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Protein

Abscisic acid receptor PYL1

Gene

PYL1

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861ABA
Sitei115 – 1151Involved in interactions with PP2Cs
Binding sitei171 – 1711ABA
Sitei182 – 1821Involved in interactions with PP2CsBy similarity

GO - Molecular functioni

  1. abscisic acid binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. receptor activity Source: UniProtKB

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: UniProtKB
  2. regulation of protein serine/threonine phosphatase activity Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Abscisic acid signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Abscisic acid receptor PYL1
Alternative name(s):
ABI1-binding protein 6
PYR1-like protein 1
Regulatory components of ABA receptor 9
Gene namesi
Name:PYL1
Synonyms:RCAR12
Ordered Locus Names:At5g46790
ORF Names:MZA15.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G46790.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 871H → A: Normal affinity for ABI1. 1 Publication
Mutagenesisi88 – 881F → A: Reduced affinity for ABI1. 1 Publication
Mutagenesisi111 – 1111I → A: Normal affinity for ABI1. 1 Publication
Mutagenesisi112 – 1121S → A: Reduced binding affinity and inhibitory activity toward ABI1. 1 Publication
Mutagenesisi114 – 1141L → A: Reduced affinity for ABI1. 1 Publication
Mutagenesisi115 – 1151P → A: Reduced affinity for ABI1. 1 Publication
Mutagenesisi142 – 1421H → A: Loss of affinity for ABI1. 1 Publication
Mutagenesisi143 – 1431R → A: Loss of affinity for ABI1. 1 Publication
Mutagenesisi144 – 1441L → A: Loss of affinity for ABI1. 1 Publication
Mutagenesisi178 – 1781P → A: Normal affinity for ABI1. 1 Publication
Mutagenesisi181 – 1811N → A: Reduced affinity for ABI1. 1 Publication
Mutagenesisi189 – 1891F → A: Reduced affinity for ABI1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Abscisic acid receptor PYL1PRO_0000391736Add
BLAST

Proteomic databases

PaxDbiQ8VZS8.
PRIDEiQ8VZS8.

Expressioni

Gene expression databases

GenevestigatoriQ8VZS8.

Interactioni

Subunit structurei

Homodimer. Binds ABA on one subunit only. Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HAB1Q9CAJ02EBI-2363104,EBI-2309302

Protein-protein interaction databases

BioGridi19970. 3 interactions.
DIPiDIP-48581N.
IntActiQ8VZS8. 3 interactions.
MINTiMINT-8299470.
STRINGi3702.AT5G46790.1-P.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Helixi34 – 4714Combined sources
Beta strandi56 – 6712Combined sources
Helixi69 – 768Combined sources
Helixi82 – 843Combined sources
Beta strandi89 – 935Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 12711Combined sources
Turni128 – 1314Combined sources
Beta strandi132 – 14312Combined sources
Beta strandi148 – 17629Combined sources
Helixi183 – 20826Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRQX-ray2.10B28-210[»]
3JRSX-ray2.05A/B/C8-211[»]
3KAYX-ray2.40A/B36-211[»]
3KDJX-ray1.88A20-221[»]
3NEFX-ray2.40A/B20-221[»]
3NEGX-ray2.80A/B20-221[»]
3NMNX-ray2.15A/C36-211[»]
ProteinModelPortaliQ8VZS8.
SMRiQ8VZS8. Positions 31-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VZS8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 206157START-likeAdd
BLAST
Regioni116 – 1216ABA binding
Regioni143 – 1497ABA binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi112 – 1165Gate loop
Motifi142 – 1443Latch loop

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.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG235377.
HOGENOMiHOG000238422.
InParanoidiQ8VZS8.
KOiK14496.
OMAiIHAPPET.
PhylomeDBiQ8VZS8.

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.

