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Protein

Abscisic acid receptor PYL8

Gene

PYL8

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) in an ABA-independent manner but more efficiently when activated by ABA. Confers enhanced sensitivity to ABA (PubMed:19407143, PubMed:19624469, PubMed:19769575, PubMed:19889877, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015).6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611ABABy similarity
Sitei62 – 621Involved in ABA bindingBy similarity
Sitei88 – 881Involved in interactions with PP2CsBy similarity
Sitei108 – 1081Involved in ABA bindingBy similarity
Binding sitei141 – 1411ABABy similarity
Sitei152 – 1521Involved in interactions with PP2CsBy similarity
Sitei160 – 1601Involved in ABA bindingBy similarity
Sitei163 – 1631Involved 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
  • positive regulation of abscisic acid-activated signaling pathway Source: TAIR
  • regulation of protein serine/threonine phosphatase activity Source: GO_Central
  • response to abscisic acid 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 PYL8
Alternative name(s):
ABI1-binding protein 1
PYR1-like protein 8
Regulatory components of ABA receptor 3
Gene namesi
Name:PYL8
Synonyms:ABIP1, RCAR3
Ordered Locus Names:At5g53160
ORF Names:MFH8.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G53160.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Abscisic acid receptor PYL8PRO_0000391743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 157ReversibleBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9FGM1.
PRIDEiQ9FGM1.

Expressioni

Gene expression databases

ExpressionAtlasiQ9FGM1. baseline and differential.
GenevisibleiQ9FGM1. AT.

Interactioni

Subunit structurei

Monomer (PubMed:21658606). Homodimer. Binds ABA on one subunit only (By similarity). interacts with ABI1 and HAB1, and possibly with other PP2Cs (PubMed:19624469, PubMed:19769575, PubMed:19874541). 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
HAB1Q9CAJ03EBI-2429535,EBI-2309302

GO - Molecular functioni

Protein-protein interaction databases

BioGridi20642. 19 interactions.
IntActiQ9FGM1. 4 interactions.
MINTiMINT-8299474.
STRINGi3702.AT5G53160.2.

Structurei

3D structure databases

ProteinModelPortaliQ9FGM1.
SMRiQ9FGM1. Positions 30-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 176152START-likeAdd
BLAST
Regioni89 – 946ABA bindingBy similarity
Regioni116 – 1227ABA bindingBy similarity

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

eggNOGiENOG410IIK9. Eukaryota.
ENOG4111HU5. LUCA.
HOGENOMiHOG000238422.
InParanoidiQ9FGM1.
KOiK14496.
OMAiHSEMING.
PhylomeDBiQ9FGM1.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FGM1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEANGIENLT NPNQEREFIR RHHKHELVDN QCSSTLVKHI NAPVHIVWSL
60 70 80 90 100
VRRFDQPQKY KPFISRCVVK GNMEIGTVRE VDVKSGLPAT RSTERLELLD
110 120 130 140 150
DNEHILSIRI VGGDHRLKNY SSIISLHPET IEGRIGTLVI ESFVVDVPEG
160 170 180
NTKDETCYFV EALIKCNLKS LADISERLAV QDTTESRV
Length:188
Mass (Da):21,397
Last modified:March 1, 2001 - v1
Checksum:iD3436ADAC890AEED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61I → F in BAF00266 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025622 Genomic DNA. Translation: BAB08419.1.
CP002688 Genomic DNA. Translation: AED96316.1.
BT003112 mRNA. Translation: AAO24544.1.
AK228324 mRNA. Translation: BAF00266.1.
RefSeqiNP_200128.1. NM_124695.3. [Q9FGM1-1]
UniGeneiAt.24684.
At.72721.

Genome annotation databases

EnsemblPlantsiAT5G53160.2; AT5G53160.2; AT5G53160. [Q9FGM1-1]
GeneIDi835397.
KEGGiath:AT5G53160.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025622 Genomic DNA. Translation: BAB08419.1.
CP002688 Genomic DNA. Translation: AED96316.1.
BT003112 mRNA. Translation: AAO24544.1.
AK228324 mRNA. Translation: BAF00266.1.
RefSeqiNP_200128.1. NM_124695.3. [Q9FGM1-1]
UniGeneiAt.24684.
At.72721.

3D structure databases

ProteinModelPortaliQ9FGM1.
SMRiQ9FGM1. Positions 30-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20642. 19 interactions.
IntActiQ9FGM1. 4 interactions.
MINTiMINT-8299474.
STRINGi3702.AT5G53160.2.

Proteomic databases

PaxDbiQ9FGM1.
PRIDEiQ9FGM1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G53160.2; AT5G53160.2; AT5G53160. [Q9FGM1-1]
GeneIDi835397.
KEGGiath:AT5G53160.

Organism-specific databases

TAIRiAT5G53160.

Phylogenomic databases

eggNOGiENOG410IIK9. Eukaryota.
ENOG4111HU5. LUCA.
HOGENOMiHOG000238422.
InParanoidiQ9FGM1.
KOiK14496.
OMAiHSEMING.
PhylomeDBiQ9FGM1.

Miscellaneous databases

PROiQ9FGM1.

Gene expression databases

ExpressionAtlasiQ9FGM1. baseline and differential.
GenevisibleiQ9FGM1. 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. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
    Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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, INTERACTION WITH HAB1.
  6. "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.
  7. Cited for: GENE FAMILY, NOMENCLATURE.
  8. "Closely related receptor complexes differ in their ABA selectivity and sensitivity."
    Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A., Assaad F.F., Christmann A., Grill E.
    Plant J. 61:25-35(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ABI1 AND ABI2.
  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 nuclear interactor PYL8/RCAR3 of Fagus sylvatica FsPP2C1 is a positive regulator of abscisic acid signaling in seeds and stress."
    Saavedra X., Modrego A., Rodriguez D., Gonzalez-Garcia M.P., Sanz L., Nicolas G., Lorenzo O.
    Plant Physiol. 152:133-150(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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.
  12. "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.
  13. "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 nameiPYL8_ARATH
AccessioniPrimary (citable) accession number: Q9FGM1
Secondary accession number(s): Q0WRI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 85 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.