PYL8_ARATH
ID PYL8_ARATH Reviewed; 188 AA.
AC Q9FGM1; Q0WRI3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Abscisic acid receptor PYL8 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469};
DE AltName: Full=ABI1-binding protein 1 {ECO:0000303|PubMed:19874541};
DE AltName: Full=PYR1-like protein 8 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469};
DE AltName: Full=Regulatory components of ABA receptor 3 {ECO:0000303|PubMed:19407143};
GN Name=PYL8 {ECO:0000303|PubMed:19407142, ECO:0000303|PubMed:19624469};
GN Synonyms=ABIP1 {ECO:0000303|PubMed:19874541},
GN RCAR3 {ECO:0000303|PubMed:19407143};
GN OrderedLocusNames=At5g53160 {ECO:0000312|Araport:AT5G53160};
GN ORFNames=MFH8.10 {ECO:0000312|EMBL:BAB08419.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH HAB1.
RX PubMed=19624469; DOI=10.1111/j.1365-313x.2009.03981.x;
RA Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F.,
RA Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.;
RT "Modulation of drought resistance by the abscisic acid receptor PYL5
RT through inhibition of clade A PP2Cs.";
RL Plant J. 60:575-588(2009).
RN [6]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=19407143; DOI=10.1126/science.1172408;
RA Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
RA Grill E.;
RT "Regulators of PP2C phosphatase activity function as abscisic acid
RT sensors.";
RL Science 324:1064-1068(2009).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19407142; DOI=10.1126/science.1173041;
RA Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
RA Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D.,
RA Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P.,
RA Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
RT "Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family
RT of START proteins.";
RL Science 324:1068-1071(2009).
RN [8]
RP FUNCTION, AND INTERACTION WITH ABI1 AND ABI2.
RX PubMed=19769575; DOI=10.1111/j.1365-313x.2009.04025.x;
RA Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A.,
RA Assaad F.F., Christmann A., Grill E.;
RT "Closely related receptor complexes differ in their ABA selectivity and
RT sensitivity.";
RL Plant J. 61:25-35(2010).
RN [9]
RP INTERACTION WITH ABI1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19889877; DOI=10.1104/pp.109.146381;
RA Saavedra X., Modrego A., Rodriguez D., Gonzalez-Garcia M.P., Sanz L.,
RA Nicolas G., Lorenzo O.;
RT "The nuclear interactor PYL8/RCAR3 of Fagus sylvatica FsPP2C1 is a positive
RT regulator of abscisic acid signaling in seeds and stress.";
RL Plant Physiol. 152:133-150(2010).
RN [11]
RP FUNCTION, MONOMER, AND GENE FAMILY.
RX PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
RA Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F.,
RA Yan N.;
RT "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass
RT of PYL proteins.";
RL Mol. Cell 42:662-672(2011).
RN [12]
RP INTERACTION WITH AIP1, AND SUBCELLULAR LOCATION.
RX PubMed=22404835; DOI=10.1016/j.plantsci.2012.01.013;
RA Lim C.W., Kim J.H., Baek W., Kim B.S., Lee S.C.;
RT "Functional roles of the protein phosphatase 2C, AtAIP1, in abscisic acid
RT signaling and sugar tolerance in Arabidopsis.";
RL Plant Sci. 187:83-88(2012).
RN [13]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=23844015; DOI=10.1371/journal.pone.0067477;
RA Zhang X., Jiang L., Wang G., Yu L., Zhang Q., Xin Q., Wu W., Gong Z.,
RA Chen Z.;
RT "Structural insights into the abscisic acid stereospecificity by the ABA
RT receptors PYR/PYL/RCAR.";
RL PLoS ONE 8:E67477-E67477(2013).
RN [14]
RP INTERACTION WITH DDA1, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=24563205; DOI=10.1105/tpc.113.122234;
RA Irigoyen M.L., Iniesto E., Rodriguez L., Puga M.I., Yanagawa Y., Pick E.,
RA Strickland E., Paz-Ares J., Wei N., De Jaeger G., Rodriguez P.L.,
RA Deng X.W., Rubio V.;
RT "Targeted degradation of abscisic acid receptors is mediated by the
RT ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.";
RL Plant Cell 26:712-728(2014).
RN [15]
RP INTERACTION WITH CAR1 AND CAR4, AND SUBCELLULAR LOCATION.
RX PubMed=25465408; DOI=10.1105/tpc.114.129973;
RA Rodriguez L., Gonzalez-Guzman M., Diaz M., Rodrigues A.,
RA Izquierdo-Garcia A.C., Peirats-Llobet M., Fernandez M.A., Antoni R.,
RA Fernandez D., Marquez J.A., Mulet J.M., Albert A., Rodriguez P.L.;
RT "C2-domain abscisic acid-related proteins mediate the interaction of
RT PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate
RT abscisic acid sensitivity in Arabidopsis.";
RL Plant Cell 26:4802-4820(2014).
