PYL9_ARATH
ID PYL9_ARATH Reviewed; 187 AA.
AC Q84MC7; Q8LA91; Q9LNI7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Abscisic acid receptor PYL9;
DE AltName: Full=ABI1-binding protein 4;
DE AltName: Full=PYR1-like protein 9;
DE AltName: Full=Regulatory components of ABA receptor 1;
GN Name=PYL9; Synonyms=RCAR1; OrderedLocusNames=At1g01360; ORFNames=F6F3.16;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ABI1; ABI2 AND HAB1, AND
RP 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 INTERACTION WITH HAB1, 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 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 [9]
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 [10]
RP INTERACTION WITH DDA1.
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 [11]
RP INTERACTION WITH TOPP1.
RX PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT negatively regulate ABA signaling.";
RL PLoS Genet. 12:E1005835-E1005835(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH ABA, FUNCTION,
RP MUTAGENESIS OF CYS-29; CYS-34; ILE-112; CYS-159 AND LEU-165, DISULFIDE
RP BOND, INTERACTION WITH ABA, 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ABA, MUTAGENESIS OF
RP CYS-29; CYS-34 AND CYS-159, AND HOMODIMER.
RX PubMed=24645846; DOI=10.1111/gtc.12140;
RA Nakagawa M., Kagiyama M., Shibata N., Hirano Y., Hakoshima T.;
RT "Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1.";
RL Genes Cells 19:386-404(2014).
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:23844015,
CC PubMed:21658606). Can be activated only by (+)-ABA but not by (-)-ABA
CC (PubMed:23844015). {ECO:0000269|PubMed:19407143,
CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015}.
CC -!- SUBUNIT: Homodimer (PubMed:24645846). Monomer (PubMed:21658606). Binds
CC ABA on one subunit only. Binds to CARs protein in an ABA-independent
CC manner, both at the plasma membrane and in the nucleus (By similarity).
CC Binds specifically (+)-ABA but not (-)-ABA (PubMed:23844015,
CC PubMed:24645846). Interacts with HAB1, ABI1 and ABI2, and possibly with
CC other PP2Cs (PubMed:19407142, PubMed:19407143, PubMed:19874541).
CC Interacts with TOPP1 (PubMed:26943172). Interacts with DDA1
CC (PubMed:24563205). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19407143,
CC ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015, ECO:0000269|PubMed:24563205,
CC ECO:0000269|PubMed:24645846, ECO:0000269|PubMed:26943172}.
CC -!- INTERACTION:
CC Q84MC7; P49597: ABI1; NbExp=14; IntAct=EBI-2349513, EBI-782526;
CC Q84MC7; O04719: ABI2; NbExp=7; IntAct=EBI-2349513, EBI-537680;
CC Q84MC7; Q9SFD5: ADA2A; NbExp=3; IntAct=EBI-2349513, EBI-979206;
CC Q84MC7; Q9LNW3: AIP1; NbExp=9; IntAct=EBI-2349513, EBI-1573499;
CC Q84MC7; A0A178WMH3: At1g23220; NbExp=3; IntAct=EBI-2349513, EBI-25519119;
CC Q84MC7; A0A1P8AVS2: At1g72340; NbExp=3; IntAct=EBI-2349513, EBI-25528474;
CC Q84MC7; Q9ZW21: At2g29380; NbExp=8; IntAct=EBI-2349513, EBI-4441103;
CC Q84MC7; A0A384LEC9: At3g29270; NbExp=3; IntAct=EBI-2349513, EBI-25528354;
CC Q84MC7; Q8GXD8: At4g22250/T10I14_80; NbExp=3; IntAct=EBI-2349513, EBI-4427572;
