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Protein

Abscisic acid receptor PYL4

Gene

PYL4

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:19624469, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811ABABy similarity
Sitei110 – 1101Involved in interactions with PP2CsBy similarity
Binding sitei160 – 1601ABABy similarity
Sitei171 – 1711Involved in interactions with PP2CsBy similarity
Sitei179 – 1791Involved 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

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 PYL4
Alternative name(s):
ABI1-binding protein 2
PYR1-like protein 4
Regulatory components of ABA receptor 10
Gene namesi
Name:PYL4
Synonyms:ABIP2, RCAR10
Ordered Locus Names:At2g38310
ORF Names:T19C21.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G38310.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Abscisic acid receptor PYL4PRO_0000391739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 176ReversibleBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO80920.
PRIDEiO80920.

PTM databases

iPTMnetiO80920.

Expressioni

Gene expression databases

GenevisibleiO80920. AT.

Interactioni

Subunit structurei

Monomer (PubMed:21658606). Homodimer. Binds ABA on one subunit only (By similarity). Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19874541, PubMed:19898420). 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).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1P495973EBI-2349683,EBI-782526

GO - Molecular functioni

Protein-protein interaction databases

BioGridi3753. 11 interactions.
DIPiDIP-53474N.
IntActiO80920. 5 interactions.
STRINGi3702.AT2G38310.1.

Structurei

3D structure databases

ProteinModelPortaliO80920.
SMRiO80920. Positions 40-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 195151START-likeAdd
BLAST
Regioni111 – 1166ABA bindingBy similarity
Regioni138 – 1447ABA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi107 – 1115Gate loopBy similarity
Motifi137 – 1393Latch 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

eggNOGiENOG410IG1P. Eukaryota.
ENOG4111MYF. LUCA.
HOGENOMiHOG000238422.
InParanoidiO80920.
KOiK14496.
OMAiVSRYHTH.
PhylomeDBiO80920.

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.

O80920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAVHRPSSA VSDGDSVQIP MMIASFQKRF PSLSRDSTAA RFHTHEVGPN
60 70 80 90 100
QCCSAVIQEI SAPISTVWSV VRRFDNPQAY KHFLKSCSVI GGDGDNVGSL
110 120 130 140 150
RQVHVVSGLP AASSTERLDI LDDERHVISF SVVGGDHRLS NYRSVTTLHP
160 170 180 190 200
SPISGTVVVE SYVVDVPPGN TKEETCDFVD VIVRCNLQSL AKIAENTAAE

SKKKMSL
Length:207
Mass (Da):22,435
Last modified:November 1, 1998 - v1
Checksum:i118160B35D7066BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004683 Genomic DNA. Translation: AAC28773.1.
CP002685 Genomic DNA. Translation: AEC09522.1.
AY039586 mRNA. Translation: AAK62641.1.
AY054141 mRNA. Translation: AAL06802.1.
AY087146 mRNA. Translation: AAM64704.1.
PIRiT02514.
RefSeqiNP_565887.1. NM_129387.2.
UniGeneiAt.12775.

Genome annotation databases

EnsemblPlantsiAT2G38310.1; AT2G38310.1; AT2G38310.
GeneIDi818411.
GrameneiAT2G38310.1; AT2G38310.1; AT2G38310.
KEGGiath:AT2G38310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC004683 Genomic DNA. Translation: AAC28773.1.
CP002685 Genomic DNA. Translation: AEC09522.1.
AY039586 mRNA. Translation: AAK62641.1.
AY054141 mRNA. Translation: AAL06802.1.
AY087146 mRNA. Translation: AAM64704.1.
PIRiT02514.
RefSeqiNP_565887.1. NM_129387.2.
UniGeneiAt.12775.

3D structure databases

ProteinModelPortaliO80920.
SMRiO80920. Positions 40-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3753. 11 interactions.
DIPiDIP-53474N.
IntActiO80920. 5 interactions.
STRINGi3702.AT2G38310.1.

PTM databases

iPTMnetiO80920.

Proteomic databases

PaxDbiO80920.
PRIDEiO80920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G38310.1; AT2G38310.1; AT2G38310.
GeneIDi818411.
GrameneiAT2G38310.1; AT2G38310.1; AT2G38310.
KEGGiath:AT2G38310.

Organism-specific databases

TAIRiAT2G38310.

Phylogenomic databases

eggNOGiENOG410IG1P. Eukaryota.
ENOG4111MYF. LUCA.
HOGENOMiHOG000238422.
InParanoidiO80920.
KOiK14496.
OMAiVSRYHTH.
PhylomeDBiO80920.

Miscellaneous databases

PROiO80920.

Gene expression databases

GenevisibleiO80920. 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. "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. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: INTERACTION WITH HAB1; ABI1 AND ABI2.
  6. "Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs."
    Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F., Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.
    Plant J. 60:575-588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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.
  8. Cited for: INTERACTION WITH HAB1, GENE FAMILY, NOMENCLATURE.
  9. "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.
  10. "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, MONOMER, GENE FAMILY.
  11. "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.
  12. "C2-domain abscisic acid-related proteins mediate the interaction of PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate abscisic acid sensitivity in Arabidopsis."
    Rodriguez L., Gonzalez-Guzman M., Diaz M., Rodrigues A., Izquierdo-Garcia A.C., Peirats-Llobet M., Fernandez M.A., Antoni R., Fernandez D., Marquez J.A., Mulet J.M., Albert A., Rodriguez P.L.
    Plant Cell 26:4802-4820(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAR1 AND CAR4, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPYL4_ARATH
AccessioniPrimary (citable) accession number: O80920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.