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Protein

Abscisic acid receptor PYR1

Gene

PYR1

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) 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei59 – 591ABA2 Publications
Sitei88 – 881Involved in interactions with PP2Cs1 Publication
Binding sitei141 – 1411ABA2 Publications
Sitei152 – 1521Involved in interactions with PP2Cs1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB
  • regulation of protein serine/threonine phosphatase activity Source: TAIR
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 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

TAIRiAT4G17870.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591K → Q: Impaired ABA-mediated binding to PP2Cs. 1 Publication
Mutagenesisi88 – 881P → S: Insensitivity to pyrabactin and impaired ABA-mediated binding to PP2Cs. 1 Publication
Mutagenesisi116 – 1161R → G: Impaired ABA-mediated binding to PP2Cs. 1 Publication
Mutagenesisi152 – 1521S → L: Insensitivity to pyrabactin and impaired ABA-mediated binding to PP2Cs. 1 Publication
Mutagenesisi157 – 1571R → H: Reduced sensitivity to pyrabactin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Abscisic acid receptor PYR1PRO_0000391735Add
BLAST

Proteomic databases

PaxDbiO49686.
PRIDEiO49686.

Expressioni

Gene expression databases

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

WithEntry#Exp.IntActNotes
itself4EBI-2349590,EBI-2349590
ABI1P495977EBI-2349590,EBI-782526
ABI2O047193EBI-2349590,EBI-537680
HAB1Q9CAJ08EBI-2349590,EBI-2309302

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi12803. 12 interactions.
DIPiDIP-53473N.
IntActiO49686. 8 interactions.
MINTiMINT-8299468.
STRINGi3702.AT4G17870.1.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi7 – 2014Combined sources
Beta strandi29 – 4012Combined sources
Helixi42 – 498Combined sources
Helixi55 – 573Combined sources
Beta strandi60 – 667Combined sources
Beta strandi78 – 8811Combined sources
Beta strandi90 – 10011Combined sources
Turni101 – 1044Combined sources
Beta strandi105 – 1139Combined sources
Helixi116 – 1183Combined sources
Beta strandi121 – 13111Combined sources
Beta strandi134 – 14613Combined sources
Beta strandi149 – 1546Combined sources
Helixi157 – 17923Combined sources
Turni180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO49686.
SMRiO49686. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO49686.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 176154START-likeAdd
BLAST
Regioni89 – 946ABA binding2 Publications
Regioni116 – 1227ABA binding2 Publications

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi85 – 895Gate loopBy similarity
Motifi115 – 1173Latch loopBy similarity

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.
OMAiHRFEKEN.
OrthoDBiEOG09360NRL.
PhylomeDBiO49686.

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.

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_117896.2.
UniGeneiAt.2045.

Genome annotation databases

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

Cross-referencesi

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_117896.2.
UniGeneiAt.2045.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO49686.
SMRiO49686. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12803. 12 interactions.
DIPiDIP-53473N.
IntActiO49686. 8 interactions.
MINTiMINT-8299468.
STRINGi3702.AT4G17870.1.

Proteomic databases

PaxDbiO49686.
PRIDEiO49686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G17870.

Phylogenomic databases

eggNOGiENOG410IJIR. Eukaryota.
ENOG410YDHK. LUCA.
HOGENOMiHOG000238422.
InParanoidiO49686.
KOiK14496.
OMAiHRFEKEN.
OrthoDBiEOG09360NRL.
PhylomeDBiO49686.

Miscellaneous databases

EvolutionaryTraceiO49686.
PROiO49686.

Gene expression databases

GenevisibleiO49686. 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 nameiPYR1_ARATH
AccessioniPrimary (citable) accession number: O49686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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.