SPCH_ARATH
ID SPCH_ARATH Reviewed; 364 AA.
AC Q700C7; Q9FK20;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Transcription factor SPEECHLESS {ECO:0000303|PubMed:17183265};
DE AltName: Full=Basic helix-loop-helix protein 98 {ECO:0000303|PubMed:12679534, ECO:0000303|PubMed:14600211};
DE Short=AtbHLH98 {ECO:0000303|PubMed:12679534, ECO:0000303|PubMed:14600211};
DE Short=bHLH 98 {ECO:0000303|PubMed:12679534, ECO:0000303|PubMed:14600211};
DE AltName: Full=Transcription factor EN 19 {ECO:0000303|PubMed:12897250};
DE AltName: Full=bHLH transcription factor bHLH098 {ECO:0000303|PubMed:12679534, ECO:0000303|PubMed:14600211};
GN Name=SPCH {ECO:0000303|PubMed:17183265};
GN Synonyms=BHLH98 {ECO:0000303|PubMed:12679534, ECO:0000303|PubMed:14600211},
GN EN19 {ECO:0000303|PubMed:12897250};
GN OrderedLocusNames=At5g53210 {ECO:0000312|Araport:AT5G53210};
GN ORFNames=MFH8.15 {ECO:0000312|EMBL:BAB09783.1};
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], MUTAGENESIS OF VAL-290 AND 358-GLN--CYS-364,
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=17183265; DOI=10.1038/nature05491;
RA MacAlister C.A., Ohashi-Ito K., Bergmann D.C.;
RT "Transcription factor control of asymmetric cell divisions that establish
RT the stomatal lineage.";
RL Nature 445:537-540(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [6]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [8]
RP REVIEW.
RX PubMed=17691100; DOI=10.1002/bies.20625;
RA Pillitteri L.J., Torii K.U.;
RT "Breaking the silence: three bHLH proteins direct cell-fate decisions
RT during stomatal development.";
RL Bioessays 29:861-870(2007).
RN [9]
RP FUNCTION.
RX PubMed=17183267; DOI=10.1038/nature05467;
RA Pillitteri L.J., Sloan D.B., Bogenschutz N.L., Torii K.U.;
RT "Termination of asymmetric cell division and differentiation of stomata.";
RL Nature 445:501-505(2007).
RN [10]
RP REVIEW.
RX PubMed=17928257; DOI=10.1016/j.tplants.2007.08.016;
RA Serna L.;
RT "bHLH proteins know when to make a stoma.";
RL Trends Plant Sci. 12:483-485(2007).
RN [11]
RP FUNCTION, INTERACTION WITH SCREAM/ICE1 AND SCREAM2, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=18641265; DOI=10.1105/tpc.108.060848;
RA Kanaoka M.M., Pillitteri L.J., Fujii H., Yoshida Y., Bogenschutz N.L.,
RA Takabayashi J., Zhu J.-K., Torii K.U.;
RT "SCREAM/ICE1 and SCREAM2 specify three cell-state transitional steps
RT leading to arabidopsis stomatal differentiation.";
RL Plant Cell 20:1775-1785(2008).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 171-SER--SER-220;
RP 171-SER--SER-264; SER-193; SER-211; THR-214; SER-219; 237-ARG--SER-367 AND
RP SER-255, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-177; SER-186; SER-193;
RP SER-211; THR-214 AND SER-219, REPRESSION BY YDA, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19008449; DOI=10.1126/science.1162263;
RA Lampard G.R., Macalister C.A., Bergmann D.C.;
RT "Arabidopsis stomatal initiation is controlled by MAPK-mediated regulation
RT of the bHLH SPEECHLESS.";
RL Science 322:1113-1116(2008).
RN [13]
RP REPRESSION BY LOW RELATIVE HUMIDITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22442411; DOI=10.1093/jxb/ers076;
RA Tricker P.J., Gibbings J.G., Rodriguez Lopez C.M., Hadley P.,
RA Wilkinson M.J.;
RT "Low relative humidity triggers RNA-directed de novo DNA methylation and
RT suppression of genes controlling stomatal development.";
RL J. Exp. Bot. 63:3799-3813(2012).
