PYL2_ARATH
ID PYL2_ARATH Reviewed; 190 AA.
AC O80992;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Abscisic acid receptor PYL2;
DE AltName: Full=PYR1-like protein 2;
DE AltName: Full=Regulatory components of ABA receptor 14;
GN Name=PYL2; Synonyms=RCAR14; OrderedLocusNames=At2g26040;
GN ORFNames=T19L18.15;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
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 [5]
RP FUNCTION, MUTAGENESIS OF VAL-87 AND ILE-88, 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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-188 IN COMPLEX WITH ABSCISIC
RP ACID AND PP2C HAB1, DIMERIZATION, FUNCTION, INTERACTION WITH HAB1; ABI1 AND
RP ABI2, GATE AND LATCH MOTIFS, MUTAGENESIS OF LYS-64; VAL-87; GLY-90; LEU-91;
RP ALA-93; GLU-98; TYR-124; GLU-147; VAL-151 AND ASN-173, AND DOMAIN.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) ALONE AND IN COMPLEX WITH ABSCISIC
RP ACID, FUNCTION, INTERACTION WITH ABI1, AND MUTAGENESIS OF LYS-64.
RX PubMed=19893533; DOI=10.1038/nsmb.1730;
RA Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J.,
RA Yan N.;
RT "Structural insights into the mechanism of abscisic acid signaling by PYL
RT proteins.";
RL Nat. Struct. Mol. Biol. 16:1230-1236(2009).
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:19893533, PubMed:19898420, PubMed:23844015,
CC PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA
CC (PubMed:23844015). {ECO:0000269|PubMed:19893533,
CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:23844015}.
CC -!- SUBUNIT: Homodimer (PubMed:19898420, PubMed:21658606). Binds ABA on one
CC subunit only. Interacts with HAB1, ABI1 and ABI2, and possibly with
CC other PP2Cs (PubMed:19407142, PubMed:19893533, PubMed:19898420). Binds
CC to CARs protein in an ABA-independent manner, both at the plasma
CC membrane and in the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:19898420,
CC ECO:0000269|PubMed:21658606}.
CC -!- INTERACTION:
CC O80992; P49597: ABI1; NbExp=6; IntAct=EBI-2363125, EBI-782526;
CC O80992; O04719-1: ABI2; NbExp=3; IntAct=EBI-2363125, EBI-15803514;
CC O80992; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363125, EBI-1573499;
CC O80992; Q9CAJ0: HAB1; NbExp=10; IntAct=EBI-2363125, EBI-2309302;
CC O80992; O80992: PYL2; NbExp=4; IntAct=EBI-2363125, EBI-2363125;
CC O80992; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363125, 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:0000269|PubMed:19898420}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AC004747; AAC31232.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07788.1; -; Genomic_DNA.
DR PIR; T02619; T02619.
DR RefSeq; NP_180174.1; NM_128163.2.
DR PDB; 3KAZ; X-ray; 1.85 A; A/B/C=14-188.
DR PDB; 3KB0; X-ray; 1.95 A; A=14-188.
DR PDB; 3KB3; X-ray; 1.95 A; A=14-188.
DR PDB; 3KDH; X-ray; 1.65 A; A/B/C=1-190.
DR PDB; 3KDI; X-ray; 2.38 A; A=1-190.
DR PDB; 3KL1; X-ray; 1.55 A; A/B=1-190.
DR PDB; 3NJ0; X-ray; 1.89 A; A/B/C=1-190.
DR PDB; 3NJ1; X-ray; 1.95 A; A=1-190.
DR PDB; 3NMH; X-ray; 1.85 A; A/B/C=14-189.
DR PDB; 3NMP; X-ray; 2.10 A; A/B/C=14-189.
DR PDB; 3NMT; X-ray; 2.56 A; A=14-189.
DR PDB; 3NMV; X-ray; 2.10 A; A=14-189.
DR PDB; 3NR4; X-ray; 2.01 A; A/B/C=1-190.
DR PDB; 3NS2; X-ray; 1.63 A; A/B/C=1-190.
DR PDB; 3UJL; X-ray; 2.50 A; A=14-188.
DR PDB; 4LA7; X-ray; 1.98 A; A=1-190.
DR PDB; 4LG5; X-ray; 2.88 A; A=14-188.
DR PDB; 4LGA; X-ray; 2.70 A; A=14-188.
DR PDB; 4LGB; X-ray; 3.15 A; A=14-188.
DR PDB; 5JNN; X-ray; 2.30 A; A=1-190.
DR PDB; 5VR7; X-ray; 2.61 A; A=14-188.
DR PDB; 5VRO; X-ray; 2.26 A; A=14-188.
DR PDB; 5VS5; X-ray; 2.80 A; A=14-188.
DR PDB; 5VSQ; X-ray; 2.62 A; A=14-188.
DR PDB; 5VSR; X-ray; 2.62 A; A=14-188.
DR PDB; 5VT7; X-ray; 2.62 A; A=14-188.
