PTR7_ARATH
ID PTR7_ARATH Reviewed; 590 AA.
AC Q05085; B9DHE6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein NRT1/ PTR FAMILY 6.3;
DE Short=AtNPF6.3;
DE AltName: Full=Nitrate transporter 1.1;
DE Short=AtNRT1;
DE AltName: Full=Nitrate/chlorate transporter;
DE AltName: Full=Protein CHLORINA 1;
GN Name=NPF6.3; Synonyms=CHL1, NRT1, NRT1.1; OrderedLocusNames=At1g12110;
GN ORFNames=F12F1.1, T28K15_13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8453665; DOI=10.1016/0092-8674(93)90399-b;
RA Tsay Y.-F., Schroeder J.I., Feldmann K.A., Crawford N.M.;
RT "The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-
RT inducible nitrate transporter.";
RL Cell 72:705-713(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION.
RX PubMed=9844028; DOI=10.1073/pnas.95.25.15134;
RA Wang R., Liu D., Crawford N.M.;
RT "The Arabidopsis CHL1 protein plays a major role in high-affinity nitrate
RT uptake.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15134-15139(1998).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY NITRATE.
RX PubMed=10330471; DOI=10.2307/3870820;
RA Liu K.H., Huang C.Y., Tsay Y.F.;
RT "CHL1 is a dual-affinity nitrate transporter of Arabidopsis involved in
RT multiple phases of nitrate uptake.";
RL Plant Cell 11:865-874(1999).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11487691; DOI=10.2307/3871317;
RA Guo F.Q., Wang R., Chen M., Crawford N.M.;
RT "The Arabidopsis dual-affinity nitrate transporter gene AtNRT1.1 (CHL1) is
RT activated and functions in nascent organ development during vegetative and
RT reproductive growth.";
RL Plant Cell 13:1761-1777(2001).
RN [9]
RP INDUCTION BY AUXIN.
RX PubMed=11912226; DOI=10.1093/jexbot/53.370.835;
RA Guo F.Q., Wang R., Crawford N.M.;
RT "The Arabidopsis dual-affinity nitrate transporter gene AtNRT1.1 (CHL1) is
RT regulated by auxin in both shoots and roots.";
RL J. Exp. Bot. 53:835-844(2002).
RN [10]
RP FUNCTION, MUTAGENESIS OF THR-28 AND THR-101, AND PHOSPHORYLATION AT
RP THR-101.
RX PubMed=12606566; DOI=10.1093/emboj/cdg118;
RA Liu K.H., Tsay Y.F.;
RT "Switching between the two action modes of the dual-affinity nitrate
RT transporter CHL1 by phosphorylation.";
RL EMBO J. 22:1005-1013(2003).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12509525; DOI=10.1105/tpc.006312;
RA Guo F.Q., Young J., Crawford N.M.;
RT "The nitrate transporter AtNRT1.1 (CHL1) functions in stomatal opening and
RT contributes to drought susceptibility in Arabidopsis.";
RL Plant Cell 15:107-117(2003).
RN [12]
RP GENE FAMILY, AND INDUCTION BY NITRATE.
RX PubMed=12668777; DOI=10.1093/pcp/pcg036;
RA Okamoto M., Vidmar J.J., Glass A.D.;
RT "Regulation of NRT1 and NRT2 gene families of Arabidopsis thaliana:
RT responses to nitrate provision.";
RL Plant Cell Physiol. 44:304-317(2003).
RN [13]
RP INDUCTION BY NITRATE.
RX PubMed=12805587; DOI=10.1104/pp.103.021253;
RA Wang R., Okamoto M., Xing X., Crawford N.M.;
RT "Microarray analysis of the nitrate response in Arabidopsis roots and
RT shoots reveals over 1,000 rapidly responding genes and new linkages to
RT glucose, trehalose-6-phosphate, iron, and sulfate metabolism.";
RL Plant Physiol. 132:556-567(2003).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15319483; DOI=10.1105/tpc.104.024380;
RA Munos S., Cazettes C., Fizames C., Gaymard F., Tillard P., Lepetit M.,
RA Lejay L., Gojon A.;
RT "Transcript profiling in the chl1-5 mutant of Arabidopsis reveals a role of
RT the nitrate transporter NRT1.1 in the regulation of another nitrate
RT transporter, NRT2.1.";
RL Plant Cell 16:2433-2447(2004).
RN [15]
RP FUNCTION.
RX PubMed=17148611; DOI=10.1073/pnas.0605275103;
RA Remans T., Nacry P., Pervent M., Filleur S., Diatloff E., Mounier E.,
RA Tillard P., Forde B.G., Gojon A.;
RT "The Arabidopsis NRT1.1 transporter participates in the signaling pathway
RT triggering root colonization of nitrate-rich patches.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19206-19211(2006).
