Abscisic acid receptor PYL8 - Arabidopsis thaliana (Mouse-ear cress)

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Q9FGM1 (PYL8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Abscisic acid receptor PYL8

Alternative name(s):
ABI1-binding protein 1
PYR1-like protein 8
Regulatory components of ABA receptor 3

Gene names

Name:	PYL8
Synonyms:	ABIP1, RCAR3
Ordered Locus Names:	At5g53160
ORF Names:	MFH8.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Confers enhanced sensitivity to ABA. Ref.5 Ref.7 Ref.9 Ref.10
Subunit structure	Homodimer. Binds ABA on one subunit only By similarity. interacts with ABI1 and HAB1, and possibly with other PP2Cs. Ref.5 Ref.6 Ref.9
Subcellular location	Cytoplasm. Nucleus Ref.10.
Domain	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 similarities	Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Receptor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from direct assay Ref.7 Ref.5 Ref.9. Source: UniProtKB positive regulation of abscisic acid mediated signaling pathway Inferred from mutant phenotype Ref.10. Source: TAIR
Cellular_component	cytoplasm Inferred from direct assay Ref.10. Source: UniProtKB nucleus Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	abscisic acid binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB receptor activity Inferred from direct assay Ref.7 Ref.5 Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FGM1-1) 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 188

188

Abscisic acid receptor PYL8

PRO_0000391743

Regions

Region

25 – 176

152

START-like

Region

89 – 94

ABA binding By similarity

Region

116 – 122

ABA binding By similarity

Motif

85 – 89

Gate loop By similarity

Motif

115 – 117

Latch loop By similarity

Sites

Binding site

ABA By similarity

Binding site

141

ABA By similarity

Site

Involved in interactions with PP2Cs By similarity

Site

152

Involved in interactions with PP2Cs By similarity

Experimental info

Sequence conflict

I → F in BAF00266. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D3436ADAC890AEED
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FASTA

188

21,397

        10         20         30         40         50         60 
MEANGIENLT NPNQEREFIR RHHKHELVDN QCSSTLVKHI NAPVHIVWSL VRRFDQPQKY 

        70         80         90        100        110        120 
KPFISRCVVK GNMEIGTVRE VDVKSGLPAT RSTERLELLD DNEHILSIRI VGGDHRLKNY 

       130        140        150        160        170        180 
SSIISLHPET IEGRIGTLVI ESFVVDVPEG NTKDETCYFV EALIKCNLKS LADISERLAV 


QDTTESRV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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. 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]	"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.
[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: FUNCTION, GENE FAMILY.
[8]	"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins." Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y., Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P., Zhu J.-K. , Schroeder J.I., Volkman B.F., Cutler S.R. Science 324:1068-1071(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"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.
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025622 Genomic DNA. Translation: BAB08419.1. CP002688 Genomic DNA. Translation: AED96316.1. BT003112 mRNA. Translation: AAO24544.1. AK228324 mRNA. Translation: BAF00266.1.
IPI	IPI00529045.
RefSeq	NP_200128.1. NM_124695.3.
UniGene	At.24684. At.72721.
3D structure databases
ProteinModelPortal	Q9FGM1.
SMR	Q9FGM1. Positions 30-181.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FGM1. 4 interactions.
Proteomic databases
PaxDb	Q9FGM1.
PRIDE	Q9FGM1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G53160.2; AT5G53160.2; AT5G53160.
GeneID	835397.
KEGG	ath:AT5G53160.
Organism-specific databases
TAIR	At5g53160.
Phylogenomic databases
eggNOG	NOG320241.
HOGENOM	HOG000238422.
InParanoid	Q9FGM1.
KO	K14496.
OMA	EHILSVR.
PhylomeDB	Q9FGM1.
ProtClustDB	CLSN2916304.
Gene expression databases
ArrayExpress	Q9FGM1.
Genevestigator	Q9FGM1.
Family and domain databases
Gene3D	3.30.530.20. 1 hit.
InterPro	IPR019587. Polyketide_cyclase/dehydratase. IPR023393. START-like_dom. [Graphical view]
Pfam	PF10604. Polyketide_cyc2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYL8_ARATH

Accession

Primary (citable) accession number: Q9FGM1
Secondary accession number(s): Q0WRI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 2, 2010
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents