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Protein

Abscisic acid receptor PYL9

Gene

PYL9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-independent manner but more efficiently when activated by ABA. Confers enhanced sensitivity to ABA (PubMed:19407143, PubMed:23844015, PubMed:21658606). Can be activated only by (+)-ABA but not by (-)-ABA (PubMed:23844015).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63ABACombined sources2 Publications1
Sitei64Involved in ABA binding1 Publication1
Sitei90Involved in interactions with PP2CsBy similarity1
Sitei110Involved in ABA binding1 Publication1
Binding sitei143ABABy similarity1
Sitei154Involved in interactions with PP2CsBy similarity1
Sitei162Involved in ABA binding1 Publication1
Sitei165Involved in ABA binding1 Publication1

GO - Molecular functioni

  • abscisic acid binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase inhibitor activity Source: UniProtKB
  • receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor, Receptor

Keywords - Biological processi

Abscisic acid signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Abscisic acid receptor PYL9
Alternative name(s):
ABI1-binding protein 4
PYR1-like protein 9
Regulatory components of ABA receptor 1
Gene namesi
Name:PYL9
Synonyms:RCAR1
Ordered Locus Names:At1g01360
ORF Names:F6F3.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G01360.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell membrane By similarity

  • Note: Localizes at the plasma membrane in the presence of a CAR protein.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29C → S: Stable homogeneity in reducing condition. 2 Publications1
Mutagenesisi34C → S: Stable homogeneity in reducing condition. 2 Publications1
Mutagenesisi112I → V: Increased HAB1 inhibitory ability. 1 Publication1
Mutagenesisi159C → S: Abnormal stable homogeneity in reducing condition. 2 Publications1
Mutagenesisi165L → V: Slight potentiation of (-)-ABA-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003917441 – 187Abscisic acid receptor PYL9Add BLAST187

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 159Reversible1 Publication
Disulfide bondi34 ↔ 159Reversible1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ84MC7.

Expressioni

Tissue specificityi

Expressed in root tips, vascular tissues, stomata, flowers, pollen tubes and developing seeds.1 Publication

Gene expression databases

GenevisibleiQ84MC7. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:24645846). Monomer (PubMed:21658606). Binds ABA on one subunit only. Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity). Binds specifically (+)-ABA but not (-)-ABA (PubMed:23844015, PubMed:24645846). Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19407143, PubMed:19874541).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1P495974EBI-2349513,EBI-782526
ABI2O047193EBI-2349513,EBI-537680

GO - Molecular functioni

Protein-protein interaction databases

BioGridi23691. 9 interactors.
DIPiDIP-53480N.
IntActiQ84MC7. 3 interactors.
STRINGi3702.AT1G01360.1.

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 28Combined sources15
Beta strandi33 – 44Combined sources12
Helixi46 – 53Combined sources8
Helixi59 – 61Combined sources3
Beta strandi66 – 70Combined sources5
Beta strandi80 – 85Combined sources6
Beta strandi92 – 102Combined sources11
Turni103 – 106Combined sources4
Beta strandi107 – 118Combined sources12
Beta strandi123 – 133Combined sources11
Beta strandi136 – 148Combined sources13
Helixi155 – 181Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OQUX-ray2.68A/B1-187[»]
3W9RX-ray1.90A1-187[»]
ProteinModelPortaliQ84MC7.
SMRiQ84MC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 178START-likeAdd BLAST152
Regioni91 – 96ABA bindingBy similarity6
Regioni118 – 124ABA bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 91Gate loopBy similarity5
Motifi117 – 119Latch loopBy similarity3

Domaini

Upon interaction with ABA, the 'latch' and 'gate' loops change in conformation leading to a tight dimerization and the creation a surface that enables the receptor to dock into and inhibit the PP2C active site.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IIK9. Eukaryota.
ENOG4111HU5. LUCA.
HOGENOMiHOG000238422.
InParanoidiQ84MC7.
KOiK14496.
OMAiHEPRETQ.
OrthoDBiEOG09360OHL.
PhylomeDBiQ84MC7.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR019587. Polyketide_cyclase/dehydratase.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF10604. Polyketide_cyc2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q84MC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDGVEGGTA MYGGLETVQY VRTHHQHLCR ENQCTSALVK HIKAPLHLVW
60 70 80 90 100
SLVRRFDQPQ KYKPFVSRCT VIGDPEIGSL REVNVKSGLP ATTSTERLEL
110 120 130 140 150
LDDEEHILGI KIIGGDHRLK NYSSILTVHP EIIEGRAGTM VIESFVVDVP
160 170 180
QGNTKDETCY FVEALIRCNL KSLADVSERL ASQDITQ
Length:187
Mass (Da):20,901
Last modified:June 1, 2003 - v1
Checksum:i070D485311163568
GO

Sequence cautioni

The sequence AAF97339 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM65514 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7G → D in AAM65514 (PubMed:11130712).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023628 Genomic DNA. Translation: AAF97339.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE27277.1.
BT006399 mRNA. Translation: AAP21207.1.
AK227623 mRNA. Translation: BAE99614.1.
AY087967 mRNA. Translation: AAM65514.1. Different initiation.
RefSeqiNP_563626.1. NM_100018.5.
UniGeneiAt.42653.

Genome annotation databases

EnsemblPlantsiAT1G01360.1; AT1G01360.1; AT1G01360.
GeneIDi838452.
GrameneiAT1G01360.1; AT1G01360.1; AT1G01360.
KEGGiath:AT1G01360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023628 Genomic DNA. Translation: AAF97339.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE27277.1.
BT006399 mRNA. Translation: AAP21207.1.
AK227623 mRNA. Translation: BAE99614.1.
AY087967 mRNA. Translation: AAM65514.1. Different initiation.
RefSeqiNP_563626.1. NM_100018.5.
UniGeneiAt.42653.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OQUX-ray2.68A/B1-187[»]
3W9RX-ray1.90A1-187[»]
ProteinModelPortaliQ84MC7.
SMRiQ84MC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23691. 9 interactors.
DIPiDIP-53480N.
IntActiQ84MC7. 3 interactors.
STRINGi3702.AT1G01360.1.

Proteomic databases

PaxDbiQ84MC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G01360.1; AT1G01360.1; AT1G01360.
GeneIDi838452.
GrameneiAT1G01360.1; AT1G01360.1; AT1G01360.
KEGGiath:AT1G01360.

Organism-specific databases

TAIRiAT1G01360.

Phylogenomic databases

eggNOGiENOG410IIK9. Eukaryota.
ENOG4111HU5. LUCA.
HOGENOMiHOG000238422.
InParanoidiQ84MC7.
KOiK14496.
OMAiHEPRETQ.
OrthoDBiEOG09360OHL.
PhylomeDBiQ84MC7.

Miscellaneous databases

PROiQ84MC7.

Gene expression databases

GenevisibleiQ84MC7. AT.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR019587. Polyketide_cyclase/dehydratase.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF10604. Polyketide_cyc2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYL9_ARATH
AccessioniPrimary (citable) accession number: Q84MC7
Secondary accession number(s): Q8LA91, Q9LNI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.