PYR1 Polyketide cyclase/dehydrase and lipid transport superfamily protein [Arabidopsis thaliana (thale cress)] - Gene

Summary

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Official Symbol: PYR1
Official Full Name: Polyketide cyclase/dehydrase and lipid transport superfamily protein
Primary source: TAIR:AT4G17870
Locus tag: AT4G17870
See related: Araport:AT4G17870
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as: PYRABACTIN RESISTANCE 1; RCAR11; regulatory component of ABA receptor 11; T6K21.50; T6K21_50
Summary: Encodes a member of the PYR (pyrabactin resistance)/PYL(PYR1-like)/RCAR (regulatory components of ABA receptor) family proteins with 14 members. PYR/PYL/RCAR family proteins function as abscisic acid sensors. Mediate ABA-dependent regulation of protein phosphatase 2Cs ABI1 and ABI2.
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Genomic context

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See PYR1 in Genome Data Viewer

Location:: chromosome: 4

Exon count:: 1

Sequence:: Chromosome: 4; NC_003075.7 (9928587..9929875)

Chromosome 4 - NC_003075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003075.7

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Role of ABA in Plant Immunity is Mediated through the PYR1 Receptor.
Title: The Role of ABA in Plant Immunity is Mediated through the PYR1 Receptor.
These findings confirm that the subfamily III plays a key role in ABA-mediated developmental processes and, more importantly, is involved in drought tolerance in the ABA-dependent pathway.
Title: ABA Receptor Subfamily III Enhances Abscisic Acid Sensitivity and Improves the Drought Tolerance of Arabidopsis.
Data indicate that bscisic acid (ABA) signaling is repressed by group A type 2C protein phosphatases (PP2Cs), and then ABA binds to its receptor of the ACTIN RESISTANCE1 (PYR1), PYR1-LIKE (PYL), and REGULATORY COMPONENTS OF ABA RECEPTORS (RCAR) family, which, in turn, inhibits PP2Cs and activates downstream ABA signaling.
Title: A Novel Chemical Inhibitor of ABA Signaling Targets All ABA Receptors.
study suggests both nuclear and cytoplasmic PYR1 participate in the control of ABA signal transduction
Title: Production of ABA responses requires both the nuclear and cytoplasmic functional involvement of PYR1.
RSL1-PYL4 and RSL1-PYR1 interaction is localized to plasma membrane. RSL1 promoted PYL4 and PYR1 degradation in vivo and mediated in vitro ubiquitylation of the receptors.
Title: The single-subunit RING-type E3 ubiquitin ligase RSL1 targets PYL4 and PYR1 ABA receptors in plasma membrane to modulate abscisic acid signaling.
The transgenic plants show an acute abscisic acid (ABA) insensitivity, demonstrating the importance of ABA-mediated PYR/PYL/RCAR-PP2C contacts for receptor function in vivo.
Title: Modulation of abscisic acid signaling in vivo by an engineered receptor-insensitive protein phosphatase type 2C allele.
Pyr1 receptor contributes to ozone, reduced air humidity and darkness induced stomatal regulation.
Title: PYR/RCAR receptors contribute to ozone-, reduced air humidity-, darkness-, and CO2-induced stomatal regulation.
findings are generally consistent with the competitive-interaction model for PYR1 but highlight dynamical contributions of the PYR1 structure in mediating interaction selectivity
Title: Molecular mechanisms in the activation of abscisic acid receptor PYR1.
This work illustrates how oligomerization of abscisic acid receptors can modulate hormonal responses in Arabidopsis and more generally, the sensitivity of a ligand-dependent signalling system.
Title: A thermodynamic switch modulates abscisic acid receptor sensitivity.
Subtle changes in the binding pockets of PYR/PYL proteins control ligand orientation inside the pocket, and this is sufficient to explain whether pyrabactin acts as an effective receptor agonist. [PYR1]
Title: Structural basis for selective activation of ABA receptors.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

NM_117896.3

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
enables abscisic acid binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables kinase regulator activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables protein homodimerization activity	IPI Inferred from Physical Interaction more info	PubMed
enables protein phosphatase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables signaling receptor activity	IDA Inferred from Direct Assay more info	PubMed
enables signaling receptor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ubiquitin-like protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in abscisic acid-activated signaling pathway	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within abscisic acid-activated signaling pathway	IPI Inferred from Physical Interaction more info	PubMed
involved_in positive regulation of response to water deprivation	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISM Inferred from Sequence Model more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
located_in plant-type vacuole membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Polyketide cyclase/dehydrase and lipid transport superfamily protein

NP_193521.1

PYRABACTIN RESISTANCE 1 (PYR1); FUNCTIONS IN: abscisic acid binding; INVOLVED IN: abscisic acid mediated signaling pathway, regulation of protein phosphatase type 2c activity; LOCATED IN: cellular_component unknown; EXPRESSED IN: 25 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Streptomyces cyclase/dehydrase (InterPro:IPR005031); BEST Arabidopsis thaliana protein match is: PYR1-like 1 (TAIR:AT5G46790.1); Has 389 Blast hits to 389 proteins in 26 species: Archae - 0; Bacteria - 0; Metazoa - 0; Fungi - 0; Plants - 389; Viruses - 0; Other Eukaryotes - 0 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003075.7 Reference assembly

Range

9928587..9929875

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_117896.3 → NP_193521.1 Polyketide cyclase/dehydrase and lipid transport superfamily protein [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_193521.1

Status: REVIEWED

UniProtKB/Swiss-Prot

O49686

UniProtKB/TrEMBL

A0A178UTC0, A0A5S9XTK0, A0A654FQK3

Conserved Domains (1) summary

cd07821
Location:30 → 176

PYR_PYL_RCAR_like; Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins