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Protein

Abscisic acid receptor PYL9

Gene

PYL9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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
  • signaling receptor activity Source: UniProtKB

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB

Keywordsi

Molecular functionProtein phosphatase inhibitor, Receptor
Biological processAbscisic 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

AraportiAT1G01360
TAIRilocus:2035227 AT1G01360

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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

ExpressionAtlasiQ84MC7 baseline and differential
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). Interacts with TOPP1 (PubMed:26943172).By similarity7 Publications

Binary interactionsi

Show more details

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
OMAiHSCREDQ
OrthoDBiEOG09360OHL
PhylomeDBiQ84MC7

Family and domain databases

Gene3Di3.30.530.20, 1 hit
InterProiView protein in InterPro
IPR019587 Polyketide_cyclase/dehydratase
IPR023393 START-like_dom_sf
PfamiView protein in Pfam
PF10604 Polyketide_cyc2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPYL9_ARATH
AccessioniPrimary (citable) accession number: Q84MC7
Secondary accession number(s): Q8LA91, Q9LNI7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 2003
Last modified: May 23, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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