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Protein

Protein NRT1/ PTR FAMILY 6.3

Gene

NPF6.3

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

Functioni

Dual affinity nitrate transporter. Involved in proton-dependent nitrate uptake and in the regulation of the nitrate transporter NRT2.1. Acts also as a nitrate sensor that trigger a specific signaling pathway stimulating lateral root growth and seed germination. The uptake activity is not required for sensor function. Displays an auxin transport facilitation inhibited by high nitrate concentration. Required to prevent auxin accumulation in preemerged lateral root primordia and young lateral roots when external nitrate concentration is low or null. May be involved in the basipetal transport of auxin out of the lateral root tips. Acts as a bidirectional transporter involved in root-to-shoot nitrate translocation. Recognizes specifically nitrate and chlorate, but not nitrite, alanine, sulfate, phosphate or the di-peptide Ala-Ala.11 Publications

Kineticsi

  1. KM=49 µM for nitrate (for the high-affinity phase, in the presence of 250 µM nitrate at pH 5.5)1 Publication
  2. KM=4 mM for nitrate (for the low-affinity phase, in the presence of 10 mM nitrate at pH 5.5)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei356 – 3561Substrate
    Binding sitei360 – 3601Substrate

    GO - Molecular functioni

    • nitrate transmembrane transporter activity Source: TAIR
    • symporter activity Source: UniProtKB-KW

    GO - Biological processi

    • auxin-activated signaling pathway Source: UniProtKB-KW
    • nitrate assimilation Source: UniProtKB-KW
    • nitrate transport Source: TAIR
    • oligopeptide transport Source: InterPro
    • response to herbicide Source: UniProtKB-KW
    • response to nitrate Source: TAIR
    • response to water deprivation Source: TAIR
    Complete GO annotation...

    Keywords - Biological processi

    Auxin signaling pathway, Herbicide resistance, Nitrate assimilation, Symport, Transport

    Protein family/group databases

    TCDBi2.A.17.3.1. the proton-dependent oligopeptide transporter (pot/ptr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein NRT1/ PTR FAMILY 6.3
    Short name:
    AtNPF6.3
    Alternative name(s):
    Nitrate transporter 1.1
    Short name:
    AtNRT1
    Nitrate/chlorate transporter
    Protein CHLORINA 1
    Gene namesi
    Name:NPF6.3
    Synonyms:CHL1, NRT1, NRT1.1
    Ordered Locus Names:At1g12110
    ORF Names:F12F1.1, T28K15_13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G12110.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6621HelicalSequence analysisAdd
    BLAST
    Transmembranei77 – 9721HelicalSequence analysisAdd
    BLAST
    Transmembranei102 – 12221HelicalSequence analysisAdd
    BLAST
    Transmembranei143 – 16321HelicalSequence analysisAdd
    BLAST
    Transmembranei193 – 21321HelicalSequence analysisAdd
    BLAST
    Transmembranei219 – 23921HelicalSequence analysisAdd
    BLAST
    Transmembranei342 – 36221HelicalSequence analysisAdd
    BLAST
    Transmembranei374 – 39421HelicalSequence analysisAdd
    BLAST
    Transmembranei423 – 44321HelicalSequence analysisAdd
    BLAST
    Transmembranei460 – 48021HelicalSequence analysisAdd
    BLAST
    Transmembranei501 – 52121HelicalSequence analysisAdd
    BLAST
    Transmembranei542 – 56221HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • integral component of membrane Source: UniProtKB-KW
    • plasma membrane Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Altered development of nascent organs. Reduced stomatal opening and reduced transpiration rates in the light resulting in enhanced drought tolerance. Slower translocation of nitrate to the leaves.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281T → A: No effect on phosphorylation and on nitrate transport. 1 Publication
    Mutagenesisi41 – 411E → A: Loss of the transporter activity. 1 Publication
    Mutagenesisi44 – 441E → A: Loss of the transporter activity. 1 Publication
    Mutagenesisi45 – 451R → A: Loss of the transporter activity. 2 Publications
    Mutagenesisi101 – 1011T → A: Loss of phosphorylation and 91% reduction of high-affinity nitrate transport, but no effect on the nitrate binding. 2 Publications
    Mutagenesisi101 – 1011T → D: Loss of low-affinity nitrate transport. 2 Publications
    Mutagenesisi130 – 1301C → A: 90% reduction of the transporter activity. 1 Publication
    Mutagenesisi164 – 1641K → A: 90% reduction of the transporter activity. 2 Publications
    Mutagenesisi356 – 3561H → A: Loss of the transporter activity. 2 Publications
    Mutagenesisi476 – 4761E → A: 80% reduction of the transporter activity. 1 Publication
    Mutagenesisi492 – 4921P → L in chl1-9; loss of high- and low-affinity nitrate transport, but no effect on nitrate sensing. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 590590Protein NRT1/ PTR FAMILY 6.3PRO_0000064316Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011Phosphothreonine; by CIPK231 Publication

    Post-translational modificationi

    Acts as a high-affinity nitrate transporter when phosphorylated and as a low-affinity transporter when dephosphorylated. Forms homodimer when unphosphorylated and monomer when phosphorylated. Low nitrogen concentration in the medium stimulates phosphorylation. Phosphorylation also regulates the nitrate signaling.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ05085.
    PRIDEiQ05085.

