BASL_ARATH
ID BASL_ARATH Reviewed; 262 AA.
AC Q5BPF3; F4K0I7; Q5Q097; Q5Q098; Q9FJG8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE {ECO:0000303|PubMed:19523675};
GN Name=BASL {ECO:0000303|PubMed:19523675};
GN OrderedLocusNames=At5g60880 {ECO:0000312|Araport:AT5G60880};
GN ORFNames=MAE1.13 {ECO:0000312|EMBL:BAB10108.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=19523675; DOI=10.1016/j.cell.2009.04.018;
RA Dong J., MacAlister C.A., Bergmann D.C.;
RT "BASL controls asymmetric cell division in Arabidopsis.";
RL Cell 137:1320-1330(2009).
RN [7]
RP REVIEW.
RX PubMed=20705185; DOI=10.1016/s0070-2153(10)91009-0;
RA Dong J., Bergmann D.C.;
RT "Stomatal patterning and development.";
RL Curr. Top. Dev. Biol. 91:267-297(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20220310; DOI=10.4161/psb.5.3.10704;
RA Hunt L., Gray J.E.;
RT "BASL and EPF2 act independently to regulate asymmetric divisions during
RT stomatal development.";
RL Plant Signal. Behav. 5:278-280(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21963668; DOI=10.1105/tpc.111.088583;
RA Pillitteri L.J., Peterson K.M., Horst R.J., Torii K.U.;
RT "Molecular profiling of stomatal meristemoids reveals new component of
RT asymmetric cell division and commonalities among stem cell populations in
RT Arabidopsis.";
RL Plant Cell 23:3260-3275(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21903812; DOI=10.1126/science.1202185;
RA Robinson S., Barbier de Reuille P., Chan J., Bergmann D., Prusinkiewicz P.,
RA Coen E.;
RT "Generation of spatial patterns through cell polarity switching.";
RL Science 333:1436-1440(2011).
RN [11]
RP REVIEW.
RX PubMed=23044038; DOI=10.1016/j.pbi.2012.09.013;
RA Facette M.R., Smith L.G.;
RT "Division polarity in developing stomata.";
RL Curr. Opin. Plant Biol. 15:585-592(2012).
RN [12]
RP INDUCTION BY MUTE.
RX PubMed=23662679; DOI=10.1111/tpj.12244;
RA Trivino M., Martin-Trillo M., Ballesteros I., Delgado D., de Marcos A.,
RA Desvoyes B., Gutierrez C., Mena M., Fenoll C.;
RT "Timely expression of the Arabidopsis stoma-fate master regulator MUTE is
RT required for specification of other epidermal cell types.";
RL Plant J. 75:808-822(2013).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 69-LEU--LEU-71; SER-72;
RP SER-89; SER-145; SER-168; 223-PHE--PHE-225; SER-235; SER-246 AND
RP 253-VAL--LEU-255, PHOSPHORYLATION AT SER-89; SER-145; SER-168; SER-235 AND
RP SER-246, SUBCELLULAR LOCATION, AND INTERACTION WITH YDA; MPK6 AND MKK5.
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 [14]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF SER-72; SER-89; SER-145; SER-168; SER-235 AND SER-246, AND
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 [15]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 51-LYS--ARG-64; 222-SER--PHE-262 AND
RP 223-PHE--PHE-225, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=27422992; DOI=10.1093/jxb/erw274;
RA Zhang Y., Bergmann D.C., Dong J.;
RT "Fine-scale dissection of the subdomains of polarity protein BASL in
RT stomatal asymmetric cell division.";
RL J. Exp. Bot. 67:5093-5103(2016).
RN [16]
RP FUNCTION, INTERACTION WITH POLAR; ASK7/BIN2 AND ASK3/SK12, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT
RP SER-72; SER-85; SER-86; SER-87; SER-89 AND THR-91, AND MUTAGENESIS OF
RP SER-72; SER-85; SER-86; SER-87; SER-89 AND THR-91.
