M3KE1_BRANA
ID M3KE1_BRANA Reviewed; 1299 AA.
AC A0A078CGE6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=MAP3K epsilon protein kinase 1 {ECO:0000303|PubMed:11489177};
DE Short=BnM3KE1 {ECO:0000303|PubMed:11489177};
DE EC=2.7.11.1 {ECO:0000269|PubMed:11489177};
GN Name=M3KE1 {ECO:0000303|PubMed:11489177};
GN ORFNames=BnaA03g30290D {ECO:0000312|EMBL:CDX74018.1},
GN GSBRNA2T00111755001 {ECO:0000312|EMBL:CDX74018.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000312|EMBL:CDX74018.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh;
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
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 [3]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
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).
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). Required for the normal
CC functioning of the plasma membrane in developing pollen. Involved in
CC the regulation of cell expansion and embryo development (By
CC similarity). {ECO:0000250|UniProtKB:Q9LJD8,
CC ECO:0000269|PubMed:11489177}.
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:0000269|PubMed:11489177};
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:0000269|PubMed:11489177};
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.
CC {ECO:0000269|PubMed:11489177}.
CC -!- INDUCTION: Expression is cell cycle-regulated, with higher expression
CC in G2-M phases. {ECO:0000250|UniProtKB:Q9LJD8}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}.
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; LK031800; CDX74018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078CGE6; -.
DR STRING; 3708.A0A078CGE6; -.
DR EnsemblPlants; CDX74018; CDX74018; GSBRNA2T00111755001.
DR Gramene; CDX74018; CDX74018; GSBRNA2T00111755001.
DR OMA; NGYAVTQ; -.
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: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:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; 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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1299
FT /note="MAP3K epsilon protein kinase 1"
FT /id="PRO_0000432226"
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 532..570
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 611..649
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 653..694
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 698..736
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 743..780
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 781..820
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 868..900
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 901..939
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 955..994
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 998..1036
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1043..1081
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1085..1122
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1125..1164
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1186..1210
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1211..1249
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REPEAT 1279..1299
FT /note="HEAT 19"
FT /evidence="ECO:0000255"
FT REGION 291..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
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 1299 AA; 143609 MW; 9CF345E57701D166 CRC64;
MARQMTSSQF HKSKTLDNKY MLGDEIGKGA YGRVYIGLDL ENGDFVAIKQ VSLENIVQED
LNTIMQEIDL LKNLNHKNIV KYLGSLKTKT HLHIILEYVE NGSLANIIKP NKFGPFPESL
VTVYIAQVLE GLVYLHEQGV IHRDIKGANI LTTKEGLVKL ADFGVATKLN EADVNTHSVV
GTPYWMAPEV IEMSGVCAAS DIWSVGCTVI ELLTCVPPYY DLQPMPALFR IVQDDSPPIP
DSLSPDITDF LRQCFKKDSR QRPDAKTLLS HPWIRNSRRA LQSSLRHSGT IRYMKGADSS
SEKDGEGSQD IAESVSAEKV GMSKTNSKSK LGVGSFRSEK DQSSASDIGE ERADSEDDIM
SDQGPTLSIH DNKSSLQSST CSISSDAKGT SQDGKSEPDG NLEMEASEGR RKASATKQVG
KESSIQMQQR SHSFGPKGED RGLRKAVKTP SSYGGNELTR FSDPPGDACL HDLFHPLNKV
PEGKLNEASA STPASNANQG DSPVADGGKN DLATKLRARI AQKQMEGETG HSNDGGDLFR
LMMGVLKDDV IDIDGLVFDE KASPDNLLPL QAVEFSRLVS SLRPSETEDA IVTSCQKLVA
MFRHRPEQKV VFVTQHGFLP VMDLLDSPKS RVTCAVLQLI NEIIKDNIDF QENACLVGLI
PLVMSFAGPE RDRSREIRKE AAYFLQQLCQ SSSLTLQMFI ACRGIPVLVG FLEADYAKYR
SMVHLAIDGM WQVFKLKRST PRNDFCRIAA KNGILLRLIN TLYSLNEATL LASEGRSGQL
DQHEALLSVI DHPDVLKTRP GGGEEPSNSQ RSDLYQPDGD RPRSSSAALD ATEDVKQHHR
ISISSNRTST DKIQKLAESA SNGYAVTQPE QVRPLLSLLE KEPPSRHVSG QLDYVKHIAG
LEKHESILPL LRASIDTMPR YFSKTMSKKV MAIEGAASAS GVLSGSGVLN ARLGSDTSSG
LLSHMVTTLS AEVASQYLEK VADLLLEFAR ADTTVKSYMC SQSLLSRLFH MFNRVEPPIL
LKILKCTNHL STDPNCLESL QRADAIKHLI PNLEVKEGNL VDQIHHEVLS ALFNLCKINK
RRQEQAAENG IIPHLMLFVM SDSPLKQYAL PLLCDMAHAS RNSREQLRSH GGLDVYLSLL
DDEYWSVIAL DSIAVCLAQD NDNRKVEQAL LKDDAIYTLV NFFQSCPERH FVHILEPFLK
IITKSSRINT TLAVNGLTPL LIARLDHQDA IARLNLLKLI KAVYEHHPRP KQLIVENDLP
QRLQNLIEER REGQHLGGQV LVKQMATSLL KALHINTVL