Q8VZS8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANSESSSSP VNEEENSQRI STLHHQTMPS DLTQDEFTQL SQSIAEFHTY
60 70 80 90 100
QLGNGRCSSL LAQRIHAPPE TVWSVVRRFD RPQIYKHFIK SCNVSEDFEM
110 120 130 140 150
RVGCTRDVNV ISGLPANTSR ERLDLLDDDR RVTGFSITGG EHRLRNYKSV
160 170 180 190 200
TTVHRFEKEE EEERIWTVVL ESYVVDVPEG NSEEDTRLFA DTVIRLNLQK
210 220
LASITEAMNR NNNNNNSSQV R
Length:221
Mass (Da):25,361
Last modified:March 1, 2002 - v1
Checksum:iB64B1A52C43072C2
GO

Sequence cautioni

The sequence BAB08923.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016882 Genomic DNA. Translation: BAB08923.1. Different initiation.
CP002688 Genomic DNA. Translation: AED95426.1.
AY063877 mRNA. Translation: AAL36233.1.
AY117328 mRNA. Translation: AAM51403.1.
RefSeqiNP_199491.2. NM_124049.4.
UniGeneiAt.27159.

Genome annotation databases

EnsemblPlantsiAT5G46790.1; AT5G46790.1; AT5G46790.
GeneIDi834722.
KEGGiath:AT5G46790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016882 Genomic DNA. Translation: BAB08923.1. Different initiation.
CP002688 Genomic DNA. Translation: AED95426.1.
AY063877 mRNA. Translation: AAL36233.1.
AY117328 mRNA. Translation: AAM51403.1.
RefSeqiNP_199491.2. NM_124049.4.
UniGeneiAt.27159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRQX-ray2.10B28-210[»]
3JRSX-ray2.05A/B/C8-211[»]
3KAYX-ray2.40A/B36-211[»]
3KDJX-ray1.88A20-221[»]
3NEFX-ray2.40A/B20-221[»]
3NEGX-ray2.80A/B20-221[»]
3NMNX-ray2.15A/C36-211[»]
ProteinModelPortaliQ8VZS8.
SMRiQ8VZS8. Positions 31-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19970. 3 interactions.
DIPiDIP-48581N.
IntActiQ8VZS8. 3 interactions.
MINTiMINT-8299470.
STRINGi3702.AT5G46790.1-P.

Proteomic databases

PaxDbiQ8VZS8.
PRIDEiQ8VZS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G46790.1; AT5G46790.1; AT5G46790.
GeneIDi834722.
KEGGiath:AT5G46790.

Organism-specific databases

TAIRiAT5G46790.

Phylogenomic databases

eggNOGiNOG235377.
HOGENOMiHOG000238422.
InParanoidiQ8VZS8.
KOiK14496.
OMAiIHAPPET.
PhylomeDBiQ8VZS8.

Miscellaneous databases

EvolutionaryTraceiQ8VZS8.

Gene expression databases

GenevestigatoriQ8VZS8.

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. "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
    Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
    DNA Res. 5:379-391(1998) [PubMed] [Europe PMC] [Abstract]
    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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-interacting proteins in Arabidopsis."
    Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.
    Plant J. 61:290-299(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABI1, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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: FUNCTION, GENE FAMILY.
  6. Cited for: INTERACTION WITH HAB1, GENE FAMILY, NOMENCLATURE.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-211, DIMERIZATION, INTERACTION WITH HAB1; ABI1 AND ABI2, FUNCTION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 8-211 IN COMPLEX WITH ABSCISIC ACID AND PP2C ABI1, INTERACTION WITH ABA AND ABI1, MUTAGENESIS OF HIS-87; PHE-88; ILE-111; SER-112; LEU-114; PRO-115; HIS-142; ARG-143; LEU-144; PRO-178; ASN-181 AND PHE-189, FUNCTION.
  10. "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 (1.88 ANGSTROMS) OF 20-221 IN COMPLEX WITH ABSCISIC ACID AND PP2C ABI1, FUNCTION.

Entry informationi

Entry nameiPYL1_ARATH
AccessioniPrimary (citable) accession number: Q8VZS8
Secondary accession number(s): Q9FIP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 71 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

External Data

Dasty 3

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 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.