M3K3A_ARATH
ID M3K3A_ARATH Reviewed; 609 AA.
AC F4HRJ4; F4HRJ5; F4HRJ8; O82649; Q56ZS2; Q8W582; Q9LPH2; Q9ZRF7;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 3 {ECO:0000303|PubMed:27679653};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:Q9C5H5};
DE AltName: Full=MAP3K alpha protein kinase {ECO:0000303|PubMed:10095117};
DE Short=AtMAP3Kalpha {ECO:0000303|PubMed:10095117};
GN Name=MAPKKK3 {ECO:0000303|PubMed:27679653};
GN Synonyms=MAP3KA {ECO:0000303|Ref.1};
GN OrderedLocusNames=At1g53570 {ECO:0000312|Araport:AT1G53570};
GN ORFNames=F22G10.18 {ECO:0000312|EMBL:AAG51965.1},
GN T3F20.12 {ECO:0000312|EMBL:AAF78433.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Tregear J.W.;
RT "Characterization of MAP3Ka, a novel MEK kinase gene from Arabidopsis
RT thaliana.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10095117; DOI=10.1016/s0378-1119(99)00012-8;
RA Jouannic S., Hamal A., Leprince A.-S., Tregear J.W., Kreis M., Henry Y.;
RT "Characterisation of novel plant genes encoding MEKK/STE11 and RAF-related
RT protein kinases.";
RL Gene 229:171-181(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-608 (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=10375615; DOI=10.1016/s0378-1119(99)00152-3;
RA Jouannic C., Hamal A., Leprince A.-S., Tregear J., Kreis M., Henry Y.;
RT "Plant MAP kinase kinase kinases structure, classification and evolution.";
RL Gene 233:1-11(1999).
RN [8]
RP GENE FAMILY.
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 [9]
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 [10]
RP INTERACTION WITH PBL27.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
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 Evidence={ECO:0000250|UniProtKB:Q9C5H5};
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; Evidence={ECO:0000250|UniProtKB:Q9C5H5};
CC -!- SUBUNIT: Interacts with PBL27. {ECO:0000269|PubMed:27679653}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=F4HRJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HRJ4-2; Sequence=VSP_058681;
CC Name=3;
CC IsoId=F4HRJ4-3; Sequence=VSP_058680;
CC Name=4;
CC IsoId=F4HRJ4-4; Sequence=VSP_058679;
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, roots, leaves, seedlings,
CC stems and immature siliques. Absent of mature pollen.
CC {ECO:0000269|PubMed:10095117}.
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; U58918; AAD10848.1; -; mRNA.
DR EMBL; AJ010090; CAA08994.1; -; mRNA.
DR EMBL; AC018748; AAF78433.1; -; Genomic_DNA.
DR EMBL; AC024260; AAG51965.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32960.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32961.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32962.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32963.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32964.1; -; Genomic_DNA.
DR EMBL; AF419572; AAL31904.1; -; mRNA.
DR EMBL; AY140005; AAM98147.1; -; mRNA.
DR EMBL; BT002598; AAO00958.1; -; mRNA.
DR EMBL; AK220889; BAD94298.1; -; mRNA.
DR PIR; G96575; G96575.
DR PIR; T51625; T51625.
DR RefSeq; NP_001031181.1; NM_001036104.2. [F4HRJ4-3]
DR RefSeq; NP_001185211.1; NM_001198282.1. [F4HRJ4-2]
DR RefSeq; NP_001185212.1; NM_001198283.1. [F4HRJ4-4]
DR RefSeq; NP_564635.1; NM_104235.4. [F4HRJ4-1]
DR RefSeq; NP_849803.1; NM_179472.3. [F4HRJ4-3]
DR AlphaFoldDB; F4HRJ4; -.
DR SMR; F4HRJ4; -.
DR STRING; 3702.AT1G53570.1; -.
DR iPTMnet; F4HRJ4; -.
DR PaxDb; F4HRJ4; -.
DR PRIDE; F4HRJ4; -.