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: Regulates asymmetric cell division (ACD), especially in
CC stomatal-lineage cells, probably by modulating accumulation and
CC subcellular polarization of POLAR and SPCH (PubMed:30429609,
CC PubMed:25843888). Mediates an attenuation of MAPK signaling upon
CC polarization of POLAR and ASK7/BIN2 in stomatal lineage ground cells
CC (SLGCs) undergoing ACD, and relieves BIN2 inhibition of SPCH in the
CC nucleus (PubMed:30429609, PubMed:25843888). When phosphorylated,
CC functions as a scaffold and recruits the MAPKKK YODA, MPK3 and MPK6 to
CC spatially reorganize the MAPK signaling pathway at the cortex of cells
CC undergoing ACD (PubMed:25843888). Cortical polarization leads to
CC elevated nuclear MPK6 signaling and lowered SPCH abundance in one of
CC the two daughter cells, thus differentiating the two daughter cells
CC after ACD (PubMed:27746029). {ECO:0000269|PubMed:19523675,
CC ECO:0000269|PubMed:20220310, ECO:0000269|PubMed:21963668,
CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27746029,
CC ECO:0000269|PubMed:30429609}.
CC -!- SUBUNIT: Component of a complex made of POLAR, BASL, ASK7/BIN2 and
CC ASK3/SK12 (PubMed:30429609). Interacts with POLAR, ASK7/BIN2 and
CC ASK3/SK12 (PubMed:30429609). Binds to YDA when phosphorylated
CC (PubMed:25843888). Interacts with MPK6, MPK3 and MKK5
CC (PubMed:25843888). {ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:30429609}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:27422992, ECO:0000269|PubMed:30429609}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:19523675,
CC ECO:0000269|PubMed:21903812, ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:27422992, ECO:0000269|PubMed:27746029,
CC ECO:0000269|PubMed:30429609}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19523675, ECO:0000269|PubMed:21903812,
CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27422992,
CC ECO:0000269|PubMed:27746029, ECO:0000269|PubMed:30429609}. Cell
CC membrane {ECO:0000269|PubMed:27746029}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27746029}. Note=Dynamic and highly polarized
CC subcellular localization at the cortical polarity in a phosphorylation
CC status-dependent manner (PubMed:19523675, PubMed:21903812,
CC PubMed:30429609, PubMed:25843888, PubMed:27746029, PubMed:27422992).
CC Polarity is only exhibited by one daughter cell after an asymmetric
CC cell division (PubMed:27746029). ASK7/BIN2-mediated nuclear exclusion
CC (PubMed:30429609). First localized to the nucleus in asymmetric cell
CC division (ACD) precursors (PubMed:30429609). In asymmetrically dividing
CC stomatal-lineage cells, before division, accumulates in a polarized
CC crescent at the cell periphery (e.g. meristemoid mother cells (MMCs)),
CC and, after division, localizes differentially to the nucleus (e.g. in
CC meristemoids) and a peripheral crescent in self-renewing cells and
CC their sisters (e.g. stomatal lineage ground cell (SLGC))
CC (PubMed:19523675, PubMed:30429609, PubMed:25843888, PubMed:27422992).
CC Localized in the cell periphery at a position that minimizes the
CC inverse distance from all points along the new division boundaries
CC (PubMed:21903812). {ECO:0000269|PubMed:19523675,
CC ECO:0000269|PubMed:21903812, ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:27422992, ECO:0000269|PubMed:27746029,
CC ECO:0000269|PubMed:30429609}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BPF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BPF3-2; Sequence=VSP_054867, VSP_054868;
CC -!- TISSUE SPECIFICITY: Mostly expressed in stomatal lineage cells
CC including asymmetrically dividing meristemoid mother cells (MMCs) and
CC meristemoids, and, at lower levels, in their sisters (PubMed:19523675,
CC PubMed:27422992). Also present in vasculature (PubMed:19523675).
CC Expressed at low levels in the epidermal pavement cells
CC (PubMed:27422992). {ECO:0000269|PubMed:19523675,
CC ECO:0000269|PubMed:27422992}.