    PTM databases

    iPTMnetiQ05085.

    Expressioni

    Tissue specificityi

    Expressed in the stele in lateral root primordia before emergence and in the tip of primary and emerged lateral roots. Detected in emerging and immature leaves, guard cells, flower buds, style, stigma, anthers and pollen grains. Not detected in the shoot apical meristem.4 Publications

    Developmental stagei

    Expressed in the columella root cap at day 1 after germination. At day 3, detected in the root meristematic region and at day 5, expressed throughout the root tip.1 Publication

    Inductioni

    By nitrate and auxin.4 Publications

    Gene expression databases

    GenevisibleiQ05085. AT.

    Interactioni

    Subunit structurei

    Monomer and homodimer. The dimer has the 2 monomers in the same orientation. Interacts with CIPK23.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CIPK23Q93VD33EBI-2463703,EBI-974277

    Protein-protein interaction databases

    BioGridi23003. 21 interactions.
    IntActiQ05085. 1 interaction.
    STRINGi3702.AT1G12110.1.

    Structurei

    Secondary structure

    1
    590
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 203Combined sources
    Beta strandi25 – 295Combined sources
    Helixi33 – 375Combined sources
    Helixi39 – 5315Combined sources
    Helixi56 – 616Combined sources
    Helixi67 – 9428Combined sources
    Helixi98 – 12124Combined sources
    Turni132 – 1343Combined sources
    Helixi143 – 17129Combined sources
    Helixi172 – 1743Combined sources
    Helixi182 – 1843Combined sources
    Helixi185 – 20420Combined sources
    Helixi207 – 2148Combined sources
    Helixi217 – 23620Combined sources
    Helixi237 – 2415Combined sources
    Helixi251 – 26111Combined sources
    Beta strandi277 – 2793Combined sources
    Helixi330 – 34011Combined sources
    Helixi343 – 3475Combined sources
    Helixi350 – 36011Combined sources
    Helixi362 – 3698Combined sources
    Helixi381 – 3855Combined sources
    Helixi386 – 40116Combined sources
    Helixi403 – 4075Combined sources
    Turni408 – 4103Combined sources
    Beta strandi414 – 4174Combined sources
    Helixi419 – 44830Combined sources
    Helixi462 – 4654Combined sources
    Helixi466 – 49025Combined sources
    Helixi497 – 52529Combined sources
    Turni526 – 5283Combined sources
    Helixi536 – 5383Combined sources
    Helixi542 – 56928Combined sources
    Turni572 – 5743Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4OH3X-ray3.25A/B1-590[»]
    5A2NX-ray3.70A/B1-590[»]
    5A2OX-ray3.71A/B1-590[»]
    ProteinModelPortaliQ05085.
    SMRiQ05085. Positions 9-581.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1237. Eukaryota.
    COG3104. LUCA.
    HOGENOMiHOG000237400.
    InParanoidiQ05085.
    OMAiHGLRPLQ.
    PhylomeDBiQ05085.

