Q8VZS8 (PYL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Abscisic acid receptor PYL1

Alternative name(s):
ABI1-binding protein 6
PYR1-like protein 1
Regulatory components of ABA receptor 9

Gene names

Name:	PYL1
Synonyms:	RCAR12
Ordered Locus Names:	At5g46790
ORF Names:	MZA15.21

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	221 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. Ref.5 Ref.7 Ref.8 Ref.9
Subunit structure	Homodimer. Binds ABA on one subunit only. Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs. Ref.4 Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
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.
Miscellaneous	The synthetic growth inhibitor pyrabactin inhibits ABA-binding and subsequent PP2Cs inhibitor properties.
Sequence similarities	Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family.
Sequence caution	The sequence BAB08923.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway
Cellular component	Cytoplasm Nucleus
Molecular function	Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from direct assay Ref.5Ref.7. Source: UniProtKB regulation of protein serine/threonine phosphatase activity Inferred from direct assay Ref.8. Source: TAIR
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	abscisic acid binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.7. Source: UniProtKB receptor activity Inferred from direct assay Ref.5Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Abscisic acid receptor PYL1

PRO_0000391736

Regions

Region

50 – 206

157

START-like

Region

116 – 121

6

ABA binding

Region

143 – 149

7

ABA binding

Motif

112 – 116

5

Gate loop

Motif

142 – 144

3

Latch loop

Sites

Binding site

86

1

ABA

Binding site

171

1

ABA

Site

115

1

Involved in interactions with PP2Cs

Site

182

1

Involved in interactions with PP2Cs By similarity

Experimental info

Mutagenesis

87

1

H → A: Normal affinity for ABI1. Ref.8

Mutagenesis

88

1

F → A: Reduced affinity for ABI1. Ref.8

Mutagenesis

111

1

I → A: Normal affinity for ABI1. Ref.8

Mutagenesis

112

1

S → A: Reduced binding affinity and inhibitory activity toward ABI1. Ref.8

Mutagenesis

114

1

L → A: Reduced affinity for ABI1. Ref.8

Mutagenesis

115

1

P → A: Reduced affinity for ABI1. Ref.8

Mutagenesis

142

1

H → A: Loss of affinity for ABI1. Ref.8

Mutagenesis

143

1

R → A: Loss of affinity for ABI1. Ref.8

Mutagenesis

144

1

L → A: Loss of affinity for ABI1. Ref.8

Mutagenesis

178

1

P → A: Normal affinity for ABI1. Ref.8

Mutagenesis

181

1

N → A: Reduced affinity for ABI1. Ref.8

Mutagenesis

189

1

F → A: Reduced affinity for ABI1. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

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.

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.

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221

Helix Strand Turn

Details...

Beta strand

29 – 31

3

Helix

34 – 47

14

Beta strand

56 – 67

12

Helix

69 – 76

8

Helix

82 – 84

3

Beta strand

89 – 93

5

Beta strand

105 – 110

6

Beta strand

113 – 115

3

Beta strand

117 – 127

11

Turn

128 – 131

4

Beta strand

132 – 143

12

Beta strand

148 – 176

29

Helix

183 – 208

26

Sequences

	Sequence		Length	Mass (Da)
	Q8VZS8 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B64B1A52C43072C2	FASTA	221	25,361
	10 20 30 40 50 60 MANSESSSSP VNEEENSQRI STLHHQTMPS DLTQDEFTQL SQSIAEFHTY QLGNGRCSSL 70 80 90 100 110 120 LAQRIHAPPE TVWSVVRRFD RPQIYKHFIK SCNVSEDFEM RVGCTRDVNV ISGLPANTSR 130 140 150 160 170 180 ERLDLLDDDR RVTGFSITGG EHRLRNYKSV TTVHRFEKEE EEERIWTVVL ESYVVDVPEG 190 200 210 220 NSEEDTRLFA DTVIRLNLQK LASITEAMNR NNNNNNSSQV R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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: INTERACTION WITH HAB1, GENE FAMILY, NOMENCLATURE.
[7]	"A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors." Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M., Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J., Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F. , Cutler S.R., Zhu J.-K., Xu H.E. Nature 462:602-608(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-211, DIMERIZATION, INTERACTION WITH HAB1; ABI1 AND ABI2, FUNCTION.
[8]	"Structural basis of abscisic acid signalling." Miyazono K.-I., Miyakawa T., Sawano Y., Kubota K., Kang H.-J., Asano A., Miyauchi Y., Takahashi M., Zhi Y., Fujita Y., Yoshida T., Kodaira K.-S., Yamaguchi-Shinozaki K., Tanokura M. Nature 462:609-614(2009) [PubMed] [Europe PMC] [Abstract] 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.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB016882 Genomic DNA. Translation: BAB08923.1. Different initiation.
CP002688 Genomic DNA. Translation: AED95426.1.
AY063877 mRNA. Translation: AAL36233.1.
AY117328 mRNA. Translation: AAM51403.1.

IPI

IPI00537816.

RefSeq

NP_199491.2. NM_124049.4.

UniGene

At.27159.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JRQ	X-ray	2.10	B	28-210	[»]
3JRS	X-ray	2.05	A/B/C	8-211	[»]
3KAY	X-ray	2.40	A/B	36-211	[»]
3KDJ	X-ray	1.88	A	20-221	[»]
3NEF	X-ray	2.40	A/B	20-221	[»]
3NEG	X-ray	2.80	A/B	20-221	[»]
3NMN	X-ray	2.15	A/C	36-211	[»]

ProteinModelPortal

Q8VZS8.

SMR

Q8VZS8. Positions 31-209.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48581N.

IntAct

Q8VZS8. 3 interactions.

MINT

MINT-8299470.

STRING

3702.AT5G46790.1-P.

Proteomic databases

PaxDb

Q8VZS8.

PRIDE

Q8VZS8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G46790.1; AT5G46790.1; AT5G46790.

GeneID

834722.

KEGG

ath:AT5G46790.

Organism-specific databases

TAIR

At5g46790.

Phylogenomic databases

eggNOG

NOG235377.

HOGENOM

HOG000238422.

InParanoid

Q8VZS8.

KO

K14496.

OMA

MANSESS.

PhylomeDB

Q8VZS8.

ProtClustDB

CLSN2686022.

Gene expression databases

Genevestigator

Q8VZS8.

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...

Other

EvolutionaryTrace

Q8VZS8.

Entry information

Entry name

PYL1_ARATH

Accession

Primary (citable) accession number: Q8VZS8
Secondary accession number(s): Q9FIP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 2, 2010
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program