PYL3_ARATH
ID PYL3_ARATH Reviewed; 209 AA.
AC Q9SSM7; Q5XVG2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Abscisic acid receptor PYL3;
DE AltName: Full=PYR1-like protein 3;
DE AltName: Full=Regulatory components of ABA receptor 13;
GN Name=PYL3; Synonyms=RCAR13; OrderedLocusNames=At1g73000; ORFNames=F3N23.20;
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 GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP INTERACTION WITH HAB1; ABI1 AND ABI2.
RX PubMed=19898420; DOI=10.1038/nature08613;
RA Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M.,
RA Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J.,
RA Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F.,
RA Cutler S.R., Zhu J.-K., Xu H.E.;
RT "A gate-latch-lock mechanism for hormone signalling by abscisic acid
RT receptors.";
RL Nature 462:602-608(2009).
RN [6]
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 FUNCTION, MONOMER AND HOMODIMER, 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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 21-209 IN COMPLEX WITH ABA,
RP FUNCTION, MUTAGENESIS OF PHE-81; VAL-134; ASN-180; SER-195; VAL-202;
RP ILE-203 AND THR-209, INTERACTION WITH HAB1, AND INHIBITION BY PYRABACTIN.
RX PubMed=22579247; DOI=10.1016/j.str.2012.02.019;
RA Zhang X., Zhang Q., Xin Q., Yu L., Wang Z., Wu W., Jiang L., Wang G.,
RA Tian W., Deng Z., Wang Y., Liu Z., Long J., Gong Z., Chen Z.;
RT "Complex structures of the abscisic acid receptor PYL3/RCAR13 reveal a
RT unique regulatory mechanism.";
RL Structure 20:780-790(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 21-209 IN COMPLEX WITH ABA,
RP FUNCTION, MUTAGENESIS OF LYS-79; PHE-81; VAL-134; HIS-139; TYR-144;
RP PHE-188; VAL-192 AND 192-VAL-VAL-193, INTERACTION WITH ABA AND HAB1, AND
RP 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).
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) when
CC activated by ABA (PubMed:22579247, PubMed:23844015, PubMed:21658606).
CC Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).
CC {ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:22579247,
CC ECO:0000269|PubMed:23844015}.
CC -!- SUBUNIT: Homodimer and monomer (PubMed:21658606). Binds ABA on one
CC subunit only. ABA-binding favors monomer and trans-homodimer
CC intermediate, and increases PP2C inhibitor activity (PubMed:22579247,
CC PubMed:23844015). Binds both (-)-ABA and (+)-ABA (PubMed:23844015).
CC Binds to CARs protein in an ABA-independent manner, both at the plasma
CC membrane and in the nucleus (By similarity). Interacts with HAB1, ABI1
CC and ABI2, and possibly with other PP2Cs (PubMed:19407142,
CC PubMed:19898420, PubMed:22579247, PubMed:23844015).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:22579247, ECO:0000269|PubMed:23844015}.
CC -!- INTERACTION:
CC Q9SSM7; P49597: ABI1; NbExp=5; IntAct=EBI-2363144, EBI-782526;
CC Q9SSM7; O04719-1: ABI2; NbExp=2; IntAct=EBI-2363144, EBI-15803514;
CC Q9SSM7; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363144, EBI-1573499;
CC Q9SSM7; Q9ZW21: At2g29380; NbExp=3; IntAct=EBI-2363144, EBI-4441103;
CC Q9SSM7; Q9CAJ0: HAB1; NbExp=10; IntAct=EBI-2363144, EBI-2309302;
CC Q9SSM7; Q9SSM7: PYL3; NbExp=8; IntAct=EBI-2363144, EBI-2363144;
CC Q9SSM7; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363144, EBI-4426178;
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 -!- 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:O80992}.
CC -!- MISCELLANEOUS: The synthetic growth inhibitor pyrabactin inhibits ABA-
CC binding and subsequent PP2Cs inhibitor properties.
CC {ECO:0000269|PubMed:22579247}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU44430.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC008017; AAD55647.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35402.1; -; Genomic_DNA.
DR EMBL; AY924726; AAX23801.1; -; Genomic_DNA.
DR EMBL; AY735560; AAU44430.1; ALT_SEQ; mRNA.
DR PIR; D96755; D96755.
DR RefSeq; NP_177443.1; NM_105958.3.
DR PDB; 3KLX; X-ray; 2.50 A; A/B=1-209.
DR PDB; 3OJI; X-ray; 1.84 A; A/B=21-209.
DR PDB; 4DS8; X-ray; 2.21 A; A=1-209.
DR PDB; 4DSB; X-ray; 2.70 A; A/B=24-209.
DR PDB; 4DSC; X-ray; 1.95 A; A/B=25-209.
DR PDB; 4JDA; X-ray; 2.65 A; A/B/C/D=21-209.
DR PDB; 5JO1; X-ray; 2.30 A; A=24-205.
DR PDB; 5JO2; X-ray; 2.42 A; A=24-205.
DR PDBsum; 3KLX; -.
DR PDBsum; 3OJI; -.
DR PDBsum; 4DS8; -.
DR PDBsum; 4DSB; -.
DR PDBsum; 4DSC; -.
DR PDBsum; 4JDA; -.
DR PDBsum; 5JO1; -.
DR PDBsum; 5JO2; -.
DR AlphaFoldDB; Q9SSM7; -.
DR SMR; Q9SSM7; -.
DR BioGRID; 28850; 9.
DR ComplexPortal; CPX-3563; PYL3 ABA receptor complex.
DR DIP; DIP-53477N; -.
DR IntAct; Q9SSM7; 17.
DR STRING; 3702.AT1G73000.1; -.