    Family and domain databases

    InterProiIPR020846. MFS_dom.
    IPR000109. POT_fam.
    IPR018456. PTR2_symporter_CS.
    [Graphical view]
    PANTHERiPTHR11654. PTHR11654. 1 hit.
    PfamiPF00854. PTR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 2 hits.
    PROSITEiPS01022. PTR2_1. 1 hit.
    PS01023. PTR2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q05085-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLPETKSDD ILLDAWDFQG RPADRSKTGG WASAAMILCI EAVERLTTLG
    60 70 80 90 100
    IGVNLVTYLT GTMHLGNATA ANTVTNFLGT SFMLCLLGGF IADTFLGRYL
    110 120 130 140 150
    TIAIFAAIQA TGVSILTLST IIPGLRPPRC NPTTSSHCEQ ASGIQLTVLY
    160 170 180 190 200
    LALYLTALGT GGVKASVSGF GSDQFDETEP KERSKMTYFF NRFFFCINVG
    210 220 230 240 250
    SLLAVTVLVY VQDDVGRKWG YGICAFAIVL ALSVFLAGTN RYRFKKLIGS
    260 270 280 290 300
    PMTQVAAVIV AAWRNRKLEL PADPSYLYDV DDIIAAEGSM KGKQKLPHTE
    310 320 330 340 350
    QFRSLDKAAI RDQEAGVTSN VFNKWTLSTL TDVEEVKQIV RMLPIWATCI
    360 370 380 390 400
    LFWTVHAQLT TLSVAQSETL DRSIGSFEIP PASMAVFYVG GLLLTTAVYD
    410 420 430 440 450
    RVAIRLCKKL FNYPHGLRPL QRIGLGLFFG SMAMAVAALV ELKRLRTAHA
    460 470 480 490 500
    HGPTVKTLPL GFYLLIPQYL IVGIGEALIY TGQLDFFLRE CPKGMKGMST
    510 520 530 540 550
    GLLLSTLALG FFFSSVLVTI VEKFTGKAHP WIADDLNKGR LYNFYWLVAV
    560 570 580 590
    LVALNFLIFL VFSKWYVYKE KRLAEVGIEL DDEPSIPMGH
    Length:590
    Mass (Da):64,922
    Last modified:June 1, 1994 - v1
    Checksum:i78D3E660AAF90D47
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10357 mRNA. Translation: AAA32770.1.
    AC002131 Genomic DNA. Translation: AAC17604.1.
    CP002684 Genomic DNA. Translation: AEE28838.1.
    BT002016 mRNA. Translation: AAN72027.1.
    BT008783 mRNA. Translation: AAP68222.1.
    AK317498 mRNA. Translation: BAH20163.1.
    PIRiA45772.
    RefSeqiNP_563899.1. NM_101083.3.
    UniGeneiAt.19624.

    Genome annotation databases

    EnsemblPlantsiAT1G12110.1; AT1G12110.1; AT1G12110.
    GeneIDi837763.
    GrameneiAT1G12110.1; AT1G12110.1; AT1G12110.
    KEGGiath:AT1G12110.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L10357 mRNA. Translation: AAA32770.1.
    AC002131 Genomic DNA. Translation: AAC17604.1.
    CP002684 Genomic DNA. Translation: AEE28838.1.
    BT002016 mRNA. Translation: AAN72027.1.
    BT008783 mRNA. Translation: AAP68222.1.
    AK317498 mRNA. Translation: BAH20163.1.
    PIRiA45772.
    RefSeqiNP_563899.1. NM_101083.3.
    UniGeneiAt.19624.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4OH3X-ray3.25A/B1-590[»]
    5A2NX-ray3.70A/B1-590[»]
    5A2OX-ray3.71A/B1-590[»]
    ProteinModelPortaliQ05085.
    SMRiQ05085. Positions 9-581.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi23003. 21 interactions.
    IntActiQ05085. 1 interaction.
    STRINGi3702.AT1G12110.1.

    Protein family/group databases

    TCDBi2.A.17.3.1. the proton-dependent oligopeptide transporter (pot/ptr) family.

    PTM databases

    iPTMnetiQ05085.

    Proteomic databases

    PaxDbiQ05085.
    PRIDEiQ05085.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G12110.1; AT1G12110.1; AT1G12110.
    GeneIDi837763.
    GrameneiAT1G12110.1; AT1G12110.1; AT1G12110.
    KEGGiath:AT1G12110.

    Organism-specific databases

    TAIRiAT1G12110.

    Phylogenomic databases

    eggNOGiKOG1237. Eukaryota.
    COG3104. LUCA.
    HOGENOMiHOG000237400.
    InParanoidiQ05085.
    OMAiHGLRPLQ.
    PhylomeDBiQ05085.

    Miscellaneous databases

    PROiQ05085.

    Gene expression databases

    GenevisibleiQ05085. AT.

