ID YODA_ARATH Reviewed; 883 AA.
AC Q9CAD5; Q6UY78;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase YODA {ECO:0000303|PubMed:14718171};
DE EC=2.7.11.25 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:22307275};
DE AltName: Full=YODA MAPKK kinase {ECO:0000303|PubMed:14718171};
GN Name=YDA {ECO:0000303|PubMed:14718171};
GN OrderedLocusNames=At1g63700 {ECO:0000312|Araport:AT1G63700};
GN ORFNames=F24D7.11 {ECO:0000312|EMBL:AAG52426.1};
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24, cv. Columbia, and cv. Landsberg erecta;
RX PubMed=14718171; DOI=10.1016/s0092-8674(03)01067-5;
RA Lukowitz W., Roeder A., Parmenter D., Somerville C.;
RT "A MAPKK kinase gene regulates extra-embryonic cell fate in Arabidopsis.";
RL Cell 116:109-119(2004).
RN [2]
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 [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 DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=15178800; DOI=10.1126/science.1096014;
RA Bergmann D.C., Lukowitz W., Somerville C.R.;
RT "Stomatal development and pattern controlled by a MAPKK kinase.";
RL Science 304:1494-1497(2004).
RN [5]
RP FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17259259; DOI=10.1105/tpc.106.048298;
RA Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S.;
RT "Stomatal development and patterning are regulated by environmentally
RT responsive mitogen-activated protein kinases in Arabidopsis.";
RL Plant Cell 19:63-73(2007).
RN [6]
RP FUNCTION.
RX PubMed=19286558; DOI=10.1126/science.1167784;
RA Bayer M., Nawy T., Giglione C., Galli M., Meinnel T., Lukowitz W.;
RT "Paternal control of embryonic patterning in Arabidopsis thaliana.";
RL Science 323:1485-1488(2009).
RN [7]
RP FUNCTION, INTERACTION WITH ASK7, AND CATALYTIC ACTIVITY.
RX PubMed=22307275; DOI=10.1038/nature10794;
RA Kim T.W., Michniewicz M., Bergmann D.C., Wang Z.Y.;
RT "Brassinosteroid regulates stomatal development by GSK3-mediated inhibition
RT of a MAPK pathway.";
RL Nature 482:419-422(2012).
RN [8]
RP FUNCTION.
RX PubMed=23263767; DOI=10.1105/tpc.112.104695;
RA Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S.;
RT "A MAPK cascade downstream of ERECTA receptor-like protein kinase regulates
RT Arabidopsis inflorescence architecture by promoting localized cell
RT proliferation.";
RL Plant Cell 24:4948-4960(2012).
RN [9]
RP INTERACTION WITH BASL AND MPK6, MUTAGENESIS OF K429R, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25843888; DOI=10.1016/j.devcel.2015.02.022;
RA Zhang Y., Wang P., Shao W., Zhu J.-K., Dong J.;
RT "The BASL polarity protein controls a MAPK signaling feedback loop in
RT asymmetric cell division.";
RL Dev. Cell 33:136-149(2015).
RN [10]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27746029; DOI=10.1016/j.cub.2016.08.066;
RA Zhang Y., Guo X., Dong J.;
RT "Phosphorylation of the polarity protein BASL differentiates asymmetric
RT cell fate through MAPKs and SPCH.";
RL Curr. Biol. 26:2957-2965(2016).
RN [11]
RP INTERACTION WITH BSK12/SSP.
RX PubMed=28821747; DOI=10.1038/s41598-017-08230-4;
RA Yuan G.L., Li H.J., Yang W.C.;
RT "The integration of Gbeta and MAPK signaling cascade in zygote
RT development.";
RL Sci. Rep. 7:8732-8732(2017).
CC -!- FUNCTION: Functions in a MAP kinase cascade that acts as a molecular
CC switch to regulate the first cell fate decisions in the zygote and the
CC early embryo. Promotes elongation of the zygote and development of its
CC basal daughter cell into the extra-embryonic suspensor. In stomatal
CC development, acts downstream of the LRR receptor TMM, but upstream of
CC the MKK4/MKK5-MPK3/MPK6 module to regulate stomatal cell fate before
CC the guard mother cell (GMC) is specified. Plays a central role in both
CC guard cell identity and pattern formation. This MAPK cascade also
CC functions downstream of the ER receptor in regulating coordinated local
CC cell proliferation, which shapes the morphology of plant organs. Upon
CC brassinosteroid signaling, is inhibited by phosphorylation of its auto-
CC inhibitory N-terminal domain by the GSK3-like kinase ASK7.
CC {ECO:0000269|PubMed:14718171, ECO:0000269|PubMed:15178800,
CC ECO:0000269|PubMed:17259259, ECO:0000269|PubMed:19286558,
CC ECO:0000269|PubMed:22307275, ECO:0000269|PubMed:23263767}.
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:0000269|PubMed:22307275};
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:0000269|PubMed:22307275};
CC -!- ACTIVITY REGULATION: Contains an N-terminal autoinhibitory domain.
CC -!- SUBUNIT: Interacts with ASK7 (PubMed:22307275). Interacts with
CC BSK12/SSP (PubMed:28821747). Binds to BASL and MPK6 (PubMed:25843888).
CC {ECO:0000269|PubMed:22307275, ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:28821747}.
CC -!- INTERACTION:
CC Q9CAD5; Q39011: ASK7; NbExp=4; IntAct=EBI-15967064, EBI-1798250;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:25843888}. Cell membrane
CC {ECO:0000269|PubMed:25843888}. Note=Recruited by BASL at the cell
CC cortex in a polarized manner. {ECO:0000269|PubMed:25843888}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, guard cells, stems,
CC flowers and siliques. {ECO:0000269|PubMed:14718171,
CC ECO:0000269|PubMed:15178800}.