RN [14]
RP FUNCTION, MUTAGENESIS OF SER-38; THR-44 AND SER-65, PHOSPHORYLATION AT
RP SER-38; THR-40; SER-43; THR-44; SER-65; SER-171; SER-177; SER-181; SER-186;
RP THR-214 AND SER-219, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22466366; DOI=10.1038/ncb2471;
RA Gudesblat G.E., Schneider-Pizon J., Betti C., Mayerhofer J., Vanhoutte I.,
RA van Dongen W., Boeren S., Zhiponova M., de Vries S., Jonak C.,
RA Russinova E.;
RT "SPEECHLESS integrates brassinosteroid and stomata signalling pathways.";
RL Nat. Cell Biol. 14:548-554(2012).
RN [15]
RP FUNCTION, MUTAGENESIS OF SER-193; SER-211; THR-214 AND SER-219, AND
RP REPRESSION BY OSMOTIC STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=25381317; DOI=10.1093/pcp/pcu159;
RA Kumari A., Jewaria P.K., Bergmann D.C., Kakimoto T.;
RT "Arabidopsis reduces growth under osmotic stress by decreasing SPEECHLESS
RT protein.";
RL Plant Cell Physiol. 55:2037-2046(2014).
RN [16]
RP FUNCTION, AND PHOSPHORYLATION.
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 [17]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-186, MUTAGENESIS OF
RP SER-38; THR-44 AND SER-186, TISSUE SPECIFICITY, REPRESSION BY BRASSINAZOLE,
RP AND INTERACTION WITH CDKA-1.
RC STRAIN=cv. Columbia;
RX PubMed=25680231; DOI=10.1016/j.molp.2014.12.014;
RA Yang K.-Z., Jiang M., Wang M., Xue S., Zhu L.-L., Wang H.-Z., Zou J.-J.,
RA Lee E.-K., Sack F., Le J.;
RT "Phosphorylation of serine 186 of bHLH transcription factor SPEECHLESS
RT promotes stomatal development in Arabidopsis.";
RL Mol. Plant 8:783-795(2015).
RN [18]
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
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 [19]
RP FUNCTION, MUTAGENESIS OF 104-HIS--ARG-112 AND ARG-111, AND INTERACTION WITH
RP SCRM/ICE1 AND SCRM2.
RC STRAIN=cv. Columbia;
RX PubMed=28507175; DOI=10.1104/pp.17.00615;
RA de Marcos A., Houbaert A., Trivino M., Delgado D., Martin-Trillo M.,
RA Russinova E., Fenoll C., Mena M.;
RT "A mutation in the bHLH domain of the SPCH transcription factor uncovers a
RT BR-dependent mechanism for stomatal development.";
RL Plant Physiol. 174:823-842(2017).
RN [20]
RP PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=30429609; DOI=10.1038/s41586-018-0714-x;
RA Houbaert A., Zhang C., Tiwari M., Wang K., de Marcos Serrano A.,
RA Savatin D.V., Urs M.J., Zhiponova M.K., Gudesblat G.E., Vanhoutte I.,
RA Eeckhout D., Boeren S., Karimi M., Betti C., Jacobs T., Fenoll C., Mena M.,
RA de Vries S., De Jaeger G., Russinova E.;
RT "POLAR-guided signalling complex assembly and localization drive asymmetric
RT cell division.";
RL Nature 563:574-578(2018).
CC -!- FUNCTION: Transcription factor acting as an integration node for
CC stomata and brassinosteroid (BR) signaling pathways to control stomatal
CC initiation and development (PubMed:22466366, PubMed:28507175).
CC Activates transcription when in the presence of SCRM/ICE1
CC (PubMed:28507175). Functions as a dimer with SCRM or SCRM2 during
CC stomatal initiation (PubMed:18641265). Required for the initiation, the
CC spacing and the formation of stomata, by promoting the first asymmetric
CC cell divisions (PubMed:25843888, PubMed:25680231, PubMed:19008449).
CC Together with FMA and MUTE, modulates the stomata formation. Involved
CC in the regulation of growth reduction under osmotic stress (e.g.
CC mannitol), associated with a quick decrease of meristemoid mother cells
CC (MMCs) number lower stomatal index and density (PubMed:25381317).
