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Q1ECF1 (PYL7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Abscisic acid receptor PYL7
Alternative name(s):
ABI1-binding protein 7
PYR1-like protein 7
Regulatory components of ABA receptor 2
Gene names
Name:PYL7
Synonyms:ABIP7, RCAR2
Ordered Locus Names:At4g01026
ORF Names:F3I3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

Subunit structure

Homodimer. Binds ABA on one subunit only By similarity. Interacts with ABI1, and possibly with other PP2Cs. Ref.5

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 By similarity.

Sequence similarities

Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family.

Sequence caution

The sequence AAM65054.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB45785.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At4g01020 has been split into 2 genes: At4g01020 and At4g01026.

The sequence CAB80911.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At4g01020 has been split into 2 genes: At4g01020 and At4g01026.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Abscisic acid receptor PYL7
PRO_0000391742

Regions

Region29 – 180152START-like
Region93 – 986ABA binding By similarity
Region120 – 1267ABA binding By similarity
Motif89 – 935Gate loop By similarity
Motif119 – 1213Latch loop By similarity

Sites

Binding site651ABA By similarity
Binding site1451ABA By similarity
Site921Involved in interactions with PP2Cs By similarity
Site1561Involved in interactions with PP2Cs By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1ECF1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 6381793C94A43C32

FASTA21123,676
        10         20         30         40         50         60 
MEMIGGDDTD TEMYGALVTA QSLRLRHLHH CRENQCTSVL VKYIQAPVHL VWSLVRRFDQ 

        70         80         90        100        110        120 
PQKYKPFISR CTVNGDPEIG CLREVNVKSG LPATTSTERL EQLDDEEHIL GINIIGGDHR 

       130        140        150        160        170        180 
LKNYSSILTV HPEMIDGRSG TMVMESFVVD VPQGNTKDDT CYFVESLIKC NLKSLACVSE 

       190        200        210 
RLAAQDITNS IATFCNASNG YREKNHTETN L 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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]"Arabidopsis ORF clones."
Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
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]"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.
[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: GENE FAMILY.
[7]"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. expand/collapse author list , Schroeder J.I., Volkman B.F., Cutler S.R.
Science 324:1068-1071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL080237 Genomic DNA. Translation: CAB45785.1. Sequence problems.
AL161491 Genomic DNA. Translation: CAB80911.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE81969.1.
BT025783 mRNA. Translation: ABF83673.1.
AY087511 mRNA. Translation: AAM65054.1. Different initiation.
PIRT10542.
RefSeqNP_567208.1. NM_116332.3.
UniGeneAt.19744.
At.75231.

3D structure databases

ProteinModelPortalQ1ECF1.
SMRQ1ECF1. Positions 21-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13214. 5 interactions.
IntActQ1ECF1. 2 interactions.
STRING3702.AT4G01026.1-P.

Proteomic databases

PRIDEQ1ECF1.

Protocols and materials databases

DNASU827923.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G01026.1; AT4G01026.1; AT4G01026.
GeneID827923.
KEGGath:AT4G01026.

Organism-specific databases

TAIRAT4G01026.

Phylogenomic databases

eggNOGNOG303563.
HOGENOMHOG000238422.
InParanoidQ1ECF1.
KOK14496.
OMAEHILGIN.
PhylomeDBQ1ECF1.
ProtClustDBCLSN2917474.

Gene expression databases

GenevestigatorQ1ECF1.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR019587. Polyketide_cyclase/dehydratase.
IPR023393. START-like_dom.
[Graphical view]
PfamPF10604. Polyketide_cyc2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYL7_ARATH
AccessionPrimary (citable) accession number: Q1ECF1
Secondary accession number(s): Q8LAZ6, Q9SV27
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names