CC Q84MC7; O82754: At4g23050; NbExp=3; IntAct=EBI-2349513, EBI-1238561;
CC Q84MC7; A0A384L3Q5: AXX17_At3g52590; NbExp=3; IntAct=EBI-2349513, EBI-25528525;
CC Q84MC7; Q9C7T4: BHLH96; NbExp=3; IntAct=EBI-2349513, EBI-15192637;
CC Q84MC7; Q9SAD4: ESR1; NbExp=3; IntAct=EBI-2349513, EBI-1536756;
CC Q84MC7; Q9LZL7: Fes1C; NbExp=3; IntAct=EBI-2349513, EBI-4431436;
CC Q84MC7; Q9CAJ0: HAB1; NbExp=5; IntAct=EBI-2349513, EBI-2309302;
CC Q84MC7; Q9LNP9: HAB2; NbExp=3; IntAct=EBI-2349513, EBI-15803614;
CC Q84MC7; O81027: HMGCL; NbExp=3; IntAct=EBI-2349513, EBI-4434127;
CC Q84MC7; Q9FGM9: HSP23.5; NbExp=3; IntAct=EBI-2349513, EBI-4428388;
CC Q84MC7; Q9C9X7: IDD14; NbExp=3; IntAct=EBI-2349513, EBI-15191579;
CC Q84MC7; Q9SCK1: LSU1; NbExp=3; IntAct=EBI-2349513, EBI-4424157;
CC Q84MC7; Q9FJ07: MYB111; NbExp=3; IntAct=EBI-2349513, EBI-25528560;
CC Q84MC7; O23160: MYB73; NbExp=7; IntAct=EBI-2349513, EBI-25506855;
CC Q84MC7; Q9SN12: MYB77; NbExp=8; IntAct=EBI-2349513, EBI-2324225;
CC Q84MC7; Q94F58: NAC089; NbExp=3; IntAct=EBI-2349513, EBI-2319707;
CC Q84MC7; Q9ZVL3: NFYC3; NbExp=3; IntAct=EBI-2349513, EBI-2125961;
CC Q84MC7; Q38845: PP2AA1; NbExp=3; IntAct=EBI-2349513, EBI-1645478;
CC Q84MC7; Q9XI19: PTAC6; NbExp=3; IntAct=EBI-2349513, EBI-7890412;
CC Q84MC7; O82277: TCP10; NbExp=3; IntAct=EBI-2349513, EBI-3133327;
CC Q84MC7; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-2349513, EBI-4424877;
CC Q84MC7; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2349513, EBI-4426144;
CC Q84MC7; A1YKT1: TCP18; NbExp=3; IntAct=EBI-2349513, EBI-15192731;
CC Q84MC7; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2349513, EBI-4426178;
CC Q84MC7; Q9FTA2: TCP21; NbExp=3; IntAct=EBI-2349513, EBI-4426168;
CC Q84MC7; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-2349513, EBI-25522447;
CC Q84MC7; O64647: TCP9; NbExp=3; IntAct=EBI-2349513, EBI-9838721;
CC Q84MC7; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2349513, EBI-4426557;
CC Q84MC7; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-2349513, EBI-4424568;
CC Q84MC7; Q8W4L5: VAL1; NbExp=3; IntAct=EBI-2349513, EBI-2616403;
CC Q84MC7; Q8GXA4: WIP1; NbExp=3; IntAct=EBI-2349513, EBI-1779367;
CC Q84MC7; Q9SCU5: WNK5; NbExp=3; IntAct=EBI-2349513, EBI-1807651;
CC Q84MC7; Q93WT0: WRKY31; NbExp=3; IntAct=EBI-2349513, EBI-15208488;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus
CC {ECO:0000250|UniProtKB:O49686}. Cell membrane
CC {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane
CC in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, vascular tissues, stomata,
CC flowers, pollen tubes and developing seeds.
CC {ECO:0000269|PubMed:19407143}.
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 -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM65514.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC023628; AAF97339.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE27277.1; -; Genomic_DNA.
DR EMBL; BT006399; AAP21207.1; -; mRNA.
DR EMBL; AK227623; BAE99614.1; -; mRNA.
DR EMBL; AY087967; AAM65514.1; ALT_INIT; mRNA.
DR RefSeq; NP_563626.1; NM_100018.5.
DR PDB; 3OQU; X-ray; 2.68 A; A/B=1-187.
DR PDB; 3W9R; X-ray; 1.90 A; A=1-187.