CC -!- DEVELOPMENTAL STAGE: First observed in nuclei of epidermal cells 16
CC hours post germination (PubMed:19523675). Later confined to cells
CC undergoing asymmetric divisions (e.g. stomatal lineage cells)
CC (PubMed:19523675). Expressed in protodermal cells in young seedlings
CC (PubMed:30429609). Copolarizes with YDA and MPK3/MPK6 in stomatal
CC asymmetric cell division (ACD) cells (PubMed:27746029).
CC {ECO:0000269|PubMed:19523675, ECO:0000269|PubMed:27746029,
CC ECO:0000269|PubMed:30429609}.
CC -!- INDUCTION: Induced by MUTE in stomatal-lineage cells.
CC {ECO:0000269|PubMed:23662679}.
CC -!- PTM: Cortical localization of BASL requires phosphorylation mediated by
CC MPK3 and MPK6 (PubMed:25843888). Phosphorylation promotes YDA binding
CC (PubMed:25843888). Phosphorylation status modulates subcellular
CC mobility (PubMed:27746029). {ECO:0000269|PubMed:25843888,
CC ECO:0000269|PubMed:27746029}.
CC -!- DISRUPTION PHENOTYPE: Clustered stomatal pattern distribution in
CC seedlings characterized by excessive numbers of small epidermal cells,
CC due to impaired meristemoid mother cell (MMC) asymmetric division
CC (PubMed:27746029). Abnormal non-polarized subcellular localization of
CC POLAR and YDA in asymmetric dividing cells (PubMed:30429609,
CC PubMed:25843888). {ECO:0000269|PubMed:19523675,
CC ECO:0000269|PubMed:20220310, ECO:0000269|PubMed:21963668,
CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27746029,
CC ECO:0000269|PubMed:30429609}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10108.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB015472; BAB10108.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB008269; BAB10108.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97391.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97392.1; -; Genomic_DNA.
DR EMBL; AY800653; AAV68889.1; -; mRNA.
DR EMBL; AY800654; AAV68890.1; -; mRNA.
DR EMBL; AY924875; AAX23950.1; -; mRNA.
DR RefSeq; NP_001032115.1; NM_001037038.1. [Q5BPF3-2]
DR RefSeq; NP_200896.1; NM_125481.3. [Q5BPF3-1]
DR AlphaFoldDB; Q5BPF3; -.
DR BioGRID; 21453; 1.
DR STRING; 3702.AT5G60880.1; -.
DR iPTMnet; Q5BPF3; -.
DR PaxDb; Q5BPF3; -.
DR PRIDE; Q5BPF3; -.
DR ProteomicsDB; 240814; -. [Q5BPF3-1]
DR EnsemblPlants; AT5G60880.1; AT5G60880.1; AT5G60880. [Q5BPF3-1]
DR EnsemblPlants; AT5G60880.2; AT5G60880.2; AT5G60880. [Q5BPF3-2]
DR GeneID; 836209; -.
DR Gramene; AT5G60880.1; AT5G60880.1; AT5G60880. [Q5BPF3-1]
DR Gramene; AT5G60880.2; AT5G60880.2; AT5G60880. [Q5BPF3-2]
DR KEGG; ath:AT5G60880; -.
DR Araport; AT5G60880; -.
DR TAIR; locus:2159305; AT5G60880.
DR eggNOG; ENOG502S4M9; Eukaryota.
DR HOGENOM; CLU_110871_0_0_1; -.
DR InParanoid; Q5BPF3; -.
DR OMA; WELMGSP; -.
DR OrthoDB; 1290428at2759; -.
DR PhylomeDB; Q5BPF3; -.
DR PRO; PR:Q5BPF3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5BPF3; baseline and differential.
DR Genevisible; Q5BPF3; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008356; P:asymmetric cell division; IGI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR040378; BASL.
