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Protein

Protein PHOSPHATE STARVATION RESPONSE 1

Gene

PHR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor involved in phosphate starvation signaling (PubMed:11511543, PubMed:17927693, PubMed:26586833). Binds as a dimer to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to promote the expression of inorganic phosphate (Pi) starvation-responsive genes (PubMed:11511543, PubMed:20838596, PubMed:26586833). SPX1 is a competitive inhibitor of this DNA-binding (PubMed:25271326). PHR1 binding to its targets is low Pi-dependent (PubMed:25271326). Regulates the expression of miR399 (PubMed:20838596). Regulates the expression of IPS1 (At3g09922), a non-coding RNA that mimics the target of miR399 to block the cleavage of PHO2 under Pi-deficient conditions (PubMed:17643101). Regulates lipid remodeling and triacylglycerol accumulation during phosphorus starvation (PubMed:25680792). Required for the shoot-specific hypoxic response (PubMed:24753539). Regulates FER1 expression upon phosphate starvation, linking iron and phosphate homeostasis (PubMed:23788639). Contributes to the homeostasis of both sulfate and phosphate in plants under phosphate deficiency (PubMed:21261953). Required for adaptation to high light and retaining functional photosynthesis during phosphate starvation (PubMed:21910737). Involved in the coregulation of Zn and Pi homeostasis (PubMed:24420568).12 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi253 – 27826H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: TAIR

GO - Biological processi

  • cellular response to high light intensity Source: TAIR
  • cellular response to phosphate starvation Source: TAIR
  • circadian rhythm Source: TAIR
  • regulation of transcription, DNA-templated Source: TAIR
  • sulfate ion homeostasis Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PHOSPHATE STARVATION RESPONSE 11 Publication
Short name:
AtPHR11 Publication
Gene namesi
Name:PHR11 Publication
Ordered Locus Names:At4g28610Imported
ORF Names:T5F17.60Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G28610.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: The localization to the nucleus is independent of the Pi status.1 Publication

GO - Cellular componenti

  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Strongly reduced shoot growth, and slightly increased root growth. Reduced expression of phosphate starvation-induced (PSI) genes, decreased cellular inorganic phosphate (Pi) content and shoot-to-root ratio, and impaired anthocyanin accumulation (PubMed:17927693).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Protein PHOSPHATE STARVATION RESPONSE 1PRO_0000436713Add
BLAST

Post-translational modificationi

Sumoylated by SIZ1. Sumoylation controls phosphate deficiency responses.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9M0H0.
PRIDEiQ9M0H0.

Expressioni

Inductioni

Only moderately up-regulated by Pi starvation.1 Publication

Interactioni

Subunit structurei

Homodimers and heterodimers (PubMed:20838596, PubMed:11511543). Interacts with SPX1 in a Pi-dependent manner (PubMed:25271326). Does not interact with PHL2 or PHL3 (PubMed:26586833).3 Publications

Protein-protein interaction databases

STRINGi3702.AT4G28610.1.

Structurei

3D structure databases

SMRiQ94CL7. Positions 225-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 28261HTH myb-typePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili314 – 33421Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi327 – 3326LHEQLECurated

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi67 – 715Poly-SerSequence analysis

Sequence similaritiesi

Belongs to the MYB-CC family.Curated
Contains 1 HTH myb-type DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEM5. Eukaryota.
ENOG410YG61. LUCA.
HOGENOMiHOG000064669.
OMAiEETRKCE.
PhylomeDBiQ94CL7.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR025756. Myb_CC_LHEQLE.
IPR017930. Myb_dom.
IPR006447. Myb_dom_plants.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF14379. Myb_CC_LHEQLE. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
TIGRFAMsiTIGR01557. myb_SHAQKYF. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q94CL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEARPVHRSG SRDLTRTSSI PSTQKPSPVE DSFMRSDNNS QLMSRPLGQT
60 70 80 90 100
YHLLSSSNGG AVGHICSSSS SGFATNLHYS TMVSHEKQQH YTGSSSNNAV
110 120 130 140 150
QTPSNNDSAW CHDSLPGGFL DFHETNPAIQ NNCQIEDGGI AAAFDDIQKR
160 170 180 190 200
SDWHEWADHL ITDDDPLMST NWNDLLLETN SNSDSKDQKT LQIPQPQIVQ
210 220 230 240 250
QQPSPSVELR PVSTTSSNSN NGTGKARMRW TPELHEAFVE AVNSLGGSER
260 270 280 290 300
ATPKGVLKIM KVEGLTIYHV KSHLQKYRTA RYRPEPSETG SPERKLTPLE
310 320 330 340 350
HITSLDLKGG IGITEALRLQ MEVQKQLHEQ LEIQRNLQLR IEEQGKYLQM
360 370 380 390 400
MFEKQNSGLT KGTASTSDSA AKSEQEDKKT ADSKEVPEEE TRKCEELESP

QPKRPKIDN
Length:409
Mass (Da):45,546
Last modified:December 1, 2001 - v1
Checksum:i2C59836D75FE33C3
GO

Sequence cautioni

The sequence CAB81449.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310799 mRNA. Translation: CAC59689.1.
AL161573 Genomic DNA. Translation: CAB81449.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85512.1.
AY081290 mRNA. Translation: AAL91179.1.
BT002187 mRNA. Translation: AAN72198.1.
PIRiT10655.
RefSeqiNP_194590.2. NM_119003.3.
UniGeneiAt.4525.