CC {ECO:0000269|PubMed:17183265, ECO:0000269|PubMed:17183267,
CC ECO:0000269|PubMed:18641265, ECO:0000269|PubMed:19008449,
CC ECO:0000269|PubMed:22466366, ECO:0000269|PubMed:25381317,
CC ECO:0000269|PubMed:25680231, ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:28507175}.
CC -!- ACTIVITY REGULATION: Negatively regulated through phosphorylation by
CC the MAPK module (PubMed:19008449). Activity is constrained by polarized
CC BASL in stomatal lineage ground cells (SLGCs) undergoing ACD
CC (PubMed:27746029). {ECO:0000269|PubMed:19008449,
CC ECO:0000269|PubMed:27746029}.
CC -!- SUBUNIT: Homodimer (Probable). Forms dimers with SCRM and SCRM2
CC (PubMed:18641265, PubMed:28507175). May interact with CDKA-1
CC (PubMed:25680231). {ECO:0000269|PubMed:18641265,
CC ECO:0000269|PubMed:25680231, ECO:0000269|PubMed:28507175, ECO:0000305}.
CC -!- INTERACTION:
CC Q700C7; Q9C4Z6: RACK1B; NbExp=3; IntAct=EBI-15976443, EBI-4457470;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:19008449}.
CC -!- TISSUE SPECIFICITY: Expressed in developing leaf epidermis
CC (PubMed:17183265). Reduced accumulation in the stomatal lineage ground
CC cells (SLGCs) where BASL is polarized in the cell cortex
CC (PubMed:27746029). Observed in small cells of non-protruding hypocotyl
CC cell files and of developing cotyledon epidermis (PubMed:22466366).
CC Restricted to meristemoids (stomatal precursor cell) in leaves
CC epidermis, mostly in dividing cells of non-protruding cell files
CC (PubMed:25680231, PubMed:18641265, PubMed:19008449).
CC {ECO:0000269|PubMed:17183265, ECO:0000269|PubMed:18641265,
CC ECO:0000269|PubMed:19008449, ECO:0000269|PubMed:22466366,
CC ECO:0000269|PubMed:25680231, ECO:0000269|PubMed:27746029}.
CC -!- DEVELOPMENTAL STAGE: First observed in a subset of undifferentiated
CC epidermal cells, often by pair of neighboring cells. Later confined to
CC small epidermal cells, including cells that have recently divided next
CC to stomatal lineage cells. Also expressed in stomatal lineage cells,
CC fading out progressively during meristemoid determination.
CC {ECO:0000269|PubMed:17183265, ECO:0000269|PubMed:18641265,
CC ECO:0000269|PubMed:19008449}.
CC -!- INDUCTION: Repressed by brassinazole (BRZ), thus leading to a reduced
CC number of stomata in hypocotyls (PubMed:25680231). Inhibited by low
CC relative humidity (LRH) via epigenetic CG methylation, thus leading to
CC a reduced stomatal index (PubMed:22442411). Repressed by YDA (at
CC protein level) (PubMed:19008449). Post-transcriptional decrease of
CC protein level in response to osmotic stress (e.g. mannitol), through
CC the action of a mitogen-activated protein kinase (MAPK) cascade; this
CC repression is reversed by the MAPK kinase inhibitor PD98059
CC (PubMed:25381317). {ECO:0000269|PubMed:19008449,
CC ECO:0000269|PubMed:22442411, ECO:0000269|PubMed:25381317,
CC ECO:0000269|PubMed:25680231}.
CC -!- PTM: Phosphorylated by ASK7/BIN2 and ASK3/SK12; this post-translational
CC modification inhibits activity and limit epidermal cell proliferation
CC (PubMed:30429609, PubMed:22466366). Phosphorylation by MPK3 and MPK6
CC leads to the inhibition of stomatal fate and to degradation
CC (PubMed:25843888, PubMed:19008449). Stabilized by CDKA-1-mediated
CC phosphorylation at Ser-186 which promotes stomatal development
CC (PubMed:25680231). {ECO:0000269|PubMed:19008449,
CC ECO:0000269|PubMed:22466366, ECO:0000269|PubMed:25680231,
CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:30429609}.
CC -!- DISRUPTION PHENOTYPE: Stomatal defects in cotyledons and hypocotyls.
CC {ECO:0000269|PubMed:19008449, ECO:0000269|PubMed:25680231}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09783.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ868373; ABI26170.1; -; mRNA.
