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MAP3K epsilon protein kinase 2 (EC 2.7.11.1) (Mitogen-activated protein kinase kinase kinase 6)

 M3KE2_ARATH             Reviewed;        1367 AA.
Q9SFB6;
04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=MAP3K epsilon protein kinase 2 {ECO:0000303|PubMed:12119167};
EC=2.7.11.1 {ECO:0000250|UniProtKB:A0A078CGE6};
AltName: Full=Mitogen-activated protein kinase kinase kinase 6 {ECO:0000305};
Name=MAP3KE2 {ECO:0000303|PubMed:12119167};
Synonyms=MAPKKK6 {ECO:0000305};
OrderedLocusNames=At3g07980 {ECO:0000312|Araport:AT3G07980};
ORFNames=F17A17.32 {ECO:0000312|EMBL:AAF21208.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12119167; DOI=10.1016/S1360-1385(02)02302-6;
MAPK group;
"Mitogen-activated protein kinase cascades in plants: a new
nomenclature.";
Trends Plant Sci. 7:301-308(2002).
[4]
TISSUE SPECIFICITY.
PubMed=11489177; DOI=10.1046/j.1365-313x.2001.01065.x;
Jouannic S., Champion A., Segui-Simarro J.-M., Salimova E., Picaud A.,
Tregear J., Testillano P., Risueno M.-C., Simanis V., Kreis M.,
Henry Y.;
"The protein kinases AtMAP3Kepsilon1 and BnMAP3Kepsilon1 are
functional homologues of S. pombe cdc7p and may be involved in cell
division.";
Plant J. 26:637-649(2001).
[5]
REVIEW.
PubMed=14740254; DOI=10.1007/s10142-003-0096-4;
Champion A., Kreis M., Mockaitis K., Picaud A., Henry Y.;
"Arabidopsis kinome: after the casting.";
Funct. Integr. Genomics 4:163-187(2004).
[6]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=15292395; DOI=10.1242/jcs.01200;
Champion A., Jouannic S., Guillon S., Mockaitis K., Krapp A.,
Picaud A., Simanis V., Kreis M., Henry Y.;
"AtSGP1, AtSGP2 and MAP4K alpha are nucleolar plant proteins that can
complement fission yeast mutants lacking a functional SIN pathway.";
J. Cell Sci. 117:4265-4275(2004).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=16965555; DOI=10.1111/j.1365-313X.2006.02863.x;
Chaiwongsar S., Otegui M.S., Jester P.J., Monson S.S., Krysan P.J.;
"The protein kinase genes MAP3K epsilon 1 and MAP3K epsilon 2 are
required for pollen viability in Arabidopsis thaliana.";
Plant J. 48:193-205(2006).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=cv. Columbia;
PubMed=23087695; DOI=10.3389/fpls.2012.00228;
Chaiwongsar S., Strohm A.K., Su S.-H., Krysan P.J.;
"Genetic analysis of the Arabidopsis protein kinases MAP3Kepsilon1 and
MAP3Kepsilon2 indicates roles in cell expansion and embryo
development.";
Front. Plant Sci. 3:1-10(2012).
-!- FUNCTION: Serine/threonine-protein kinase involved in the spatial
and temporal control system organizing cortical activities in
mitotic and postmitotic cells (PubMed:15292395). Required for the
normal functioning of the plasma membrane in developing pollen
(PubMed:16965555). Involved in the regulation of cell expansion
and embryo development (PubMed:23087695).
{ECO:0000269|PubMed:15292395, ECO:0000269|PubMed:16965555,
ECO:0000269|PubMed:23087695}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:A0A078CGE6}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q8T2I8}.
Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane
{ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus
during interphase (PubMed:15292395). Localized to the plasma
membrane in developing pollen grains (By similarity).
{ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:15292395}.
-!- TISSUE SPECIFICITY: Expressed in both the sporophytic and the
gametophytic tissues, especially in dividing cells. Mostly present
in flower buds and mature flowers. Accumulates also in embryos and
in roots. {ECO:0000269|PubMed:11489177,
ECO:0000269|PubMed:15292395, ECO:0000269|PubMed:23087695}.
-!- DEVELOPMENTAL STAGE: Expressed during embryo development.
{ECO:0000269|PubMed:23087695}.
-!- INDUCTION: Expression is cell cycle-regulated, with higher
expression in G2-M phases. {ECO:0000269|PubMed:15292395}.
-!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:A0A078CGE6}.
-!- DISRUPTION PHENOTYPE: Pollen lethality in plants lacking both
MAP3KE1 and MAP3KE2, associated with plasma membrane
irregularities following pollen mitosis I (PubMed:16965555).
Smaller plants with shorter roots due to reduced cell elongation
in roots and reduced cell expansion in rosette leaves, as well as
embryos arrest in the early stages of development
(PubMed:23087695). {ECO:0000269|PubMed:16965555,
ECO:0000269|PubMed:23087695}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC013483; AAF21208.1; -; Genomic_DNA.
EMBL; CP002686; AEE74627.1; -; Genomic_DNA.
RefSeq; NP_187455.1; NM_111677.4.
UniGene; At.43491; -.
ProteinModelPortal; Q9SFB6; -.
SMR; Q9SFB6; -.
STRING; 3702.AT3G07980.1; -.
iPTMnet; Q9SFB6; -.
PaxDb; Q9SFB6; -.
EnsemblPlants; AT3G07980.1; AT3G07980.1; AT3G07980.
GeneID; 819989; -.
Gramene; AT3G07980.1; AT3G07980.1; AT3G07980.
KEGG; ath:AT3G07980; -.
Araport; AT3G07980; -.
TAIR; locus:2077417; AT3G07980.
eggNOG; KOG0198; Eukaryota.
eggNOG; ENOG410XQGS; LUCA.
HOGENOM; HOG000030141; -.
OMA; DLEFIMA; -.
OrthoDB; EOG093600A9; -.
PhylomeDB; Q9SFB6; -.
PRO; PR:Q9SFB6; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9SFB6; baseline and differential.
Genevisible; Q9SFB6; AT.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00185; ARM; 5.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Cell division; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Serine/threonine-protein kinase; Transferase.
CHAIN 1 1367 MAP3K epsilon protein kinase 2.
/FTId=PRO_0000432225.
DOMAIN 20 274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 25 62 HEAT 1. {ECO:0000255}.
REPEAT 86 125 HEAT 2. {ECO:0000255}.
REPEAT 218 256 HEAT 3. {ECO:0000255}.
REPEAT 538 576 HEAT 4. {ECO:0000255}.
REPEAT 577 614 HEAT 5. {ECO:0000255}.
REPEAT 633 658 HEAT 6. {ECO:0000255}.
REPEAT 659 700 HEAT 7. {ECO:0000255}.
REPEAT 704 742 HEAT 8. {ECO:0000255}.
REPEAT 850 888 HEAT 9. {ECO:0000255}.
REPEAT 906 943 HEAT 10. {ECO:0000255}.
REPEAT 1045 1066 HEAT 11. {ECO:0000255}.
REPEAT 1067 1105 HEAT 12. {ECO:0000255}.
REPEAT 1112 1150 HEAT 13. {ECO:0000255}.
REPEAT 1154 1191 HEAT 14. {ECO:0000255}.
REPEAT 1196 1236 HEAT 15. {ECO:0000255}.
REPEAT 1257 1280 HEAT 16. {ECO:0000255}.
REPEAT 1281 1317 HEAT 17. {ECO:0000255}.
REPEAT 1347 1367 HEAT 18. {ECO:0000255}.
NP_BIND 26 34 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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


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