Genome annotation databases

EnsemblPlantsiAT4G28610.1; AT4G28610.1; AT4G28610.
GeneIDi828979.
GrameneiAT4G28610.1; AT4G28610.1; AT4G28610.
KEGGiath:AT4G28610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310799 mRNA. Translation: CAC59689.1.
AL161573 Genomic DNA. Translation: CAB81449.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85512.1.
AY081290 mRNA. Translation: AAL91179.1.
BT002187 mRNA. Translation: AAN72198.1.
PIRiT10655.
RefSeqiNP_194590.2. NM_119003.3.
UniGeneiAt.4525.

3D structure databases

SMRiQ94CL7. Positions 225-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G28610.1.

Proteomic databases

PaxDbiQ9M0H0.
PRIDEiQ9M0H0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G28610.1; AT4G28610.1; AT4G28610.
GeneIDi828979.
GrameneiAT4G28610.1; AT4G28610.1; AT4G28610.
KEGGiath:AT4G28610.

Organism-specific databases

TAIRiAT4G28610.

Phylogenomic databases

eggNOGiENOG410IEM5. Eukaryota.
ENOG410YG61. LUCA.
HOGENOMiHOG000064669.
OMAiEETRKCE.
PhylomeDBiQ94CL7.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR025756. Myb_CC_LHEQLE.
IPR017930. Myb_dom.
IPR006447. Myb_dom_plants.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF14379. Myb_CC_LHEQLE. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
TIGRFAMsiTIGR01557. myb_SHAQKYF. 1 hit.
PROSITEiPS51294. HTH_MYB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A conserved MYB transcription factor involved in phosphate starvation signaling both in vascular plants and in unicellular algae."
    Rubio V., Linhares F., Solano R., Martin A.C., Iglesias J., Leyva A., Paz-Ares J.
    Genes Dev. 15:2122-2133(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INDUCTION BY PHOSPHATE, GENE FAMILY, SUBCELLULAR LOCATION.
  2. "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.
  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. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. Cited for: SUMOYLATION.
  6. Cited for: FUNCTION.
  7. "Increased expression of the MYB-related transcription factor, PHR1, leads to enhanced phosphate uptake in Arabidopsis thaliana."
    Nilsson L., Mueller R., Nielsen T.H.
    Plant Cell Environ. 30:1499-1512(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A central regulatory system largely controls transcriptional activation and repression responses to phosphate starvation in Arabidopsis."
    Bustos R., Castrillo G., Linhares F., Puga M.I., Rubio V., Perez-Perez J., Solano R., Leyva A., Paz-Ares J.
    PLoS Genet. 6:E1001102-E1001102(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  11. "The transcription factor PHR1 plays a key role in the regulation of sulfate shoot-to-root flux upon phosphate starvation in Arabidopsis."
    Rouached H., Secco D., Arpat B., Poirier Y.
    BMC Plant Biol. 11:19-19(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The Arabidopsis transcription factor PHR1 is essential for adaptation to high light and retaining functional photosynthesis during phosphate starvation."
    Nilsson L., Lundmark M., Jensen P.E., Nielsen T.H.
    Physiol. Plantarum 144:35-47(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Arabidopsis ferritin 1 (AtFer1) gene regulation by the phosphate starvation response 1 (AtPHR1) transcription factor reveals a direct molecular link between iron and phosphate homeostasis."
    Bournier M., Tissot N., Mari S., Boucherez J., Lacombe E., Briat J.F., Gaymard F.
    J. Biol. Chem. 288:22670-22680(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Coordination between zinc and phosphate homeostasis involves the transcription factor PHR1, the phosphate exporter PHO1, and its homologue PHO1;H3 in Arabidopsis."
    Khan G.A., Bouraine S., Wege S., Li Y., de Carbonnel M., Berthomieu P., Poirier Y., Rouached H.
    J. Exp. Bot. 65:871-884(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "A Shoot-specific hypoxic response of Arabidopsis sheds light on the role of the phosphate-responsive transcription factor PHOSPHATE STARVATION RESPONSE1."
    Klecker M., Gasch P., Peisker H., Doermann P., Schlicke H., Grimm B., Mustroph A.
    Plant Physiol. 165:774-790(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: FUNCTION, INTERACTION WITH SPX1.
  17. "The transcription factor PHR1 regulates lipid remodeling and triacylglycerol accumulation in Arabidopsis thaliana during phosphorus starvation."
    Pant B.D., Burgos A., Pant P., Cuadros-Inostroza A., Willmitzer L., Scheible W.R.
    J. Exp. Bot. 66:1907-1918(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Arabidopsis PHL2 and PHR1 act redundantly as the key components of the central regulatory system controlling transcriptional responses to phosphate starvation."
    Sun L., Song L., Zhang Y., Zheng Z., Liu D.
    Plant Physiol. 170:499-514(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LACK OF INTERACTION WITH PHL2 AND PHL3.

Entry informationi

Entry nameiPHR1_ARATH
AccessioniPrimary (citable) accession number: Q94CL7
Secondary accession number(s): Q9M0H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 124 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

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.