    Family and domain databases

    InterProiIPR020846. MFS_dom.
    IPR000109. POT_fam.
    IPR018456. PTR2_symporter_CS.
    [Graphical view]
    PANTHERiPTHR11654. PTHR11654. 1 hit.
    PfamiPF00854. PTR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 2 hits.
    PROSITEiPS01022. PTR2_1. 1 hit.
    PS01023. PTR2_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-inducible nitrate transporter."
      Tsay Y.-F., Schroeder J.I., Feldmann K.A., Crawford N.M.
      Cell 72:705-713(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.
    5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "The Arabidopsis CHL1 protein plays a major role in high-affinity nitrate uptake."
      Wang R., Liu D., Crawford N.M.
      Proc. Natl. Acad. Sci. U.S.A. 95:15134-15139(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "CHL1 is a dual-affinity nitrate transporter of Arabidopsis involved in multiple phases of nitrate uptake."
      Liu K.H., Huang C.Y., Tsay Y.F.
      Plant Cell 11:865-874(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY NITRATE.
    8. "The Arabidopsis dual-affinity nitrate transporter gene AtNRT1.1 (CHL1) is activated and functions in nascent organ development during vegetative and reproductive growth."
      Guo F.Q., Wang R., Chen M., Crawford N.M.
      Plant Cell 13:1761-1777(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    9. "The Arabidopsis dual-affinity nitrate transporter gene AtNRT1.1 (CHL1) is regulated by auxin in both shoots and roots."
      Guo F.Q., Wang R., Crawford N.M.
      J. Exp. Bot. 53:835-844(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY AUXIN.
    10. "Switching between the two action modes of the dual-affinity nitrate transporter CHL1 by phosphorylation."
      Liu K.H., Tsay Y.F.
      EMBO J. 22:1005-1013(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-28 AND THR-101, PHOSPHORYLATION AT THR-101.
    11. "The nitrate transporter AtNRT1.1 (CHL1) functions in stomatal opening and contributes to drought susceptibility in Arabidopsis."
      Guo F.Q., Young J., Crawford N.M.
      Plant Cell 15:107-117(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    12. "Regulation of NRT1 and NRT2 gene families of Arabidopsis thaliana: responses to nitrate provision."
      Okamoto M., Vidmar J.J., Glass A.D.
      Plant Cell Physiol. 44:304-317(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, INDUCTION BY NITRATE.
    13. "Microarray analysis of the nitrate response in Arabidopsis roots and shoots reveals over 1,000 rapidly responding genes and new linkages to glucose, trehalose-6-phosphate, iron, and sulfate metabolism."
      Wang R., Okamoto M., Xing X., Crawford N.M.
      Plant Physiol. 132:556-567(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY NITRATE.
    14. "Transcript profiling in the chl1-5 mutant of Arabidopsis reveals a role of the nitrate transporter NRT1.1 in the regulation of another nitrate transporter, NRT2.1."
      Munos S., Cazettes C., Fizames C., Gaymard F., Tillard P., Lepetit M., Lejay L., Gojon A.
      Plant Cell 16:2433-2447(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    15. "The Arabidopsis NRT1.1 transporter participates in the signaling pathway triggering root colonization of nitrate-rich patches."
      Remans T., Nacry P., Pervent M., Filleur S., Diatloff E., Mounier E., Tillard P., Forde B.G., Gojon A.
      Proc. Natl. Acad. Sci. U.S.A. 103:19206-19211(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Nitrate transporters and peptide transporters."
      Tsay Y.F., Chiu C.C., Tsai C.B., Ho C.H., Hsu P.K.
      FEBS Lett. 581:2290-2300(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, GENE FAMILY.
    17. "CHL1 functions as a nitrate sensor in plants."
      Ho C.H., Lin S.H., Hu H.C., Tsay Y.F.
      Cell 138:1184-1194(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF PRO-492, INTERACTION WITH CIPK23.
    18. "A genetic screen for nitrate regulatory mutants captures the nitrate transporter gene NRT1.1."
      Wang R., Xing X., Wang Y., Tran A., Crawford N.M.
      Plant Physiol. 151:472-478(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Nitrate-regulated auxin transport by NRT1.1 defines a mechanism for nutrient sensing in plants."
      Krouk G., Lacombe B., Bielach A., Perrine-Walker F., Malinska K., Mounier E., Hoyerova K., Tillard P., Leon S., Ljung K., Zazimalova E., Benkova E., Nacry P., Gojon A.
      Dev. Cell 18:927-937(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    20. "Arabidopsis NRT1.1 is a bidirectional transporter involved in root-to-shoot nitrate translocation."
      Leran S., Munos S., Brachet C., Tillard P., Gojon A., Lacombe B.
      Mol. Plant 6:1984-1987(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    21. Cited for: GENE FAMILY, NOMENCLATURE.
    22. "Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1."
      Parker J.L., Newstead S.
      Nature 507:68-72(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN COMPLEX WITH NITRATE, SUBSTRATE, MUTAGENESIS OF ARG-45; THR-101; LYS-164 AND HIS-356.
    23. "Crystal structure of the plant dual-affinity nitrate transporter NRT1.1."
      Sun J., Bankston J.R., Payandeh J., Hinds T.R., Zagotta W.N., Zheng N.
      Nature 507:73-77(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) IN COMPLEX WITH NITRATE, SUBUNIT, MUTAGENESIS OF GLU-41; GLU-44; ARG-45; CYS-130; LYS-164; HIS-356 AND GLU-476.

    Entry informationi

    Entry nameiPTR7_ARATH
    AccessioniPrimary (citable) accession number: Q05085
    Secondary accession number(s): B9DHE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: February 17, 2016
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    When mutated confers resistance to the herbicide chlorate.
    The kinase CIPK23 is a negative regulator of the high-affinity response, while the kinase CIPK8 is a positive regulator of the low-affinity response. Thr-101 is not the direct target of CIPK8.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.