RN [16]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=17481610; DOI=10.1016/j.febslet.2007.04.047;
RA Tsay Y.F., Chiu C.C., Tsai C.B., Ho C.H., Hsu P.K.;
RT "Nitrate transporters and peptide transporters.";
RL FEBS Lett. 581:2290-2300(2007).
RN [17]
RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF PRO-492, AND INTERACTION WITH
RP CIPK23.
RX PubMed=19766570; DOI=10.1016/j.cell.2009.07.004;
RA Ho C.H., Lin S.H., Hu H.C., Tsay Y.F.;
RT "CHL1 functions as a nitrate sensor in plants.";
RL Cell 138:1184-1194(2009).
RN [18]
RP FUNCTION.
RX PubMed=19633234; DOI=10.1104/pp.109.140434;
RA Wang R., Xing X., Wang Y., Tran A., Crawford N.M.;
RT "A genetic screen for nitrate regulatory mutants captures the nitrate
RT transporter gene NRT1.1.";
RL Plant Physiol. 151:472-478(2009).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20627075; DOI=10.1016/j.devcel.2010.05.008;
RA Krouk G., Lacombe B., Bielach A., Perrine-Walker F., Malinska K.,
RA Mounier E., Hoyerova K., Tillard P., Leon S., Ljung K., Zazimalova E.,
RA Benkova E., Nacry P., Gojon A.;
RT "Nitrate-regulated auxin transport by NRT1.1 defines a mechanism for
RT nutrient sensing in plants.";
RL Dev. Cell 18:927-937(2010).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23645597; DOI=10.1093/mp/sst068;
RA Leran S., Munos S., Brachet C., Tillard P., Gojon A., Lacombe B.;
RT "Arabidopsis NRT1.1 is a bidirectional transporter involved in root-to-
RT shoot nitrate translocation.";
RL Mol. Plant 6:1984-1987(2013).
RN [21]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24055139; DOI=10.1016/j.tplants.2013.08.008;
RA Leran S., Varala K., Boyer J.C., Chiurazzi M., Crawford N.,
RA Daniel-Vedele F., David L., Dickstein R., Fernandez E., Forde B.,
RA Gassmann W., Geiger D., Gojon A., Gong J.M., Halkier B.A., Harris J.M.,
RA Hedrich R., Limami A.M., Rentsch D., Seo M., Tsay Y.F., Zhang M.,
RA Coruzzi G., Lacombe B.;
RT "A unified nomenclature of NITRATE TRANSPORTER 1/PEPTIDE TRANSPORTER family
RT members in plants.";
RL Trends Plant Sci. 19:5-9(2014).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN COMPLEX WITH NITRATE, SUBSTRATE,
RP AND MUTAGENESIS OF ARG-45; THR-101; LYS-164 AND HIS-356.
RX PubMed=24572366; DOI=10.1038/nature13116;
RA Parker J.L., Newstead S.;
RT "Molecular basis of nitrate uptake by the plant nitrate transporter
RT NRT1.1.";
RL Nature 507:68-72(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) IN COMPLEX WITH NITRATE, SUBUNIT,
RP AND MUTAGENESIS OF GLU-41; GLU-44; ARG-45; CYS-130; LYS-164; HIS-356 AND
RP GLU-476.
RX PubMed=24572362; DOI=10.1038/nature13074;
RA Sun J., Bankston J.R., Payandeh J., Hinds T.R., Zagotta W.N., Zheng N.;
RT "Crystal structure of the plant dual-affinity nitrate transporter NRT1.1.";
RL Nature 507:73-77(2014).
CC -!- FUNCTION: Dual affinity nitrate transporter. Involved in proton-
CC dependent nitrate uptake and in the regulation of the nitrate
CC transporter NRT2.1. Acts also as a nitrate sensor that trigger a
CC specific signaling pathway stimulating lateral root growth and seed
CC germination. The uptake activity is not required for sensor function.
CC Displays an auxin transport facilitation inhibited by high nitrate
CC concentration. Required to prevent auxin accumulation in preemerged
CC lateral root primordia and young lateral roots when external nitrate
CC concentration is low or null. May be involved in the basipetal
CC transport of auxin out of the lateral root tips. Acts as a
CC bidirectional transporter involved in root-to-shoot nitrate
CC translocation. Recognizes specifically nitrate and chlorate, but not
CC nitrite, alanine, sulfate, phosphate or the di-peptide Ala-Ala.
CC {ECO:0000269|PubMed:10330471, ECO:0000269|PubMed:12509525,
CC ECO:0000269|PubMed:12606566, ECO:0000269|PubMed:15319483,
CC ECO:0000269|PubMed:17148611, ECO:0000269|PubMed:19633234,
CC ECO:0000269|PubMed:19766570, ECO:0000269|PubMed:20627075,
CC ECO:0000269|PubMed:23645597, ECO:0000269|PubMed:8453665,
CC ECO:0000269|PubMed:9844028}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49 uM for nitrate (for the high-affinity phase, in the presence of
CC 250 uM nitrate at pH 5.5) {ECO:0000269|PubMed:10330471};
CC KM=4 mM for nitrate (for the low-affinity phase, in the presence of
CC 10 mM nitrate at pH 5.5) {ECO:0000269|PubMed:10330471};
CC -!- SUBUNIT: Monomer and homodimer. The dimer has the 2 monomers in the
CC same orientation. Interacts with CIPK23. {ECO:0000269|PubMed:19766570,
CC ECO:0000269|PubMed:24572362, ECO:0000269|PubMed:24572366}.
CC -!- INTERACTION:
CC Q05085; Q93VD3: CIPK23; NbExp=3; IntAct=EBI-2463703, EBI-974277;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20627075}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:20627075}.
CC -!- TISSUE SPECIFICITY: Expressed in the stele in lateral root primordia
CC before emergence and in the tip of primary and emerged lateral roots.
CC Detected in emerging and immature leaves, guard cells, flower buds,
CC style, stigma, anthers and pollen grains. Not detected in the shoot
CC apical meristem. {ECO:0000269|PubMed:11487691,
CC ECO:0000269|PubMed:12509525, ECO:0000269|PubMed:17481610,
CC ECO:0000269|PubMed:20627075}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the columella root cap at day 1 after
CC germination. At day 3, detected in the root meristematic region and at
CC day 5, expressed throughout the root tip.
CC {ECO:0000269|PubMed:11487691}.
CC -!- INDUCTION: By nitrate and auxin. {ECO:0000269|PubMed:10330471,
CC ECO:0000269|PubMed:11912226, ECO:0000269|PubMed:12668777,
CC ECO:0000269|PubMed:12805587}.
CC -!- PTM: Acts as a high-affinity nitrate transporter when phosphorylated
CC and as a low-affinity transporter when dephosphorylated. Forms
CC homodimer when unphosphorylated and monomer when phosphorylated. Low
CC nitrogen concentration in the medium stimulates phosphorylation.
CC Phosphorylation also regulates the nitrate signaling.
CC {ECO:0000269|PubMed:12606566, ECO:0000269|PubMed:19766570}.
CC -!- DISRUPTION PHENOTYPE: Altered development of nascent organs. Reduced
CC stomatal opening and reduced transpiration rates in the light resulting
CC in enhanced drought tolerance. Slower translocation of nitrate to the
CC leaves. {ECO:0000269|PubMed:12509525, ECO:0000269|PubMed:15319483,
CC ECO:0000269|PubMed:23645597}.
CC -!- MISCELLANEOUS: When mutated confers resistance to the herbicide
CC chlorate.
CC -!- MISCELLANEOUS: The kinase CIPK23 is a negative regulator of the high-
CC affinity response, while the kinase CIPK8 is a positive regulator of
CC the low-affinity response. Thr-101 is not the direct target of CIPK8.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; L10357; AAA32770.1; -; mRNA.
DR EMBL; AC002131; AAC17604.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28838.1; -; Genomic_DNA.
DR EMBL; BT002016; AAN72027.1; -; mRNA.
DR EMBL; BT008783; AAP68222.1; -; mRNA.
DR EMBL; AK317498; BAH20163.1; -; mRNA.
DR PIR; A45772; A45772.
DR RefSeq; NP_563899.1; NM_101083.4.
DR PDB; 4OH3; X-ray; 3.25 A; A/B=1-590.
DR PDB; 5A2N; X-ray; 3.70 A; A/B=1-590.
DR PDB; 5A2O; X-ray; 3.71 A; A/B=1-590.
DR PDBsum; 4OH3; -.
DR PDBsum; 5A2N; -.
DR PDBsum; 5A2O; -.
DR AlphaFoldDB; Q05085; -.
DR SMR; Q05085; -.
DR BioGRID; 23003; 21.
DR IntAct; Q05085; 20.
DR STRING; 3702.AT1G12110.1; -.
DR TCDB; 2.A.17.3.1; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q05085; -.
DR PaxDb; Q05085; -.
DR PRIDE; Q05085; -.
DR ProteomicsDB; 226104; -.
DR EnsemblPlants; AT1G12110.1; AT1G12110.1; AT1G12110.
DR GeneID; 837763; -.
DR Gramene; AT1G12110.1; AT1G12110.1; AT1G12110.