DR PDBsum; 3KAZ; -.
DR PDBsum; 3KB0; -.
DR PDBsum; 3KB3; -.
DR PDBsum; 3KDH; -.
DR PDBsum; 3KDI; -.
DR PDBsum; 3KL1; -.
DR PDBsum; 3NJ0; -.
DR PDBsum; 3NJ1; -.
DR PDBsum; 3NMH; -.
DR PDBsum; 3NMP; -.
DR PDBsum; 3NMT; -.
DR PDBsum; 3NMV; -.
DR PDBsum; 3NR4; -.
DR PDBsum; 3NS2; -.
DR PDBsum; 3UJL; -.
DR PDBsum; 4LA7; -.
DR PDBsum; 4LG5; -.
DR PDBsum; 4LGA; -.
DR PDBsum; 4LGB; -.
DR PDBsum; 5JNN; -.
DR PDBsum; 5VR7; -.
DR PDBsum; 5VRO; -.
DR PDBsum; 5VS5; -.
DR PDBsum; 5VSQ; -.
DR PDBsum; 5VSR; -.
DR PDBsum; 5VT7; -.
DR AlphaFoldDB; O80992; -.
DR SMR; O80992; -.
DR BioGRID; 2497; 7.
DR ComplexPortal; CPX-3562; PYL2 ABA receptor complex.
DR DIP; DIP-48582N; -.
DR IntAct; O80992; 6.
DR STRING; 3702.AT2G26040.1; -.
DR BindingDB; O80992; -.
DR MetOSite; O80992; -.
DR PaxDb; O80992; -.
DR PRIDE; O80992; -.
DR ProteomicsDB; 226009; -.
DR EnsemblPlants; AT2G26040.1; AT2G26040.1; AT2G26040.
DR GeneID; 817145; -.
DR Gramene; AT2G26040.1; AT2G26040.1; AT2G26040.
DR KEGG; ath:AT2G26040; -.
DR Araport; AT2G26040; -.
DR TAIR; locus:2057407; AT2G26040.
DR eggNOG; ENOG502QU62; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; O80992; -.
DR OMA; MFVDTVI; -.
DR OrthoDB; 1267148at2759; -.
DR PhylomeDB; O80992; -.
DR EvolutionaryTrace; O80992; -.
DR PRO; PR:O80992; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80992; baseline and differential.
DR Genevisible; O80992; 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; ISS: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; 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 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..190
FT /note="Abscisic acid receptor PYL2"
FT /id="PRO_0000391737"
FT REGION 28..182
FT /note="START-like"
FT MOTIF 89..93
FT /note="Gate loop"
FT /evidence="ECO:0000269|PubMed:19898420"
FT MOTIF 119..121
FT /note="Latch loop"
FT /evidence="ECO:0000269|PubMed:19898420"
FT BINDING 64
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19893533,
FT ECO:0000269|PubMed:19898420"
FT BINDING 93..98
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19893533,
FT ECO:0000269|PubMed:19898420"
FT BINDING 120..126
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19893533,
FT ECO:0000269|PubMed:19898420"
FT BINDING 147
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000269|PubMed:19893533,
FT ECO:0000269|PubMed:19898420"
FT SITE 92
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 158
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 166
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT MUTAGEN 64
FT /note="K->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19893533,
FT ECO:0000269|PubMed:19898420"
FT MUTAGEN 87
FT /note="V->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 87
FT /note="V->L: Increased constitutive inhibition of PP2C
FT phosphatase."
FT /evidence="ECO:0000269|PubMed:21658606"
FT MUTAGEN 88
FT /note="I->K: Monomer due to impaired homodimerization.
FT Increased ABA-binding affinity and increased constitutive
FT inhibition of PP2C phosphatase."
FT /evidence="ECO:0000269|PubMed:21658606"
FT MUTAGEN 90
FT /note="G->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 91
FT /note="L->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 93
FT /note="A->S: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 98
FT /note="E->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 124
FT /note="Y->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 147
FT /note="E->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 151
FT /note="V->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT MUTAGEN 173
FT /note="N->A: Impaired ABA-mediated binding to PP2Cs and
FT subsequent inhibition."
FT /evidence="ECO:0000269|PubMed:19898420"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:3KL1"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:3KL1"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 65..78
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:3KL1"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:3KL1"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:3KL1"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3NS2"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:3KL1"
FT HELIX 159..183
FT /evidence="ECO:0007829|PDB:3KL1"
SQ SEQUENCE 190 AA; 21282 MW; CBB16E64BE2B8164 CRC64;
MSSSPAVKGL TDEEQKTLEP VIKTYHQFEP DPTTCTSLIT QRIHAPASVV WPLIRRFDNP
ERYKHFVKRC RLISGDGDVG SVREVTVISG LPASTSTERL EFVDDDHRVL SFRVVGGEHR
LKNYKSVTSV NEFLNQDSGK VYTVVLESYT VDIPEGNTEE DTKMFVDTVV KLNLQKLGVA
ATSAPMHDDE
