Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q1ECF1

- PYL7_ARATH

UniProt

Q1ECF1 - PYL7_ARATH

Protein

Abscisic acid receptor PYL7

Gene

PYL7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (11 Jul 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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) when activated by ABA By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651ABABy similarity
    Sitei92 – 921Involved in interactions with PP2CsBy similarity
    Binding sitei145 – 1451ABABy similarity
    Sitei156 – 1561Involved in interactions with PP2CsBy similarity

    GO - Molecular functioni

    1. abscisic acid binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. receptor activity Source: UniProtKB

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Abscisic acid signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abscisic acid receptor PYL7
    Alternative name(s):
    ABI1-binding protein 7
    PYR1-like protein 7
    Regulatory components of ABA receptor 2
    Gene namesi
    Name:PYL7
    Synonyms:ABIP7, RCAR2
    Ordered Locus Names:At4g01026
    ORF Names:F3I3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G01026.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Abscisic acid receptor PYL7PRO_0000391742Add
    BLAST

    Proteomic databases

    PRIDEiQ1ECF1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ1ECF1.

    Interactioni

    Subunit structurei

    Homodimer. Binds ABA on one subunit only By similarity. Interacts with ABI1, and possibly with other PP2Cs.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi13214. 5 interactions.
    IntActiQ1ECF1. 2 interactions.
    STRINGi3702.AT4G01026.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1ECF1.
    SMRiQ1ECF1. Positions 21-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 180152START-likeAdd
    BLAST
    Regioni93 – 986ABA bindingBy similarity
    Regioni120 – 1267ABA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi89 – 935Gate loopBy similarity
    Motifi119 – 1213Latch 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

    eggNOGiNOG303563.
    HOGENOMiHOG000238422.
    InParanoidiQ1ECF1.
    KOiK14496.
    OMAiEHILGIN.
    PhylomeDBiQ1ECF1.

    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.

    Q1ECF1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMIGGDDTD TEMYGALVTA QSLRLRHLHH CRENQCTSVL VKYIQAPVHL    50
    VWSLVRRFDQ PQKYKPFISR CTVNGDPEIG CLREVNVKSG LPATTSTERL 100
    EQLDDEEHIL GINIIGGDHR LKNYSSILTV HPEMIDGRSG TMVMESFVVD 150
    VPQGNTKDDT CYFVESLIKC NLKSLACVSE RLAAQDITNS IATFCNASNG 200
    YREKNHTETN L 211
    Length:211
    Mass (Da):23,676
    Last modified:July 11, 2006 - v1
    Checksum:i6381793C94A43C32
    GO

    Sequence cautioni

    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 databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiT10542.
    RefSeqiNP_567208.1. NM_116332.3.
    UniGeneiAt.19744.
    At.75231.

    Genome annotation databases

    EnsemblPlantsiAT4G01026.1; AT4G01026.1; AT4G01026.
    GeneIDi827923.
    KEGGiath:AT4G01026.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRi T10542.
    RefSeqi NP_567208.1. NM_116332.3.
    UniGenei At.19744.
    At.75231.

    3D structure databases

    ProteinModelPortali Q1ECF1.
    SMRi Q1ECF1. Positions 21-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 13214. 5 interactions.
    IntActi Q1ECF1. 2 interactions.
    STRINGi 3702.AT4G01026.1-P.

    Proteomic databases

    PRIDEi Q1ECF1.

    Protocols and materials databases

    DNASUi 827923.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G01026.1 ; AT4G01026.1 ; AT4G01026 .
    GeneIDi 827923.
    KEGGi ath:AT4G01026.

    Organism-specific databases

    TAIRi AT4G01026.

    Phylogenomic databases

    eggNOGi NOG303563.
    HOGENOMi HOG000238422.
    InParanoidi Q1ECF1.
    KOi K14496.
    OMAi EHILGIN.
    PhylomeDBi Q1ECF1.

    Gene expression databases

    Genevestigatori Q1ECF1.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR019587. Polyketide_cyclase/dehydratase.
    IPR023393. START-like_dom.
    [Graphical view ]
    Pfami PF10604. Polyketide_cyc2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiPYL7_ARATH
    AccessioniPrimary (citable) accession number: Q1ECF1
    Secondary accession number(s): Q8LAZ6, Q9SV27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 2, 2010
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 54 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

    External Data

    Dasty 3