECO:0000305};
GN OrderedLocusNames=At3g13530 {ECO:0000312|Araport:AT3G13530};
GN ORFNames=MRP15.19 {ECO:0000312|EMBL:BAB01760.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REVIEW.
RX AGRICOLA=IND22077984; DOI=10.1016/S0065-2296(00)32028-6;
RA Jouannic S., Leprince A.S., Hamal A., Kreis M., Henry Y.;
RT "Plant mitogen-activated protein kinase signalling pathways in the
RT limelight.";
RL Adv. Bot. Res. 32:299-354(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11489177; DOI=10.1046/j.1365-313x.2001.01065.x;
RA Jouannic S., Champion A., Segui-Simarro J.-M., Salimova E., Picaud A.,
RA Tregear J., Testillano P., Risueno M.-C., Simanis V., Kreis M., Henry Y.;
RT "The protein kinases AtMAP3Kepsilon1 and BnMAP3Kepsilon1 are functional
RT homologues of S. pombe cdc7p and may be involved in cell division.";
RL Plant J. 26:637-649(2001).
RN [5]
RP GENE FAMILY, AND 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 [6]
RP REVIEW.
RX PubMed=14740254; DOI=10.1007/s10142-003-0096-4;
RA Champion A., Kreis M., Mockaitis K., Picaud A., Henry Y.;
RT "Arabidopsis kinome: after the casting.";
RL Funct. Integr. Genomics 4:163-187(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH SGP1.
RC STRAIN=cv. Columbia;
RX PubMed=15292395; DOI=10.1242/jcs.01200;
RA Champion A., Jouannic S., Guillon S., Mockaitis K., Krapp A., Picaud A.,
RA Simanis V., Kreis M., Henry Y.;
RT "AtSGP1, AtSGP2 and MAP4K alpha are nucleolar plant proteins that can
RT complement fission yeast mutants lacking a functional SIN pathway.";
RL J. Cell Sci. 117:4265-4275(2004).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16965555; DOI=10.1111/j.1365-313x.2006.02863.x;
RA Chaiwongsar S., Otegui M.S., Jester P.J., Monson S.S., Krysan P.J.;
RT "The protein kinase genes MAP3K epsilon 1 and MAP3K epsilon 2 are required
RT for pollen viability in Arabidopsis thaliana.";
RL Plant J. 48:193-205(2006).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=19123141; DOI=10.1387/ijdb.072488mb;
RA Bedhomme M., Mathieu C., Pulido A., Henry Y., Bergounioux C.;
RT "Arabidopsis monomeric G-proteins, markers of early and late events in cell
RT differentiation.";
RL Int. J. Dev. Biol. 53:177-185(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23087695; DOI=10.3389/fpls.2012.00228;
RA Chaiwongsar S., Strohm A.K., Su S.-H., Krysan P.J.;
RT "Genetic analysis of the Arabidopsis protein kinases MAP3Kepsilon1 and
RT MAP3Kepsilon2 indicates roles in cell expansion and embryo development.";
RL Front. Plant Sci. 3:1-10(2012).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the spatial and
CC temporal control system organizing cortical activities in mitotic and
CC postmitotic cells (PubMed:11489177, PubMed:15292395). Required for the
CC normal functioning of the plasma membrane in developing pollen
CC (PubMed:16965555). Involved in the regulation of cell expansion, cell
CC elongation, and embryo development (PubMed:23087695).
CC {ECO:0000269|PubMed:11489177, ECO:0000269|PubMed:15292395,
CC ECO:0000269|PubMed:16965555, ECO:0000269|PubMed:23087695}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:A0A078CGE6};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A078CGE6};
CC -!- SUBUNIT: Interacts with SGP1. {ECO:0000269|PubMed:15292395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:15292395}. Cell membrane
CC {ECO:0000269|PubMed:16965555}. Note=Accumulates in the nucleolus during
CC interphase (PubMed:15292395). Localized to the plasma membrane in
CC developing pollen grains (PubMed:16965555).
CC {ECO:0000269|PubMed:15292395, ECO:0000269|PubMed:16965555}.
CC -!- TISSUE SPECIFICITY: Expressed in both the sporophytic and the
CC gametophytic tissues, especially in dividing cells. Mostly present in
CC flower buds and mature flowers. Accumulates also in embryos, in roots
CC apices, trichomes and ovule integuments. {ECO:0000269|PubMed:11489177,
CC ECO:0000269|PubMed:15292395, ECO:0000269|PubMed:19123141,
CC ECO:0000269|PubMed:23087695}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryo development.
CC {ECO:0000269|PubMed:23087695}.
CC -!- INDUCTION: Expression is cell cycle-regulated, with higher expression
CC in G2-M phases. {ECO:0000269|PubMed:11489177,
CC ECO:0000269|PubMed:15292395}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:A0A078CGE6}.
CC -!- DISRUPTION PHENOTYPE: Pollen lethality in plants lacking both MAP3KE1
CC and MAP3KE2, associated with plasma membrane irregularities following
CC pollen mitosis I (PubMed:16965555). Smaller plants with shorter roots
CC due to reduced cell elongation in roots and reduced cell expansion in
CC rosette leaves, as well as embryos arrest in the early stages of
CC development (PubMed:23087695). {ECO:0000269|PubMed:16965555,
CC ECO:0000269|PubMed:23087695}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ224982; CAA12272.1; -; Genomic_DNA.