DR PANTHER; PTHR33914; PTHR33914; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..262
FT /note="Protein BREAKING OF ASYMMETRY IN THE STOMATAL
FT LINEAGE"
FT /id="PRO_0000429315"
FT REGION 32..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..262
FT /note="Required for polarization at the cell cortex"
FT /evidence="ECO:0000269|PubMed:27422992"
FT MOTIF 50..57
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768,
FT ECO:0000269|PubMed:27422992"
FT MOTIF 61..68
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000269|PubMed:27422992"
FT MOTIF 223..226
FT /note="FxFP, required for cortical polarity formation"
FT /evidence="ECO:0000269|PubMed:27422992"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:30429609"
FT MOD_RES 85
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:30429609"
FT MOD_RES 86
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:30429609"
FT MOD_RES 87
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000269|PubMed:30429609"
FT MOD_RES 89
FT /note="Phosphoserine; by ASK7 and MPK6"
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:30429609"
FT MOD_RES 91
FT /note="Phosphothreonine; by ASK7"
FT /evidence="ECO:0000269|PubMed:30429609"
FT MOD_RES 145
FT /note="Phosphoserine; by MPK6"
FT /evidence="ECO:0000269|PubMed:25843888"
FT MOD_RES 168
FT /note="Phosphoserine; by MPK6"
FT /evidence="ECO:0000269|PubMed:25843888"
FT MOD_RES 235
FT /note="Phosphoserine; by MPK6"
FT /evidence="ECO:0000269|PubMed:25843888"
FT MOD_RES 246
FT /note="Phosphoserine; by MPK6"
FT /evidence="ECO:0000269|PubMed:25843888"
FT VAR_SEQ 197..208
FT /note="RTKEEEDIDASD -> VMLRNIFQLQSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_054867"
FT VAR_SEQ 209..262
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_054868"
FT MUTAGEN 51..64
FT /note="Missing: In BASL_NLS; impaired nuclear localization,
FT but diffuse accumulation in the cytoplasm and polarized at
FT the cell cortex in stomatal asymmetric cell division (ACD)
FT cells. Can rescue disruption phenotypes."
FT /evidence="ECO:0000269|PubMed:27422992"
FT MUTAGEN 69..71
FT /note="LSL->ASA: In BASL-d1; impaired cortical polar
FT accumulation and stomata defects, reduced interaction with
FT YDA and fails to induce polarization; when associated with
FT 223-AAA-225 and 253-AAA-255."
FT /evidence="ECO:0000269|PubMed:25843888"
FT MUTAGEN 72
FT /note="S->A: Reduced ASK7-mediated phosphorylation and
FT impaired polarized subcellular localization. Reduced
FT interaction with YDA and fails to induce polarization; when
FT associated with A-89, A-145, A-168, A-235 and A-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029, ECO:0000269|PubMed:30429609"
FT MUTAGEN 72
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-89, D-145, D-168, D-235 and D-246. In
FT BASL_14D; reduced mobility leading to severely retarded
FT recovery at the cell cortex and prolonged accumulation even
FT in mature pavement cells, and impaired stomatal production
FT due to suppressed SLGC division potential; when associated
FT with D-89."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 85
FT /note="S->A: Reduced ASK7-mediated phosphorylation; when
FT associated with A-86, A-87, A-89 and A-91."
FT /evidence="ECO:0000269|PubMed:30429609"
FT MUTAGEN 86
FT /note="S->A: Reduced ASK7-mediated phosphorylation; when
FT associated with A-85, A-87, A-89 and A-91."
FT /evidence="ECO:0000269|PubMed:30429609"
FT MUTAGEN 87
FT /note="S->A: Reduced ASK7-mediated phosphorylation; when
FT associated with A-85, A-86, A-89 and A-91."
FT /evidence="ECO:0000269|PubMed:30429609"
FT MUTAGEN 89
FT /note="S->A: Reduced ASK7-mediated phosphorylation; when
FT associated with A-85, A-86, A-87 and A-91. Abrogated
FT MPK3/MPK6-mediated phosphorylation and abnormal nuclear
FT retention associated with impaired cortical polar
FT accumulation; when associated with A-145, A-168, A-235 and
FT A-246. Reduced interaction with YDA and fails to induce
FT polarization; when associated with A-72, A-145, A-168, A-
FT 235 and A-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029, ECO:0000269|PubMed:30429609"
FT MUTAGEN 89
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-72, D-145, D-168, D-235 and D-246. In
FT BASL_14D; reduced mobility leading to severely retarded
FT recovery at the cell cortex and prolonged accumulation even
FT in mature pavement cells, and impaired stomatal production
FT due to suppressed SLGC division potential; when associated
FT with D-72."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 91
FT /note="T->A: Reduced ASK7-mediated phosphorylation; when
FT associated with A-85, A-86, A-87 and A-89."