DR EMBL; AB013388; BAB09783.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96323.1; -; Genomic_DNA.
DR EMBL; AJ630498; CAG25871.1; -; mRNA.
DR EMBL; AY568670; AAS79560.1; -; mRNA.
DR RefSeq; NP_200133.2; NM_124700.3.
DR AlphaFoldDB; Q700C7; -.
DR SMR; Q700C7; -.
DR BioGRID; 20647; 3.
DR DIP; DIP-61849N; -.
DR IntAct; Q700C7; 2.
DR STRING; 3702.AT5G53210.1; -.
DR iPTMnet; Q700C7; -.
DR PaxDb; Q700C7; -.
DR EnsemblPlants; AT5G53210.1; AT5G53210.1; AT5G53210.
DR GeneID; 835402; -.
DR Gramene; AT5G53210.1; AT5G53210.1; AT5G53210.
DR KEGG; ath:AT5G53210; -.
DR Araport; AT5G53210; -.
DR TAIR; locus:2154197; AT5G53210.
DR eggNOG; ENOG502QS6Y; Eukaryota.
DR HOGENOM; CLU_044652_0_1_1; -.
DR InParanoid; Q700C7; -.
DR OMA; VDDTMVH; -.
DR OrthoDB; 1208483at2759; -.
DR PhylomeDB; Q700C7; -.
DR PRO; PR:Q700C7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q700C7; baseline and differential.
DR Genevisible; Q700C7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0010052; P:guard cell differentiation; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0090547; P:response to low humidity; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR044283; FAMA/SPEECHLESS/MUTE.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR46684; PTHR46684; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..364
FT /note="Transcription factor SPEECHLESS"
FT /id="PRO_0000358856"
FT DOMAIN 99..150
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 35..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..112
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 113..150
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 171..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 40
FT /note="Phosphothreonine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 43
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 44
FT /note="Phosphothreonine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 65
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 171
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 177
FT /note="Phosphoserine; by ASK7, MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:22466366,
FT ECO:0000305|PubMed:19008449"
FT MOD_RES 181
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:22466366"
FT MOD_RES 186
FT /note="Phosphoserine; by CDKA-1, ASK7, MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:22466366,
FT ECO:0000269|PubMed:25680231, ECO:0000305|PubMed:19008449"
FT MOD_RES 193
FT /note="Phosphoserine; by MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:19008449"
FT MOD_RES 211
FT /note="Phosphoserine; by MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:19008449"
FT MOD_RES 214
FT /note="Phosphothreonine; by ASK7, MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:19008449,
FT ECO:0000269|PubMed:22466366"
FT MOD_RES 219
FT /note="Phosphoserine; by ASK7, MPK3 and MPK6"
FT /evidence="ECO:0000269|PubMed:19008449,
FT ECO:0000269|PubMed:22466366"
FT MUTAGEN 38
FT /note="S->A: Extra divisions outside the stomatal cell
FT lineage and reduced phosphorylation by ASK7; when
FT associated with A-44."
FT /evidence="ECO:0000269|PubMed:22466366,
FT ECO:0000269|PubMed:25680231"
FT MUTAGEN 44
FT /note="T->A: Extra divisions outside the stomatal cell
FT lineage and reduced phosphorylation by ASK7; when
FT associated with A-38."
FT /evidence="ECO:0000269|PubMed:22466366,
FT ECO:0000269|PubMed:25680231"
FT MUTAGEN 65
FT /note="S->A: Extra divisions outside the stomatal cell
FT lineage and reduced phosphorylation by ASK7."
FT /evidence="ECO:0000269|PubMed:22466366"
FT MUTAGEN 104..112
FT /note="HVTVERNRR->PVTVPRNRP: Plants are fertile and have a
FT normal growth, but they form few stomata, some of them
FT clustered, in cotyledons and leaves, and lack stomata in
FT hypocotyls."
FT /evidence="ECO:0000269|PubMed:28507175"
FT MUTAGEN 111
FT /note="R->W: In spch-5; normal growth, but extremely low
FT number of sometimes clustered stomata in leaves and stomata
FT free hypocotyls due to decreased ability to initiate and
FT amplify lineages, defects in asymmetric cell fate
FT allocation, and misorientation of asymmetric division
FT planes. These phenotypes are partly rescued by
FT brassinosteroids (BRs) by rescuing the expression of a set
FT of target genes."
