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Protein

Abscisic acid receptor PYL2

Gene

PYL2

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:19893533, PubMed:19898420, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641ABA2 Publications
Sitei92 – 921Involved in interactions with PP2CsBy similarity
Binding sitei147 – 1471ABA2 Publications
Sitei158 – 1581Involved in interactions with PP2CsBy similarity
Sitei166 – 1661Involved in ABA bindingBy similarity

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

  • abscisic acid-activated signaling pathway Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • regulation of protein serine/threonine phosphatase activity Source: GO_Central
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 PYL2
Alternative name(s):
PYR1-like protein 2
Regulatory components of ABA receptor 14
Gene namesi
Name:PYL2
Synonyms:RCAR14
Ordered Locus Names:At2g26040
ORF Names:T19L18.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G26040.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641K → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 2 Publications
Mutagenesisi87 – 871V → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi87 – 871V → L: Increased constitutive inhibition of PP2C phosphatase. 1 Publication
Mutagenesisi88 – 881I → K: Monomer due to impaired homodimerization. Increased ABA-binding affinity and increased constitutive inhibition of PP2C phosphatase. 1 Publication
Mutagenesisi90 – 901G → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi91 – 911L → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi93 – 931A → S: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi98 – 981E → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi124 – 1241Y → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi147 – 1471E → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi151 – 1511V → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication
Mutagenesisi173 – 1731N → A: Impaired ABA-mediated binding to PP2Cs and subsequent inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Abscisic acid receptor PYL2PRO_0000391737Add
BLAST

Proteomic databases

PaxDbiO80992.
PRIDEiO80992.

Expressioni

Gene expression databases

GenevisibleiO80992. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:19898420, PubMed:21658606). Binds ABA on one subunit only. Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19893533, PubMed:19898420). Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity).By similarity4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi2497. 4 interactions.
DIPiDIP-48582N.
IntActiO80992. 2 interactions.
STRINGi3702.AT2G26040.1.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2514Combined sources
Beta strandi34 – 4512Combined sources
Helixi47 – 559Combined sources
Helixi60 – 623Combined sources
Beta strandi65 – 7814Combined sources
Beta strandi82 – 876Combined sources
Beta strandi89 – 924Combined sources
Beta strandi94 – 10411Combined sources
Turni105 – 1084Combined sources
Beta strandi109 – 12012Combined sources
Beta strandi125 – 13410Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 15212Combined sources
Helixi159 – 18325Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KAZX-ray1.85A/B/C14-188[»]
3KB0X-ray1.95A14-188[»]
3KB3X-ray1.95A14-188[»]
3KDHX-ray1.65A/B/C1-190[»]
3KDIX-ray2.38A1-190[»]
3KL1X-ray1.55A/B1-190[»]
3NJ0X-ray1.89A/B/C1-190[»]
3NJ1X-ray1.95A1-190[»]
3NMHX-ray1.85A/B/C14-189[»]
3NMPX-ray2.10A/B/C14-189[»]
3NMTX-ray2.56A14-189[»]
3NMVX-ray2.10A14-189[»]
3NR4X-ray2.01A/B/C1-190[»]
3NS2X-ray1.63A/B/C1-190[»]
3UJLX-ray2.50A14-188[»]
4LA7X-ray1.98A1-190[»]
4LG5X-ray2.88A14-188[»]
4LGAX-ray2.70A14-188[»]
4LGBX-ray3.15A14-188[»]
ProteinModelPortaliO80992.
SMRiO80992. Positions 8-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO80992.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 182155START-likeAdd
BLAST
Regioni93 – 986ABA binding2 Publications
Regioni120 – 1267ABA binding2 Publications

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 935Gate loop1 Publication
Motifi119 – 1213Latch loop1 Publication

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IVVS. Eukaryota.
ENOG410YE0A. LUCA.
HOGENOMiHOG000238422.
InParanoidiO80992.
KOiK14496.
OMAiHFIKSCD.
PhylomeDBiO80992.

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.

O80992-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPAVKGL TDEEQKTLEP VIKTYHQFEP DPTTCTSLIT QRIHAPASVV
60 70 80 90 100
WPLIRRFDNP ERYKHFVKRC RLISGDGDVG SVREVTVISG LPASTSTERL
110 120 130 140 150
EFVDDDHRVL SFRVVGGEHR LKNYKSVTSV NEFLNQDSGK VYTVVLESYT
160 170 180 190
VDIPEGNTEE DTKMFVDTVV KLNLQKLGVA ATSAPMHDDE
Length:190
Mass (Da):21,282
Last modified:November 1, 1998 - v1
Checksum:iCBB16E64BE2B8164
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004747 Genomic DNA. Translation: AAC31232.1.
CP002685 Genomic DNA. Translation: AEC07788.1.
PIRiT02619.
RefSeqiNP_180174.1. NM_128163.1.
UniGeneiAt.66246.