DR PDBsum; 3OQU; -.
DR PDBsum; 3W9R; -.
DR AlphaFoldDB; Q84MC7; -.
DR SMR; Q84MC7; -.
DR BioGRID; 23691; 45.
DR DIP; DIP-53480N; -.
DR IntAct; Q84MC7; 44.
DR STRING; 3702.AT1G01360.1; -.
DR PaxDb; Q84MC7; -.
DR PRIDE; Q84MC7; -.
DR ProteomicsDB; 226014; -.
DR EnsemblPlants; AT1G01360.1; AT1G01360.1; AT1G01360.
DR GeneID; 838452; -.
DR Gramene; AT1G01360.1; AT1G01360.1; AT1G01360.
DR KEGG; ath:AT1G01360; -.
DR Araport; AT1G01360; -.
DR TAIR; locus:2035227; AT1G01360.
DR eggNOG; ENOG502QPYH; Eukaryota.
DR HOGENOM; CLU_077517_0_0_1; -.
DR InParanoid; Q84MC7; -.
DR OMA; HIKAPLR; -.
DR OrthoDB; 1261133at2759; -.
DR PhylomeDB; Q84MC7; -.
DR PRO; PR:Q84MC7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84MC7; baseline and differential.
DR Genevisible; Q84MC7; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; IDA: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:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR DisProt; DP02995; -.
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 3D-structure; Abscisic acid signaling pathway; Cell membrane; Cytoplasm;
KW Disulfide bond; Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..187
FT /note="Abscisic acid receptor PYL9"
FT /id="PRO_0000391744"
FT REGION 27..178
FT /note="START-like"
FT MOTIF 87..91
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 117..119
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 63
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:23844015,
FT ECO:0000269|PubMed:24645846, ECO:0007744|PDB:3OQU,
FT ECO:0007744|PDB:3W9R"
FT BINDING 91..96
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 118..124
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 143
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 64
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000269|PubMed:24645846"
FT SITE 90
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 110
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000269|PubMed:24645846"
FT SITE 154
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 162
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000269|PubMed:24645846"
FT SITE 165
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000269|PubMed:24645846"
FT DISULFID 29..159
FT /note="Reversible"
FT /evidence="ECO:0000269|PubMed:23844015"
FT DISULFID 34..159
FT /note="Reversible"
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 29
FT /note="C->S: Stable homogeneity in reducing condition."
FT /evidence="ECO:0000269|PubMed:23844015,
FT ECO:0000269|PubMed:24645846"
FT MUTAGEN 34
FT /note="C->S: Stable homogeneity in reducing condition."
FT /evidence="ECO:0000269|PubMed:23844015,
FT ECO:0000269|PubMed:24645846"
FT MUTAGEN 112
FT /note="I->V: Increased HAB1 inhibitory ability."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 159
FT /note="C->S: Abnormal stable homogeneity in reducing
FT condition."
FT /evidence="ECO:0000269|PubMed:23844015,
FT ECO:0000269|PubMed:24645846"
FT MUTAGEN 165
FT /note="L->V: Slight potentiation of (-)-ABA-binding."
FT /evidence="ECO:0000269|PubMed:23844015"
FT CONFLICT 7
FT /note="G -> D (in Ref. 1; AAM65514)"
FT /evidence="ECO:0000305"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:3W9R"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3W9R"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:3W9R"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:3W9R"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:3W9R"
FT HELIX 155..181
FT /evidence="ECO:0007829|PDB:3W9R"
SQ SEQUENCE 187 AA; 20901 MW; 070D485311163568 CRC64;
MMDGVEGGTA MYGGLETVQY VRTHHQHLCR ENQCTSALVK HIKAPLHLVW SLVRRFDQPQ
KYKPFVSRCT VIGDPEIGSL REVNVKSGLP ATTSTERLEL LDDEEHILGI KIIGGDHRLK
NYSSILTVHP EIIEGRAGTM VIESFVVDVP QGNTKDETCY FVEALIRCNL KSLADVSERL
ASQDITQ