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Protein

Abscisic acid receptor PYR1

Gene

PYR1

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) when activated by ABA (PubMed:19407142, PubMed:19624469, PubMed:19769575, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).5 Publications

Miscellaneous

The synthetic growth inhibitor pyrabactin inhibits ABA-binding and subsequent PP2Cs inhibitor properties.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei59ABA2 Publications1
Sitei88Involved in interactions with PP2Cs1 Publication1
Binding sitei141ABA2 Publications1
Sitei152Involved in interactions with PP2Cs1 Publication1

GO - Molecular functioni

  • abscisic acid binding Source: TAIR
  • identical protein binding Source: IntAct
  • 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
  • regulation of protein serine/threonine phosphatase activity Source: TAIR

Keywordsi

Molecular functionProtein phosphatase inhibitor, Receptor
Biological processAbscisic acid signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Abscisic acid receptor PYR1
Alternative name(s):
ABI1-binding protein 6
Protein PYRABACTIN RESISTANCE 1
Regulatory components of ABA receptor 11
Gene namesi
Name:PYR1
Synonyms:ABIP6, RCAR11
Ordered Locus Names:At4g17870
ORF Names:T6K21.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

AraportiAT4G17870
TAIRilocus:2141040 AT4G17870

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
Mutagenesisi59K → Q: Impaired ABA-mediated binding to PP2Cs. 1 Publication1
Mutagenesisi88P → S: Insensitivity to pyrabactin and impaired ABA-mediated binding to PP2Cs. 1 Publication1
Mutagenesisi116R → G: Impaired ABA-mediated binding to PP2Cs. 1 Publication1
Mutagenesisi152S → L: Insensitivity to pyrabactin and impaired ABA-mediated binding to PP2Cs. 1 Publication1
Mutagenesisi157R → H: Reduced sensitivity to pyrabactin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003917351 – 191Abscisic acid receptor PYR1Add BLAST191

Proteomic databases

PaxDbiO49686
PRIDEiO49686

Expressioni

Gene expression databases

ExpressionAtlasiO49686 baseline and differential
GenevisibleiO49686 AT

Interactioni

Subunit structurei

Homodimer (PubMed:21658606,PubMed:19898494,PubMed:19933100). Binds ABA on one subunit only. Interacts with HAB1, AHG3, ABI1 and ABI2 when complexed to ABA, and possibly with other PP2Cs (PubMed:19407142, PubMed:19874541, PubMed:19898420, PubMed:19898494, PubMed:19933100). Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus. Interacts directly with CAR1 and CAR4 (PubMed:25465408).7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi12803, 12 interactors
DIPiDIP-53473N
IntActiO49686, 8 interactors
MINTiO49686
STRINGi3702.AT4G17870.1

Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi7 – 12Combined sources6
Helixi14 – 20Combined sources7
Beta strandi29 – 40Combined sources12
Helixi42 – 49Combined sources8
Helixi55 – 57Combined sources3
Beta strandi60 – 66Combined sources7
Beta strandi78 – 83Combined sources6
Beta strandi87 – 100Combined sources14
Turni101 – 104Combined sources4
Beta strandi105 – 116Combined sources12
Beta strandi121 – 131Combined sources11
Beta strandi134 – 146Combined sources13
Beta strandi149 – 154Combined sources6
Helixi158 – 179Combined sources22
Turni180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K3KX-ray1.70A/B1-191[»]
3K90X-ray2.00A/B/C/D1-191[»]
3NJOX-ray2.47A/B/C1-191[»]
3QN1X-ray1.80A3-191[»]
3WG8X-ray2.30A1-191[»]
3ZVUX-ray2.10A3-191[»]
4WVOX-ray2.25A1-181[»]
5UR4X-ray1.52A1-181[»]
5UR5X-ray1.93A1-181[»]
5UR6X-ray1.63A1-181[»]
ProteinModelPortaliO49686
SMRiO49686
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO49686

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 176START-likeAdd BLAST154
Regioni89 – 94ABA binding2 Publications6
Regioni116 – 122ABA binding2 Publications7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi85 – 89Gate loopBy similarity5
Motifi115 – 117Latch 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

eggNOGiENOG410IJIR Eukaryota
ENOG410YDHK LUCA
HOGENOMiHOG000238422
InParanoidiO49686
KOiK14496
OMAiFHSYRIN
OrthoDBiEOG09360NRL
PhylomeDBiO49686

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.

O49686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSELTPEER SELKNSIAEF HTYQLDPGSC SSLHAQRIHA PPELVWSIVR
60 70 80 90 100
RFDKPQTYKH FIKSCSVEQN FEMRVGCTRD VIVISGLPAN TSTERLDILD
110 120 130 140 150
DERRVTGFSI IGGEHRLTNY KSVTTVHRFE KENRIWTVVL ESYVVDMPEG
160 170 180 190
NSEDDTRMFA DTVVKLNLQK LATVAEAMAR NSGDGSGSQV T
Length:191
Mass (Da):21,575
Last modified:June 1, 1998 - v1
Checksum:iAD35DA240E286B55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021889 Genomic DNA Translation: CAA17130.1
AL161547 Genomic DNA Translation: CAB78789.1
CP002687 Genomic DNA Translation: AEE83959.1
AY042890 mRNA Translation: AAK68830.1
AY081526 mRNA Translation: AAM10088.1
PIRiT05073
RefSeqiNP_193521.1, NM_117896.3
UniGeneiAt.2045

Genome annotation databases

EnsemblPlantsiAT4G17870.1; AT4G17870.1; AT4G17870
GeneIDi827510
GrameneiAT4G17870.1; AT4G17870.1; AT4G17870
KEGGiath:AT4G17870

Similar proteinsi

Entry informationi

Entry nameiPYR1_ARATH
AccessioniPrimary (citable) accession number: O49686
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 110 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

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
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Main funding by: National Institutes of Health