CC -!- DEVELOPMENTAL STAGE: Copolarizes with BASL and MPK3/MPK6 in stomatal
CC asymmetric cell division (ACD) cells. {ECO:0000269|PubMed:27746029}.
CC -!- DISRUPTION PHENOTYPE: Severely dwarf plants that rarely survive on
CC soil, small rosettes, compact leaves, extremely compressed shoots, and
CC short, sterile flowers. No proper elongation of the zygote and
CC differentiation of the extra-embryonic suspensor. Excess of stomata in
CC leaves. {ECO:0000269|PubMed:14718171, ECO:0000269|PubMed:15178800}.
CC -!- MISCELLANEOUS: N-terminal deletions of YDA results in gain-of-function
CC alleles with phenotypes (no stomata and exaggerated suspensor growth)
CC opposite to loss-of-function phenotypes. {ECO:0000305|PubMed:14718171}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AY357947; AAR10434.1; -; mRNA.
DR EMBL; AY357948; AAR10435.1; -; Genomic_DNA.
DR EMBL; AY357949; AAR10436.1; -; Genomic_DNA.
DR EMBL; AC011622; AAG52426.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34135.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60901.1; -; Genomic_DNA.
DR PIR; A96662; A96662.
DR RefSeq; NP_001319310.1; NM_001334122.1.
DR RefSeq; NP_176557.1; NM_105047.2.
DR AlphaFoldDB; Q9CAD5; -.
DR SMR; Q9CAD5; -.
DR BioGRID; 27895; 2.
DR DIP; DIP-59652N; -.
DR IntAct; Q9CAD5; 1.
DR STRING; 3702.Q9CAD5; -.
DR iPTMnet; Q9CAD5; -.
DR PaxDb; 3702-AT1G63700-1; -.
DR ProteomicsDB; 242919; -.
DR EnsemblPlants; AT1G63700.1; AT1G63700.1; AT1G63700.
DR EnsemblPlants; AT1G63700.2; AT1G63700.2; AT1G63700.
DR GeneID; 842674; -.
DR Gramene; AT1G63700.1; AT1G63700.1; AT1G63700.
DR Gramene; AT1G63700.2; AT1G63700.2; AT1G63700.
DR KEGG; ath:AT1G63700; -.
DR Araport; AT1G63700; -.
DR TAIR; AT1G63700; YDA.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_124_0_1; -.
DR InParanoid; Q9CAD5; -.
DR OMA; MRIFGHE; -.
DR OrthoDB; 145974at2759; -.
DR PhylomeDB; Q9CAD5; -.
DR PRO; PR:Q9CAD5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAD5; baseline and differential.
DR Genevisible; Q9CAD5; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0010229; P:inflorescence development; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IMP:TAIR.
DR GO; GO:0010098; P:suspensor development; IMP:UniProtKB.
DR CDD; cd06632; STKc_MEKK1_plant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF17; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE YODA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Developmental protein;
KW Growth regulation; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..883
FT /note="Mitogen-activated protein kinase kinase kinase YODA"
FT /id="PRO_0000422174"
FT DOMAIN 400..656
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 525
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 406..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 429
FT /note="K->R: Kinase-inactive, enhanced polarized
FT subcellular localization in a BASL-dependent manner."
FT /evidence="ECO:0000269|PubMed:25843888"
FT CONFLICT 197
FT /note="P -> A (in Ref. 1; AAR10436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 95935 MW; 6A3FB18068F4318E CRC64;
MPWWSKSKDE KKKTNKESII DAFNRKLGFA SEDRSSGRSR KSRRRRDEIV SERGAISRLP
SRSPSPSTRV SRCQSFAERS PAVPLPRPIV RPHVTSTDSG MNGSQRPGLD ANLKPSWLPL
PKPHGATSIP DNTGAEPDFA TASVSSGSSV GDIPSDSLLS PLASDCENGN RTPVNISSRD
QSMHSNKNSA EMFKPVPNKN RILSASPRRR PLGTHVKNLQ IPQRDLVLCS APDSLLSSPS
RSPMRSFIPD QVSNHGLLIS KPYSDVSLLG SGQCSSPGSG YNSGNNSIGG DMATQLFWPQ
SRCSPECSPV PSPRMTSPGP SSRIQSGAVT PLHPRAGGST TGSPTRRLDD NRQQSHRLPL
PPLLISNTCP FSPTYSAATS PSVPRSPARA EATVSPGSRW KKGRLLGMGS FGHVYLGFNS
ESGEMCAMKE VTLCSDDPKS RESAQQLGQE ISVLSRLRHQ NIVQYYGSET VDDKLYIYLE
YVSGGSIYKL LQEYGQFGEN AIRNYTQQIL SGLAYLHAKN TVHRDIKGAN ILVDPHGRVK
VADFGMAKHI TAQSGPLSFK GSPYWMAPEV IKNSNGSNLA VDIWSLGCTV LEMATTKPPW
SQYEGVPAMF KIGNSKELPD IPDHLSEEGK DFVRKCLQRN PANRPTAAQL LDHAFVRNVM
PMERPIVSGE PAEAMNVASS TMRSLDIGHA RSLPCLDSED ATNYQQKGLK HGSGFSISQS
PRNMSCPISP VGSPIFHSHS PHISGRRSPS PISSPHALSG SSTPLTGCGG AIPFHHQRQT
TVNFLHEGIG SSRSPGSGGN FYTNSFFQEP SRQQDRSRSS PRTPPHVFWD NNGSIQPGYN
WNKDNQPVLS DHVSQQLLSE HLKLKSLDLR PGFSTPGSTN RGP
//