DR EMBL; AP000603; BAB01760.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75368.1; -; Genomic_DNA.
DR RefSeq; NP_187962.1; NM_112199.3.
DR AlphaFoldDB; Q9LJD8; -.
DR SMR; Q9LJD8; -.
DR IntAct; Q9LJD8; 3.
DR STRING; 3702.AT3G13530.1; -.
DR iPTMnet; Q9LJD8; -.
DR PaxDb; Q9LJD8; -.
DR PRIDE; Q9LJD8; -.
DR ProteomicsDB; 238815; -.
DR EnsemblPlants; AT3G13530.1; AT3G13530.1; AT3G13530.
DR GeneID; 820555; -.
DR Gramene; AT3G13530.1; AT3G13530.1; AT3G13530.
DR KEGG; ath:AT3G13530; -.
DR Araport; AT3G13530; -.
DR TAIR; locus:2092890; AT3G13530.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_0_1_1; -.
DR InParanoid; Q9LJD8; -.
DR OMA; NIARDKY; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q9LJD8; -.
DR PRO; PR:Q9LJD8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJD8; baseline and differential.
DR Genevisible; Q9LJD8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IDA:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0061387; P:regulation of extent of cell growth; IMP:UniProtKB.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
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; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1368
FT /note="MAP3K epsilon protein kinase 1"
FT /id="PRO_0000432224"
FT DOMAIN 20..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 25..62
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 86..125
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 218..256
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 533..571
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 628..653
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 654..695
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 699..737
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 750..788
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 903..940
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1025..1063
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1067..1105
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1112..1150
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1154..1191
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1196..1234
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1258..1281
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1282..1318
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1348..1368
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REGION 296..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 88
FT /note="T -> H (in Ref. 1; CAA12272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1368 AA; 151177 MW; 675BAB2ABA8A1BE0 CRC64;
MARQMTSSQF HKSKTLDNKY MLGDEIGKGA YGRVYKGLDL ENGDFVAIKQ VSLENIVQED
LNTIMQEIDL LKNLNHKNIV KYLGSSKTKT HLHIILEYVE NGSLANIIKP NKFGPFPESL
VAVYIAQVLE GLVYLHEQGV IHRDIKGANI LTTKEGLVKL ADFGVATKLN EADVNTHSVV
GTPYWMAPEV IEMSGVCAAS DIWSVGCTVI ELLTCVPPYY DLQPMPALFR IVQDDNPPIP
DSLSPDITDF LRQCFKKDSR QRPDAKTLLS HPWIRNSRRA LQSSLRHSGT IKYMKEATAS
SEKDDEGSQD AAESLSGENV GISKTDSKSK LPLVGVSSFR SEKDQSTPSD LGEEGTDNSE
DDIMSDQVPT LSIHEKSSDA KGTPQDVSDF HGKSERGETP ENLVTETSEA RKNTSAIKHV
GKELSIPVDQ TSHSFGRKGE ERGIRKAVKT PSSVSGNELA RFSDPPGDAS LHDLFHPLDK
VSEGKPNEAS TSMPTSNVNQ GDSPVADGGK NDLATKLRAT IAQKQMEGET GHSNDGGDLF
RLMMGVLKDD VIDIDGLVFD EKVPAENLFP LQAVEFSRLV SSLRPDESED AIVSSCQKLV
AMFRQRPEQK VVFVTQHGFL PLMDLLDIPK SRVICAVLQL INEIIKDNTD FQENACLVGL
IPVVMSFAGP ERDRSREIRK EAAYFLQQLC QSSPLTLQMF IACRGIPVLV GFLEADYAKY
REMVHLAIDG MWQVFKLKRS TPRNDFCRIA AKNGILLRLI NTLYSLNEAT RLASISGGLD
GQAPRVRSGQ LDPNNPIFGQ NETSSLSMID QPDVLKTRHG GGEEPSHAST SNSQRSDVHQ
PDALHPDGDK PRVSSVAPDA STSGTEDVRQ QHRISLSANR TSTDKLQKLA EGASNGFPVT
QTEQVRPLLS LLDKEPPSRH YSGQLDYVKH ITGIERHESR LPLLHGSNEK KNNGDLDFLM
AEFAEVSGRG KENGSLDTTT RYPSKTMTKK VLAIEGVAST SGIASQTASG VLSGSGVLNA
RPGSATSSGL LAHMVSTLSA DVAREYLEKV ADLLLEFARA DTTVKSYMCS QSLLSRLFQM
FNRVEPPILL KILECTNHLS TDPNCLENLQ RADAIKHLIP NLELKDGHLV YQIHHEVLSA
LFNLCKINKR RQEQAAENGI IPHLMLFIMS DSPLKQYALP LLCDMAHASR NSREQLRAHG
GLDVYLSLLD DEYWSVIALD SIAVCLAQDN DNRKVEQALL KQDAIQKLVD FFQSCPERHF
VHILEPFLKI ITKSYRINKT LAVNGLTPLL ISRLDHQDAI ARLNLLKLIK AVYEHHPRPK
QLIVENDLPQ KLQNLIEERR DGQRSGGQVL VKQMATSLLK ALHINTIL
