M3KE2_ARATH
ID M3KE2_ARATH Reviewed; 1367 AA.
AC Q9SFB6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=MAP3K epsilon protein kinase 2 {ECO:0000303|PubMed:12119167};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A0A078CGE6};
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 6 {ECO:0000305};
GN Name=MAP3KE2 {ECO:0000303|PubMed:12119167}; Synonyms=MAPKKK6 {ECO:0000305};
GN OrderedLocusNames=At3g07980 {ECO:0000312|Araport:AT3G07980};
GN ORFNames=F17A17.32 {ECO:0000312|EMBL:AAF21208.1};
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 [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 [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 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 [4]
RP TISSUE SPECIFICITY.
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 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
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:15292395). Required for the normal
CC functioning of the plasma membrane in developing pollen
CC (PubMed:16965555). Involved in the regulation of cell expansion and
CC embryo development (PubMed:23087695). {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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:15292395}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus
CC during interphase (PubMed:15292395). Localized to the plasma membrane
CC in developing pollen grains (By similarity).
CC {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:15292395}.
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 and in
CC roots. {ECO:0000269|PubMed:11489177, ECO:0000269|PubMed:15292395,
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: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; AC013483; AAF21208.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74627.1; -; Genomic_DNA.
DR RefSeq; NP_187455.1; NM_111677.4.
DR AlphaFoldDB; Q9SFB6; -.
DR SMR; Q9SFB6; -.
DR STRING; 3702.AT3G07980.1; -.
DR iPTMnet; Q9SFB6; -.
DR PaxDb; Q9SFB6; -.
DR PRIDE; Q9SFB6; -.
DR EnsemblPlants; AT3G07980.1; AT3G07980.1; AT3G07980.
DR GeneID; 819989; -.
DR Gramene; AT3G07980.1; AT3G07980.1; AT3G07980.
DR KEGG; ath:AT3G07980; -.
DR Araport; AT3G07980; -.
DR TAIR; locus:2077417; AT3G07980.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_1_1_1; -.
DR InParanoid; Q9SFB6; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q9SFB6; -.
DR PRO; PR:Q9SFB6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFB6; baseline and differential.
DR Genevisible; Q9SFB6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA: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; ISS: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; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 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; 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..1367
FT /note="MAP3K epsilon protein kinase 2"
FT /id="PRO_0000432225"
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 538..576
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 577..614
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 633..658
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 659..700
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 704..742
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 850..888
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 906..943
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1045..1066
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1067..1105
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1112..1150
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1154..1191
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1196..1236
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1257..1280
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1281..1317
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1347..1367
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REGION 285..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..847
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"
SQ SEQUENCE 1367 AA; 151137 MW; 7618AFA6B41A227C CRC64;
MARQMTSSQF HKSKTLDNKY MLGDEIGKGA YGRVYIGLDL ENGDFVAIKQ VSLENIGQED
LNTIMQEIDL LKNLNHKNIV KYLGSLKTKT HLHIILEYVE NGSLANIIKP NKFGPFPESL
VTVYIAQVLE GLVYLHEQGV IHRDIKGANI LTTKEGLVKL ADFGVATKLN EADFNTHSVV
GTPYWMAPEV IELSGVCAAS DIWSVGCTII ELLTCVPPYY DLQPMPALYR IVQDDTPPIP
DSLSPDITDF LRLCFKKDSR QRPDAKTLLS HPWIRNSRRA LRSSLRHSGT IRYMKETDSS
SEKDAEGSQE VVESVSAEKV EVTKTNSKSK LPVIGGASFR SEKDQSSPSD LGEEGTDSED
DINSDQGPTL SMHDKSSRQS GTCSISSDAK GTSQDVLENH EKYDRDEIPG NLETEASEGR
RNTLATKLVG KEYSIQSSHS FSQKGEDGLR KAVKTPSSFG GNELTRFSDP PGDASLHDLF
HPLDKVPEGK TNEASTSTPT ANVNQGDSPV ADGGKNDLAT KLRARIAQKQ MEGETGHSQD
GGDLFRLMMG VLKDDVLNID DLVFDEKVPP ENLFPLQAVE FSRLVSSLRP DESEDAIVTS
SLKLVAMFRQ RPGQKAVFVT QNGFLPLMDL LDIPKSRVIC AVLQLINEIV KDNTDFLENA
CLVGLIPLVM SFAGFERDRS REIRKEAAYF LQQLCQSSPL TLQMFISCRG IPVLVGFLEA
DYAKHREMVH LAIDGMWQVF KLKKSTSRND FCRIAAKNGI LLRLVNTLYS LSEATRLASI
SGDALILDGQ TPRARSGQLD PNNPIFSQRE TSPSVIDHPD GLKTRNGGGE EPSHALTSNS
QSSDVHQPDA LHPDGDRPRL SSVVADATED VIQQHRISLS ANRTSTDKLQ KLAEGASNGF
PVTQPDQVRP LLSLLEKEPP SRKISGQLDY VKHIAGIERH ESRLPLLYAS DEKKTNGDLE
FIMAEFAEVS GRGKENGNLD TAPRYSSKTM TKKVMAIERV ASTCGIASQT ASGVLSGSGV
LNARPGSTTS SGLLAHALSA DVSMDYLEKV ADLLLEFARA ETTVKSYMCS QSLLSRLFQM
FNRVEPPILL KILECTNHLS TDPNCLENLQ RADAIKQLIP NLELKEGPLV YQIHHEVLSA
LFNLCKINKR RQEQAAENGI IPHLMLFVMS DSPLKQYALP LLCDMAHASR NSREQLRAHG
GLDVYLSLLD DEYWSVIALD SIAVCLAQDV DQKVEQAFLK KDAIQKLVNF FQNCPERHFV
HILEPFLKII TKSSSINKTL ALNGLTPLLI ARLDHQDAIA RLNLLKLIKA VYEKHPKPKQ
LIVENDLPQK LQNLIEERRD GQRSGGQVLV KQMATSLLKA LHINTIL