FT /evidence="ECO:0000269|PubMed:28507175"
FT MUTAGEN 171..264
FT /note="Missing: In delta-93; impaired MPK3/MPK6 mediated
FT phosphorylation and large clusters of stomata in leaves
FT epidermis."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 171..220
FT /note="Missing: In delta-49; reduced MPK3/MPK6 mediated
FT phosphorylation and excessive numbers of asymmetric cell
FT divisions in leaves epidermis leading to the creation of
FT cells with meristemoid morphology, but fails to produce
FT stomata."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 186
FT /note="S->A: Strong reduction of CDKA-1-mediated
FT phosphorylation. Unable to rescue stomatal defects in
FT disrupted mutants. Triggers excess physically asymmetric
FT divisions but not stomata formation."
FT /evidence="ECO:0000269|PubMed:25680231"
FT MUTAGEN 186
FT /note="S->D: Phosphomimetic, presence of stomatal clusters
FT and increased stomatal density, can complement stomatal
FT production defects associated with inactive CDKA-1."
FT /evidence="ECO:0000269|PubMed:25680231"
FT MUTAGEN 193
FT /note="S->A: Unable to rescue disruption phenotype. Ectopic
FT stomata formation and increased accumulation; when
FT associated with A-211, A-214, A-219 and A-255. Ectopic
FT asymmetric cell divisions, but fails to produce stomata,
FT and reduced repression by osmotic stress (e.g. mannitol);
FT when associated with A-211, A-214 and A-219."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 211
FT /note="S->A: Ectopic stomata formation and increased
FT accumulation; when associated with A-193, A-214, A-219 and
FT A-255. Ectopic asymmetric cell divisions, but fails to
FT produce stomata, and reduced repression by osmotic stress
FT (e.g. mannitol); when associated with A-193, A-214 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 214
FT /note="T->A: Ectopic stomata formation and increased
FT accumulation; when associated with A-193, A-211, A-219 and
FT A-255. Ectopic asymmetric cell divisions, but fails to
FT produce stomata, and reduced repression by osmotic stress
FT (e.g. mannitol); when associated with A-193, A-211 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 219
FT /note="S->A: Ectopic stomata formation and increased
FT accumulation; when associated with A-193, A-211, A-214 and
FT A-255. Ectopic asymmetric cell divisions, but fails to
FT produce stomata, and reduced repression by osmotic stress
FT (e.g. mannitol); when associated with A-193, A-211 and A-
FT 214."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 237..267
FT /note="Missing: In delta-31; reduced MPK3/MPK6 mediated
FT phosphorylation and excessive numbers of asymmetric cell
FT divisions in leaves epidermis leading to the creation of
FT cells with meristemoid morphology."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 255
FT /note="S->A: Ectopic stomata formation and increased
FT accumulation; when associated with A-193, A-211, A-214 and
FT A-219."
FT /evidence="ECO:0000269|PubMed:19008449"
FT MUTAGEN 290
FT /note="V->M: In spch-2; reduced stomatal index."
FT /evidence="ECO:0000269|PubMed:17183265"
FT MUTAGEN 358..364
FT /note="Missing: In spch-1; no stomata."
FT /evidence="ECO:0000269|PubMed:17183265"
SQ SEQUENCE 364 AA; 40169 MW; 3946B847B6D4371C CRC64;
MQEIIPDFLE ECEFVDTSLA GDDLFAILES LEGAGEISPT AASTPKDGTT SSKELVKDQD
YENSSPKRKK QRLETRKEED EEEEDGDGEA EEDNKQDGQQ KMSHVTVERN RRKQMNEHLT
VLRSLMPCFY VKRGDQASII GGVVEYISEL QQVLQSLEAK KQRKTYAEVL SPRVVPSPRP
SPPVLSPRKP PLSPRINHHQ IHHHLLLPPI SPRTPQPTSP YRAIPPQLPL IPQPPLRSYS
SLASCSSLGD PPPYSPASSS SSPSVSSNHE SSVINELVAN SKSALADVEV KFSGANVLLK
TVSHKIPGQV MKIIAALEDL ALEILQVNIN TVDETMLNSF TIKIGIECQL SAEELAQQIQ
QTFC