DR ProteomicsDB; 238841; -. [F4HRJ4-1]
DR EnsemblPlants; AT1G53570.1; AT1G53570.1; AT1G53570. [F4HRJ4-1]
DR EnsemblPlants; AT1G53570.2; AT1G53570.2; AT1G53570. [F4HRJ4-3]
DR EnsemblPlants; AT1G53570.3; AT1G53570.3; AT1G53570. [F4HRJ4-3]
DR EnsemblPlants; AT1G53570.4; AT1G53570.4; AT1G53570. [F4HRJ4-2]
DR EnsemblPlants; AT1G53570.5; AT1G53570.5; AT1G53570. [F4HRJ4-4]
DR GeneID; 841792; -.
DR Gramene; AT1G53570.1; AT1G53570.1; AT1G53570. [F4HRJ4-1]
DR Gramene; AT1G53570.2; AT1G53570.2; AT1G53570. [F4HRJ4-3]
DR Gramene; AT1G53570.3; AT1G53570.3; AT1G53570. [F4HRJ4-3]
DR Gramene; AT1G53570.4; AT1G53570.4; AT1G53570. [F4HRJ4-2]
DR Gramene; AT1G53570.5; AT1G53570.5; AT1G53570. [F4HRJ4-4]
DR KEGG; ath:AT1G53570; -.
DR Araport; AT1G53570; -.
DR TAIR; locus:2024832; AT1G53570.
DR eggNOG; KOG0198; Eukaryota.
DR InParanoid; F4HRJ4; -.
DR PhylomeDB; F4HRJ4; -.
DR PRO; PR:F4HRJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HRJ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IGI:TAIR.
DR GO; GO:1900150; P:regulation of defense response to fungus; IGI:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..609
FT /note="Mitogen-activated protein kinase kinase kinase 3"
FT /id="PRO_0000438542"
FT DOMAIN 214..470
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 347..372
FT /note="Missing (in isoform 4)"
FT /id="VSP_058679"
FT VAR_SEQ 497
FT /note="Missing (in isoform 3)"
FT /id="VSP_058680"
FT VAR_SEQ 525
FT /note="Missing (in isoform 2)"
FT /id="VSP_058681"
FT CONFLICT 32
FT /note="Missing (in Ref. 1; AAD10848 and 2; CAA08994)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> P (in Ref. 5; AAL31904)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="A -> P (in Ref. 1; AAD10848 and 2; CAA08994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 66447 MW; C7C451CE5E8209BB CRC64;
MPTWWGRKSC KNKDDNHRGI ISTDRDIKSS AVVVDPPLTP TRGGTPRCSR EFAGASSAFS
GFDSDSTEKK GHPLPRPLLS PVSIHHQDHV SGSTSGSTSV SSVSSSGSAD DQSQLVASRG
RGDVKFNVAA APRSPERVSP KAATITTRPT SPRHQRLSGV VSLESSTGRN DDGRSSSECH
PLPRPPTSPT SPSAVHGSRI GGGYETSPSG FSTWKKGKFL GSGTFGQVYL GFNSEKGKMC
AIKEVKVISD DQTSKECLKQ LNQEINLLNQ LCHPNIVQYY GSELSEETLS VYLEYVSGGS
IHKLLKDYGS FTEPVIQNYT RQILAGLAYL HGRNTVHRDI KGANILVDPN GEIKLADFGM
AKHVTAFSTM LSFKGSPYWM APEVVMSQNG YTHAVDIWSL GCTILEMATS KPPWSQFEGV
AAIFKIGNSK DTPEIPDHLS NDAKNFIRLC LQRNPTVRPT ASQLLEHPFL RNTTRVASTS
LPKDFPPRSY DGNFSLQPTR EPYPGRLSHD NYAKQPLSRT IKSPSRENVR AITSLPVSPC
SSPLRQLGPA YKSCFLSPPH PSYAFPGQDS GYNLAEFAAS PFRMKKDAMM EPSSFRTQTP
NSPLRSRLV