RN [16]
RP FUNCTION, INTERACTION WITH MYB44; MYB73 AND MYB77, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24894996; DOI=10.1126/scisignal.2005051;
RA Zhao Y., Xing L., Wang X., Hou Y.J., Gao J., Wang P., Duan C.G., Zhu X.,
RA Zhu J.K.;
RT "The ABA receptor PYL8 promotes lateral root growth by enhancing MYB77-
RT dependent transcription of auxin-responsive genes.";
RL Sci. Signal. 7:RA53-RA53(2014).
RN [17]
RP INTERACTION WITH CARK1 AND ABI1, PHOSPHORYLATION AT THR-77, MUTAGENESIS OF
RP THR-77, PTM, AND SUBCELLULAR LOCATION.
RX PubMed=29928509; DOI=10.1038/s41421-018-0029-y;
RA Zhang L., Li X., Li D., Sun Y., Li Y., Luo Q., Liu Z., Wang J., Li X.,
RA Zhang H., Lou Z., Yang Y.;
RT "CARK1 mediates ABA signaling by phosphorylation of ABA receptors.";
RL Cell Discov. 4:30-30(2018).
CC -!- FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated
CC responses such as stomatal closure and germination inhibition. Inhibits
CC the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-
CC independent manner but more efficiently when activated by ABA. Confers
CC enhanced sensitivity to ABA (PubMed:19407143, PubMed:19624469,
CC PubMed:19769575, PubMed:19889877, PubMed:23844015, PubMed:21658606).
CC Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).
CC Mediates crosstalk between ABA and auxin signaling to regulate lateral
CC root growth. Required for lateral root growth suppression by ABA. In
CC response to auxin, promotes lateral root growth by enhancing MYB77-
CC dependent transcription of the auxin-responsive gene IAA19. Enhances
CC the abilities of MYB44 and MYB73 to activate IAA19 gene
CC (PubMed:24894996). {ECO:0000269|PubMed:19407143,
CC ECO:0000269|PubMed:19624469, ECO:0000269|PubMed:19769575,
CC ECO:0000269|PubMed:19889877, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015, ECO:0000269|PubMed:24894996}.
CC -!- SUBUNIT: Monomer (PubMed:21658606). Homodimer. Binds ABA on one subunit
CC only (By similarity). interacts with ABI1 and HAB1, and possibly with
CC other PP2Cs (PubMed:19624469, PubMed:19769575, PubMed:19874541). Binds
CC to CARs protein in an ABA-independent manner, both at the plasma
CC membrane and in the nucleus. Interacts directly with CAR1 and CAR4
CC (PubMed:25465408). Interacts with MYB44, MYB73 and MYB77 in an ABA-
CC independent manner (PubMed:24894996). Interacts with DDA1
CC (PubMed:24563205). Interacts with CARK1 in the cytosol
CC (PubMed:29928509). Binds to ABI1 when phosphorylated by CARK1
CC (PubMed:29928509, PubMed:19624469, PubMed:19769575, PubMed:19874541,
CC PubMed:21658606, PubMed:24563205, PubMed:24894996, PubMed:25465408) (By
CC similarity). Interacts with AIP1 in the nucleus (PubMed:22404835).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19624469,
CC ECO:0000269|PubMed:19769575, ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:22404835,
CC ECO:0000269|PubMed:24563205, ECO:0000269|PubMed:24894996,
CC ECO:0000269|PubMed:25465408, ECO:0000269|PubMed:29928509}.
CC -!- INTERACTION:
CC Q9FGM1; P49597: ABI1; NbExp=7; IntAct=EBI-2429535, EBI-782526;
CC Q9FGM1; O04719: ABI2; NbExp=3; IntAct=EBI-2429535, EBI-537680;
CC Q9FGM1; Q9LNW3: AIP1; NbExp=9; IntAct=EBI-2429535, EBI-1573499;
CC Q9FGM1; Q93WK5: APRR7; NbExp=3; IntAct=EBI-2429535, EBI-25528701;
CC Q9FGM1; Q9ZW21: At2g29380; NbExp=7; IntAct=EBI-2429535, EBI-4441103;
CC Q9FGM1; Q9SZE1: At4g29120; NbExp=3; IntAct=EBI-2429535, EBI-25528671;
CC Q9FGM1; Q9C7T4: BHLH96; NbExp=3; IntAct=EBI-2429535, EBI-15192637;
CC Q9FGM1; Q9CAJ0: HAB1; NbExp=7; IntAct=EBI-2429535, EBI-2309302;
CC Q9FGM1; Q9LNP9: HAB2; NbExp=5; IntAct=EBI-2429535, EBI-15803614;
CC Q9FGM1; Q8H174: IAA31; NbExp=3; IntAct=EBI-2429535, EBI-3946408;
CC Q9FGM1; Q9FDW1: MYB44; NbExp=5; IntAct=EBI-2429535, EBI-15192813;
CC Q9FGM1; O22179: MYB70; NbExp=5; IntAct=EBI-2429535, EBI-1238013;
CC Q9FGM1; O23160: MYB73; NbExp=5; IntAct=EBI-2429535, EBI-25506855;
CC Q9FGM1; Q9SN12: MYB77; NbExp=4; IntAct=EBI-2429535, EBI-2324225;
CC Q9FGM1; Q9FIF5: SAG113; NbExp=5; IntAct=EBI-2429535, EBI-2363373;
CC Q9FGM1; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2429535, EBI-4426144;
CC Q9FGM1; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2429535, EBI-4426178;
CC Q9FGM1; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2429535, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}.