DR PaxDb; Q9SSM7; -.
DR PRIDE; Q9SSM7; -.
DR ProteomicsDB; 226010; -.
DR EnsemblPlants; AT1G73000.1; AT1G73000.1; AT1G73000.
DR GeneID; 843631; -.
DR Gramene; AT1G73000.1; AT1G73000.1; AT1G73000.
DR KEGG; ath:AT1G73000; -.
DR Araport; AT1G73000; -.
DR TAIR; locus:2032738; AT1G73000.
DR eggNOG; ENOG502QU62; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q9SSM7; -.
DR OMA; PIIRTHH; -.
DR OrthoDB; 1267148at2759; -.
DR PhylomeDB; Q9SSM7; -.
DR EvolutionaryTrace; Q9SSM7; -.
DR PRO; PR:Q9SSM7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSM7; baseline and differential.
DR Genevisible; Q9SSM7; 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:0062049; C:protein phosphatase inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0010427; F:abscisic acid binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS: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 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 Membrane; Nucleus; Protein phosphatase inhibitor; Receptor;
KW Reference proteome.
FT CHAIN 1..209
FT /note="Abscisic acid receptor PYL3"
FT /id="PRO_0000391738"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..205
FT /note="START-like"
FT MOTIF 109..113
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 139..141
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 79
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:22579247,
FT ECO:0000269|PubMed:23844015, ECO:0007744|PDB:4DS8,
FT ECO:0007744|PDB:4DSB, ECO:0007744|PDB:4DSC,
FT ECO:0007744|PDB:4JDA"
FT BINDING 113..118
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 140..146
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:22579247,
FT ECO:0007744|PDB:4DSC"
FT BINDING 170
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 112
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 181
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 189
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 195
FT /note="Involved in the cis- to trans-homodimer conformation
FT in the presence of ABA"
FT /evidence="ECO:0000269|PubMed:22579247"
FT MUTAGEN 79
FT /note="K->A: Impaired HAB1-binding and lost HAB1-inhibition
FT in the presence of (-)-ABA, but normal HAB1-inhibition in
FT the presence of (+)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 81
FT /note="F->A: Impaired HAB1-binding and lost HAB1-inhibition
FT in the presence of (-)-ABA, but normal HAB1-inhibition in
FT the presence of (+)-ABA. Impaired trans-homodimerization;
FT when associated with A-202 and A-203."
FT /evidence="ECO:0000269|PubMed:22579247,
FT ECO:0000269|PubMed:23844015"
FT MUTAGEN 134
FT /note="V->I: Increased PP2C inhibitory activity in the
FT presence of (+)-ABA but reduced PP2C inhibitory activity in
FT the presence of (-)-ABA."
FT /evidence="ECO:0000269|PubMed:22579247,
FT ECO:0000269|PubMed:23844015"
FT MUTAGEN 139
FT /note="H->A: Impaired HAB1-binding and lost HAB1-inhibition
FT in the presence of (-)-ABA, but normal HAB1-inhibition in
FT the presence of (+)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 144
FT /note="Y->A: Impaired HAB1-binding and lost HAB1-inhibition
FT in the presence of (-)-ABA, but normal HAB1-inhibition in
FT the presence of (+)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 180
FT /note="N->C: Formation of trans-homodimer only in the
FT presence of ABA under non-reducing conditions with
FT disulfide bond formation; when associated with C-209."
FT /evidence="ECO:0000269|PubMed:22579247"
FT MUTAGEN 188
FT /note="F->A: Impaired HAB1-binding and lost HAB1-inhibition
FT in the presence of (-)-ABA, but normal HAB1-inhibition in
FT the presence of (+)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 192..193
FT /note="VV->AA: Impaired HAB1-binding and lost HAB1-
FT inhibition in the presence of (-)-ABA, but normal HAB1-
FT inhibition in the presence of (+)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 192
FT /note="V->L: Reduced PP2C inhibitory activity (-)-ABA."
FT /evidence="ECO:0000269|PubMed:23844015"
FT MUTAGEN 195
FT /note="S->L: Maintenance of cis-homodimer in the presence
FT of ABA."
FT /evidence="ECO:0000269|PubMed:22579247"
FT MUTAGEN 202
FT /note="V->AA: Impaired trans-homodimerization; when
FT associated with A-81 and A-203."
FT /evidence="ECO:0000269|PubMed:22579247"
FT MUTAGEN 203
FT /note="I->AA: Impaired trans-homodimerization; when
FT associated with A-81 and A-202."
FT /evidence="ECO:0000269|PubMed:22579247"
FT MUTAGEN 209
FT /note="T->C: Formation of trans-homodimer only in the
FT presence of ABA under non-reducing conditions with
FT disulfide bond formation; when associated with C-180."
FT /evidence="ECO:0000269|PubMed:22579247"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3KLX"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:3OJI"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3OJI"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 109..124
FT /evidence="ECO:0007829|PDB:3OJI"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3OJI"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:3OJI"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:5JO2"
FT STRAND 162..175
FT /evidence="ECO:0007829|PDB:3OJI"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:3OJI"
SQ SEQUENCE 209 AA; 23291 MW; 4A25A6E47D469890 CRC64;
MNLAPIHDPS SSSTTTTSSS TPYGLTKDEF STLDSIIRTH HTFPRSPNTC TSLIAHRVDA
PAHAIWRFVR DFANPNKYKH FIKSCTIRVN GNGIKEIKVG TIREVSVVSG LPASTSVEIL
EVLDEEKRIL SFRVLGGEHR LNNYRSVTSV NEFVVLEKDK KKRVYSVVLE SYIVDIPQGN
TEEDTRMFVD TVVKSNLQNL AVISTASPT
