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Protein

Abscisic acid receptor PYL9

Gene

PYL9

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:23844015, PubMed:21658606). Can be activated only by (+)-ABA but not by (-)-ABA (PubMed:23844015).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ABACombined sources2 Publications
Sitei64 – 641Involved in ABA binding1 Publication
Sitei90 – 901Involved in interactions with PP2CsBy similarity
Sitei110 – 1101Involved in ABA binding1 Publication
Binding sitei143 – 1431ABABy similarity
Sitei154 – 1541Involved in interactions with PP2CsBy similarity
Sitei162 – 1621Involved in ABA binding1 Publication
Sitei165 – 1651Involved in ABA binding1 Publication

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 PYL9
Alternative name(s):
ABI1-binding protein 4
PYR1-like protein 9
Regulatory components of ABA receptor 1
Gene namesi
Name:PYL9
Synonyms:RCAR1
Ordered Locus Names:At1g01360
ORF Names:F6F3.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G01360.

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
Mutagenesisi29 – 291C → S: Stable homogeneity in reducing condition. 2 Publications
Mutagenesisi34 – 341C → S: Stable homogeneity in reducing condition. 2 Publications
Mutagenesisi112 – 1121I → V: Increased HAB1 inhibitory ability. 1 Publication
Mutagenesisi159 – 1591C → S: Abnormal stable homogeneity in reducing condition. 2 Publications
Mutagenesisi165 – 1651L → V: Slight potentiation of (-)-ABA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187187Abscisic acid receptor PYL9PRO_0000391744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 159Reversible1 Publication
Disulfide bondi34 ↔ 159Reversible1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ84MC7.
PRIDEiQ84MC7.

Expressioni

Tissue specificityi

Expressed in root tips, vascular tissues, stomata, flowers, pollen tubes and developing seeds.1 Publication

Gene expression databases

GenevisibleiQ84MC7. AT.

Interactioni

Subunit structurei

Homodimer (PubMed:24645846). Monomer (PubMed:21658606). Binds ABA on one subunit only. Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity). Binds specifically (+)-ABA but not (-)-ABA (PubMed:23844015, PubMed:24645846). Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19407143, PubMed:19874541).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1P495974EBI-2349513,EBI-782526
ABI2O047193EBI-2349513,EBI-537680

GO - Molecular functioni

Protein-protein interaction databases

BioGridi23691. 9 interactions.
IntActiQ84MC7. 3 interactions.
STRINGi3702.AT1G01360.1.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2815Combined sources
Beta strandi33 – 4412Combined sources
Helixi46 – 538Combined sources
Helixi59 – 613Combined sources
Beta strandi66 – 705Combined sources
Beta strandi80 – 856Combined sources
Beta strandi92 – 10211Combined sources
Turni103 – 1064Combined sources
Beta strandi107 – 11812Combined sources
Beta strandi123 – 13311Combined sources
Beta strandi136 – 14813Combined sources
Helixi155 – 18127Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQUX-ray2.68A/B1-187[»]
3W9RX-ray1.90A1-187[»]
ProteinModelPortaliQ84MC7.
SMRiQ84MC7. Positions 13-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 178152START-likeAdd
BLAST
Regioni91 – 966ABA bindingBy similarity
Regioni118 – 1247ABA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi87 – 915Gate loopBy similarity
Motifi117 – 1193Latch 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.
InParanoidiQ84MC7.
KOiK14496.
OMAiDEEHILC.
PhylomeDBiQ84MC7.

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.

Q84MC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDGVEGGTA MYGGLETVQY VRTHHQHLCR ENQCTSALVK HIKAPLHLVW
60 70 80 90 100
SLVRRFDQPQ KYKPFVSRCT VIGDPEIGSL REVNVKSGLP ATTSTERLEL
110 120 130 140 150
LDDEEHILGI KIIGGDHRLK NYSSILTVHP EIIEGRAGTM VIESFVVDVP
160 170 180
QGNTKDETCY FVEALIRCNL KSLADVSERL ASQDITQ
Length:187
Mass (Da):20,901
Last modified:June 1, 2003 - v1
Checksum:i070D485311163568
GO

Sequence cautioni

The sequence AAF97339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM65514.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71G → D in AAM65514 (PubMed:11130712).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023628 Genomic DNA. Translation: AAF97339.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE27277.1.
BT006399 mRNA. Translation: AAP21207.1.
AK227623 mRNA. Translation: BAE99614.1.
AY087967 mRNA. Translation: AAM65514.1. Different initiation.
RefSeqiNP_563626.1. NM_100018.4.
UniGeneiAt.42653.

Genome annotation databases

EnsemblPlantsiAT1G01360.1; AT1G01360.1; AT1G01360.
GeneIDi838452.
GrameneiAT1G01360.1; AT1G01360.1; AT1G01360.
KEGGiath:AT1G01360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC023628 Genomic DNA. Translation: AAF97339.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE27277.1.
BT006399 mRNA. Translation: AAP21207.1.
AK227623 mRNA. Translation: BAE99614.1.
AY087967 mRNA. Translation: AAM65514.1. Different initiation.
RefSeqiNP_563626.1. NM_100018.4.
UniGeneiAt.42653.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OQUX-ray2.68A/B1-187[»]
3W9RX-ray1.90A1-187[»]
ProteinModelPortaliQ84MC7.
SMRiQ84MC7. Positions 13-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23691. 9 interactions.
IntActiQ84MC7. 3 interactions.
STRINGi3702.AT1G01360.1.

Proteomic databases

PaxDbiQ84MC7.
PRIDEiQ84MC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G01360.1; AT1G01360.1; AT1G01360.
GeneIDi838452.
GrameneiAT1G01360.1; AT1G01360.1; AT1G01360.
KEGGiath:AT1G01360.

Organism-specific databases

TAIRiAT1G01360.

Phylogenomic databases

eggNOGiENOG410IIK9. Eukaryota.
ENOG4111HU5. LUCA.
HOGENOMiHOG000238422.
InParanoidiQ84MC7.
KOiK14496.
OMAiDEEHILC.
PhylomeDBiQ84MC7.

Miscellaneous databases

PROiQ84MC7.

Gene expression databases

GenevisibleiQ84MC7. 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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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. "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. "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].
  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, TISSUE SPECIFICITY, INTERACTION WITH ABI1; ABI2 AND HAB1, GENE FAMILY.
  7. Cited for: INTERACTION WITH HAB1, GENE FAMILY, NOMENCLATURE.
  8. "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.
  9. "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.
  10. "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: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) IN COMPLEX WITH ABA, FUNCTION, MUTAGENESIS OF CYS-29; CYS-34; ILE-112; CYS-159 AND LEU-165, DISULFIDE BOND, INTERACTION WITH ABA, GENE FAMILY.
  11. "Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1."
    Nakagawa M., Kagiyama M., Shibata N., Hirano Y., Hakoshima T.
    Genes Cells 19:386-404(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ABA, MUTAGENESIS OF CYS-29; CYS-34 AND CYS-159, HOMODIMER.

Entry informationi

Entry nameiPYL9_ARATH
AccessioniPrimary (citable) accession number: Q84MC7
Secondary accession number(s): Q8LA91, Q9LNI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: June 1, 2003
Last modified: February 17, 2016
This is version 69 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.