Genome annotation databases

EnsemblPlantsiAT2G26040.1; AT2G26040.1; AT2G26040.
GeneIDi817145.
GrameneiAT2G26040.1; AT2G26040.1; AT2G26040.
KEGGiath:AT2G26040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004747 Genomic DNA. Translation: AAC31232.1.
CP002685 Genomic DNA. Translation: AEC07788.1.
PIRiT02619.
RefSeqiNP_180174.1. NM_128163.1.
UniGeneiAt.66246.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KAZX-ray1.85A/B/C14-188[»]
3KB0X-ray1.95A14-188[»]
3KB3X-ray1.95A14-188[»]
3KDHX-ray1.65A/B/C1-190[»]
3KDIX-ray2.38A1-190[»]
3KL1X-ray1.55A/B1-190[»]
3NJ0X-ray1.89A/B/C1-190[»]
3NJ1X-ray1.95A1-190[»]
3NMHX-ray1.85A/B/C14-189[»]
3NMPX-ray2.10A/B/C14-189[»]
3NMTX-ray2.56A14-189[»]
3NMVX-ray2.10A14-189[»]
3NR4X-ray2.01A/B/C1-190[»]
3NS2X-ray1.63A/B/C1-190[»]
3UJLX-ray2.50A14-188[»]
4LA7X-ray1.98A1-190[»]
4LG5X-ray2.88A14-188[»]
4LGAX-ray2.70A14-188[»]
4LGBX-ray3.15A14-188[»]
ProteinModelPortaliO80992.
SMRiO80992. Positions 8-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2497. 4 interactions.
DIPiDIP-48582N.
IntActiO80992. 2 interactions.
STRINGi3702.AT2G26040.1.

Proteomic databases

PaxDbiO80992.
PRIDEiO80992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G26040.1; AT2G26040.1; AT2G26040.
GeneIDi817145.
GrameneiAT2G26040.1; AT2G26040.1; AT2G26040.
KEGGiath:AT2G26040.

Organism-specific databases

TAIRiAT2G26040.

Phylogenomic databases

eggNOGiENOG410IVVS. Eukaryota.
ENOG410YE0A. LUCA.
HOGENOMiHOG000238422.
InParanoidiO80992.
KOiK14496.
OMAiHFIKSCD.
PhylomeDBiO80992.

Miscellaneous databases

EvolutionaryTraceiO80992.
PROiO80992.

Gene expression databases

GenevisibleiO80992. 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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Regulators of PP2C phosphatase activity function as abscisic acid sensors."
    Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., Grill E.
    Science 324:1064-1068(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  4. Cited for: INTERACTION WITH HAB1, GENE FAMILY, NOMENCLATURE.
  5. "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass of PYL proteins."
    Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F., Yan N.
    Mol. Cell 42:662-672(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-87 AND ILE-88, HOMODIMER, GENE FAMILY.
  6. "Structural insights into the abscisic acid stereospecificity by the ABA receptors PYR/PYL/RCAR."
    Zhang X., Jiang L., Wang G., Yu L., Zhang Q., Xin Q., Wu W., Gong Z., Chen Z.
    PLoS ONE 8:E67477-E67477(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GENE FAMILY.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-188 IN COMPLEX WITH ABSCISIC ACID AND PP2C HAB1, DIMERIZATION, FUNCTION, INTERACTION WITH HAB1; ABI1 AND ABI2, GATE AND LATCH MOTIFS, MUTAGENESIS OF LYS-64; VAL-87; GLY-90; LEU-91; ALA-93; GLU-98; TYR-124; GLU-147; VAL-151 AND ASN-173, DOMAIN.
  8. "Structural insights into the mechanism of abscisic acid signaling by PYL proteins."
    Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J., Yan N.
    Nat. Struct. Mol. Biol. 16:1230-1236(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) ALONE AND IN COMPLEX WITH ABSCISIC ACID, FUNCTION, INTERACTION WITH ABI1, MUTAGENESIS OF LYS-64.

Entry informationi

Entry nameiPYL2_ARATH
AccessioniPrimary (citable) accession number: O80992
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 88 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.