CC Cytoplasm {ECO:0000269|PubMed:19889877, ECO:0000269|PubMed:22404835}.
CC Nucleus {ECO:0000269|PubMed:19889877, ECO:0000269|PubMed:22404835,
CC ECO:0000269|PubMed:24563205, ECO:0000269|PubMed:25465408}. Cell
CC membrane {ECO:0000269|PubMed:25465408}. Note=Localizes at the plasma
CC membrane in the presence of a CAR protein (e.g. CAR1 and CAR4).
CC {ECO:0000269|PubMed:25465408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FGM1-1; Sequence=Displayed;
CC -!- INDUCTION: Down-regulated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:24894996}.
CC -!- DOMAIN: Upon interaction with ABA, the 'latch' and 'gate' loops change
CC in conformation leading to a tight dimerization and the creation a
CC surface that enables the receptor to dock into and inhibit the PP2C
CC active site. {ECO:0000250|UniProtKB:Q8VZS8}.
CC -!- PTM: Phosphorylated by CARK1 especially in response to abscisic acid
CC (ABA); this phosphorylation promotes its stability and inhibitory
CC ability to ABI1. {ECO:0000269|PubMed:29928509}.
CC -!- PTM: Ubiquitinated in DDA1- and CDD complex-dependent manner
CC (PubMed:24563205). Ubiquitination leads to its subsequent proteasomal
CC degradation (PubMed:24563205). {ECO:0000269|PubMed:24563205}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit enhanced sensitivity of
CC lateral root inhibition by abscisic acid (ABA), and reduced suppression
CC of primary root growth by ABA. {ECO:0000269|PubMed:24894996}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AB025622; BAB08419.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96316.1; -; Genomic_DNA.
DR EMBL; BT003112; AAO24544.1; -; mRNA.
DR EMBL; AK228324; BAF00266.1; -; mRNA.
DR RefSeq; NP_200128.1; NM_124695.4. [Q9FGM1-1]
DR AlphaFoldDB; Q9FGM1; -.
DR SMR; Q9FGM1; -.
DR BioGRID; 20642; 27.
DR IntAct; Q9FGM1; 19.
DR MINT; Q9FGM1; -.
DR STRING; 3702.AT5G53160.2; -.
DR iPTMnet; Q9FGM1; -.
DR PaxDb; Q9FGM1; -.
DR PRIDE; Q9FGM1; -.
DR ProteomicsDB; 226013; -. [Q9FGM1-1]
DR EnsemblPlants; AT5G53160.2; AT5G53160.2; AT5G53160. [Q9FGM1-1]
DR GeneID; 835397; -.
DR Gramene; AT5G53160.2; AT5G53160.2; AT5G53160. [Q9FGM1-1]
DR KEGG; ath:AT5G53160; -.
DR Araport; AT5G53160; -.
DR TAIR; locus:2163731; AT5G53160.
DR eggNOG; ENOG502QPYH; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q9FGM1; -.
DR OMA; HILCIRI; -.
DR PhylomeDB; Q9FGM1; -.
DR PRO; PR:Q9FGM1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGM1; baseline and differential.
DR Genevisible; Q9FGM1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR019587; Polyketide_cyclase/dehydratase.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF10604; Polyketide_cyc2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cell membrane;
KW Cytoplasm; Disulfide bond; Membrane; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Receptor; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..188
FT /note="Abscisic acid receptor PYL8"
FT /id="PRO_0000391743"
FT REGION 25..176
FT /note="START-like"
FT MOTIF 85..89
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 115..117
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 61
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 89..94
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 116..122
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 141
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 62
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 88
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 108
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 152
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 160
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 163
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT MOD_RES 77
FT /note="Phosphothreonine; by CARK1"
FT /evidence="ECO:0000269|PubMed:29928509"
FT DISULFID 32..157
FT /note="Reversible"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT MUTAGEN 77
FT /note="T->A: Reduced CARK1-mediated phosphorylation and
FT lower affinity for ABI1."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 77
FT /note="T->D: Phosphomimetic; increased affinity for ABI1
FT and constitutive abscisic acid (ABA) sensitivity."
FT /evidence="ECO:0000269|PubMed:29928509"
FT CONFLICT 6
FT /note="I -> F (in Ref. 4; BAF00266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21397 MW; D3436ADAC890AEED CRC64;
MEANGIENLT NPNQEREFIR RHHKHELVDN QCSSTLVKHI NAPVHIVWSL VRRFDQPQKY
KPFISRCVVK GNMEIGTVRE VDVKSGLPAT RSTERLELLD DNEHILSIRI VGGDHRLKNY
SSIISLHPET IEGRIGTLVI ESFVVDVPEG NTKDETCYFV EALIKCNLKS LADISERLAV
QDTTESRV