FT /evidence="ECO:0000269|PubMed:30429609"
FT MUTAGEN 145
FT /note="S->A: Abrogated MPK3/MPK6-mediated phosphorylation
FT and abnormal nuclear retention associated with impaired
FT cortical polar accumulation; when associated with A-89, A-
FT 168, A-235 and A-246. Reduced interaction with YDA and
FT fails to induce polarization; when associated with A-72, A-
FT 89, A-168, A-235 and A-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 145
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-72, D-89, D-168, D-235 and D-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 168
FT /note="S->A: Abrogated MPK3/MPK6-mediated phosphorylation
FT and abnormal nuclear retention associated with impaired
FT cortical polar accumulation; when associated with A-89, A-
FT 145, A-235 and A-246. Reduced interaction with YDA and
FT fails to induce polarization; when associated with A-72, A-
FT 89, A-145, A-235 and A-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 168
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-72, D-89, D-145, D-235 and D-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 222..262
FT /note="Missing: In BASL_d41; impaired polarization at the
FT cell cortex but accumulation in cytoplasm and nucleus.
FT Cannot complement disruption phenotype."
FT /evidence="ECO:0000269|PubMed:27422992"
FT MUTAGEN 223..225
FT /note="FAF->AAA: In BASL-def; impaired cortical polar
FT accumulation and stomata defects, reduced interaction with
FT YDA and fails to induce polarization; when associated with
FT 69-ASA-71 and 253-AAA-255."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27422992"
FT MUTAGEN 235
FT /note="S->A: Abrogated MPK3/MPK6-mediated phosphorylation
FT and abnormal nuclear retention associated with impaired
FT cortical polar accumulation; when associated with A-89, A-
FT 145, A-168 and A-246. Reduced interaction with YDA and
FT fails to induce polarization; when associated with A-72, A-
FT 89, A-145, A-168 and A-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 235
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-72, D-89, D-145, D-168 and D-246."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 246
FT /note="S->A: Abrogated MPK3/MPK6-mediated phosphorylation
FT and abnormal nuclear retention associated with impaired
FT cortical polar accumulation; when associated with A-89, A-
FT 145, A-168 and A-235. Reduced interaction with YDA and
FT fails to induce polarization; when associated with A-72, A-
FT 89, A-145, A-168 and A-235."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 246
FT /note="S->D: In BASL_123456D; phosphomimetic, increased
FT interaction with YDA and promoted polarization; when
FT associated with D-72, D-89, D-145, D-168 and D-235."
FT /evidence="ECO:0000269|PubMed:25843888,
FT ECO:0000269|PubMed:27746029"
FT MUTAGEN 253..255
FT /note="VAL->AAA: In basl-d2; impaired cortical polar
FT accumulation and stomata defects, reduced interaction with
FT YDA and fails to induce polarization; when associated with
FT 69-ASA-71 and 223-AAA-225."
FT /evidence="ECO:0000269|PubMed:25843888"
SQ SEQUENCE 262 AA; 29123 MW; 11EF8972A4AB97E2 CRC64;
MASQWTIPKL VTWRVRDWAS CFLACKIPLD GDEDGANNNG NTTNNNNLTF KRIKRKIKST
KKKRSERKLS LSPPGTRHHH LHLRSSSVSP TTSGSQHRRL SWPQPPVSEE SGFIVFCFDR
EDGGFDVVKE GKQEKKETES SSEKSPRTVN RKLIYGDQGV GGTEKNNSPE TKGTEQDQND
NTSCQGTKDV SSDVTERTKE EEDIDASDKS SGSSHSDEGR GSFAFPILGV EWMGSPAKMP
ESDDLSPKKQ KPVALGFQCC RF
