PYL11_ARATH
ID PYL11_ARATH Reviewed; 161 AA.
AC Q9FJ50;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Abscisic acid receptor PYL11;
DE AltName: Full=PYR1-like protein 11;
DE AltName: Full=Regulatory components of ABA receptor 5;
GN Name=PYL11; Synonyms=RCAR5; OrderedLocusNames=At5g45860; ORFNames=K15I22.6;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 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 [6]
RP FUNCTION, AND INTERACTION WITH I-2 AND 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).
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 (By similarity). Suppresses the phosphatase activity
CC of TOPP1 in a dose-dependent manner in vitro (PubMed:26943172).
CC {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:26943172}.
CC -!- SUBUNIT: Homodimer. Binds ABA on one subunit only. Interacts with
CC PP2Cs. Binds to CARs protein in an ABA-independent manner, both at the
CC plasma membrane and in the nucleus (By similarity). Interacts with I-2
CC and TOPP1 (PubMed:26943172). {ECO:0000250|UniProtKB:O49686,
CC ECO:0000269|PubMed:26943172}.
CC -!- INTERACTION:
CC Q9FJ50; P49597: ABI1; NbExp=3; IntAct=EBI-2363233, EBI-782526;
CC Q9FJ50; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-2363233, EBI-1573499;
CC Q9FJ50; Q9ZW21: At2g29380; NbExp=7; IntAct=EBI-2363233, EBI-4441103;
CC Q9FJ50; Q9CAJ0: HAB1; NbExp=4; IntAct=EBI-2363233, EBI-2309302;
CC Q9FJ50; Q9SN12: MYB77; NbExp=3; IntAct=EBI-2363233, EBI-2324225;
CC Q9FJ50; Q8H157: NPF4.6; NbExp=3; IntAct=EBI-2363233, EBI-4433263;
CC Q9FJ50; Q9LT89: TCP19; NbExp=3; IntAct=EBI-2363233, 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:Q8VZS8}.
CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular
CC receptor family. {ECO:0000305}.
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DR EMBL; AB016870; BAB09314.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95308.1; -; Genomic_DNA.
DR RefSeq; NP_199398.1; NM_123954.2.
DR AlphaFoldDB; Q9FJ50; -.
DR SMR; Q9FJ50; -.
DR BioGRID; 19875; 10.
DR IntAct; Q9FJ50; 7.
DR STRING; 3702.AT5G45860.1; -.
DR PaxDb; Q9FJ50; -.
DR PRIDE; Q9FJ50; -.
DR ProteomicsDB; 226008; -.
DR EnsemblPlants; AT5G45860.1; AT5G45860.1; AT5G45860.
DR GeneID; 834626; -.
DR Gramene; AT5G45860.1; AT5G45860.1; AT5G45860.
DR KEGG; ath:AT5G45860; -.
DR Araport; AT5G45860; -.
DR TAIR; locus:2152420; AT5G45860.
DR eggNOG; ENOG502RY2P; Eukaryota.
DR HOGENOM; CLU_077517_2_0_1; -.
DR InParanoid; Q9FJ50; -.
DR OMA; LPNQCGS; -.
DR OrthoDB; 1432499at2759; -.
DR PhylomeDB; Q9FJ50; -.
DR PRO; PR:Q9FJ50; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ50; baseline and differential.
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; 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; ISS:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; ISS: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 Abscisic acid signaling pathway; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Protein phosphatase inhibitor; Receptor; Reference proteome.
FT CHAIN 1..161
FT /note="Abscisic acid receptor PYL11"
FT /id="PRO_0000391746"
FT REGION 3..154
FT /note="START-like"
FT MOTIF 64..68
FT /note="Gate loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT MOTIF 94..96
FT /note="Latch loop"
FT /evidence="ECO:0000250|UniProtKB:Q8VZS8"
FT BINDING 39
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 68..73
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 95..101
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT BINDING 119
FT /ligand="abscisate"
FT /ligand_id="ChEBI:CHEBI:62432"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 67
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
FT SITE 87
FT /note="Involved in ABA binding"
FT /evidence="ECO:0000250|UniProtKB:Q84MC7"
FT SITE 130
FT /note="Involved in interactions with PP2Cs"
FT /evidence="ECO:0000250|UniProtKB:O49686"
SQ SEQUENCE 161 AA; 17805 MW; C2DC792735D5F200 CRC64;
METSQKYHTC GSTLVQTIDA PLSLVWSILR RFDNPQAYKQ FVKTCNLSSG DGGEGSVREV
TVVSGLPAEF SRERLDELDD ESHVMMISII GGDHRLVNYR SKTMAFVAAD TEEKTVVVES
YVVDVPEGNS EEETTSFADT IVGFNLKSLA KLSERVAHLK L