DR KEGG; ath:AT1G12110; -.
DR Araport; AT1G12110; -.
DR TAIR; locus:2008855; AT1G12110.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_1_1; -.
DR InParanoid; Q05085; -.
DR OMA; RMGRFWT; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q05085; -.
DR BRENDA; 7.3.2.4; 399.
DR PRO; PR:Q05085; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q05085; baseline and differential.
DR Genevisible; Q05085; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010540; P:basipetal auxin transport; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0015706; P:nitrate transmembrane transport; IMP:TAIR.
DR GO; GO:0006857; P:oligopeptide transport; IEA:InterPro.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0010167; P:response to nitrate; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Herbicide resistance; Membrane;
KW Nitrate assimilation; Phosphoprotein; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..590
FT /note="Protein NRT1/ PTR FAMILY 6.3"
FT /id="PRO_0000064316"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 356
FT /ligand="substrate"
FT BINDING 360
FT /ligand="substrate"
FT MOD_RES 101
FT /note="Phosphothreonine; by CIPK23"
FT /evidence="ECO:0000269|PubMed:12606566"
FT MUTAGEN 28
FT /note="T->A: No effect on phosphorylation and on nitrate
FT transport."
FT /evidence="ECO:0000269|PubMed:12606566"
FT MUTAGEN 41
FT /note="E->A: Loss of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362"
FT MUTAGEN 44
FT /note="E->A: Loss of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362"
FT MUTAGEN 45
FT /note="R->A: Loss of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362,
FT ECO:0000269|PubMed:24572366"
FT MUTAGEN 101
FT /note="T->A: Loss of phosphorylation and 91% reduction of
FT high-affinity nitrate transport, but no effect on the
FT nitrate binding."
FT /evidence="ECO:0000269|PubMed:12606566,
FT ECO:0000269|PubMed:24572366"
FT MUTAGEN 101
FT /note="T->D: Loss of low-affinity nitrate transport."
FT /evidence="ECO:0000269|PubMed:12606566,
FT ECO:0000269|PubMed:24572366"
FT MUTAGEN 130
FT /note="C->A: 90% reduction of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362"
FT MUTAGEN 164
FT /note="K->A: 90% reduction of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362,
FT ECO:0000269|PubMed:24572366"
FT MUTAGEN 356
FT /note="H->A: Loss of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362,
FT ECO:0000269|PubMed:24572366"
FT MUTAGEN 476
FT /note="E->A: 80% reduction of the transporter activity."
FT /evidence="ECO:0000269|PubMed:24572362"
FT MUTAGEN 492
FT /note="P->L: In chl1-9; loss of high- and low-affinity
FT nitrate transport, but no effect on nitrate sensing."
FT /evidence="ECO:0000269|PubMed:19766570"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4OH3"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 67..94
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 98..121
FT /evidence="ECO:0007829|PDB:4OH3"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 143..171
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 185..204
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 217..236
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:4OH3"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:4OH3"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:4OH3"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 419..448
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 466..490
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 497..525
FT /evidence="ECO:0007829|PDB:4OH3"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:4OH3"
FT HELIX 542..569
FT /evidence="ECO:0007829|PDB:4OH3"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:4OH3"
SQ SEQUENCE 590 AA; 64922 MW; 78D3E660AAF90D47 CRC64;
MSLPETKSDD ILLDAWDFQG RPADRSKTGG WASAAMILCI EAVERLTTLG IGVNLVTYLT
GTMHLGNATA ANTVTNFLGT SFMLCLLGGF IADTFLGRYL TIAIFAAIQA TGVSILTLST
IIPGLRPPRC NPTTSSHCEQ ASGIQLTVLY LALYLTALGT GGVKASVSGF GSDQFDETEP
KERSKMTYFF NRFFFCINVG SLLAVTVLVY VQDDVGRKWG YGICAFAIVL ALSVFLAGTN
RYRFKKLIGS PMTQVAAVIV AAWRNRKLEL PADPSYLYDV DDIIAAEGSM KGKQKLPHTE
QFRSLDKAAI RDQEAGVTSN VFNKWTLSTL TDVEEVKQIV RMLPIWATCI LFWTVHAQLT
TLSVAQSETL DRSIGSFEIP PASMAVFYVG GLLLTTAVYD RVAIRLCKKL FNYPHGLRPL
QRIGLGLFFG SMAMAVAALV ELKRLRTAHA HGPTVKTLPL GFYLLIPQYL IVGIGEALIY
TGQLDFFLRE CPKGMKGMST GLLLSTLALG FFFSSVLVTI VEKFTGKAHP WIADDLNKGR
LYNFYWLVAV LVALNFLIFL VFSKWYVYKE KRLAEVGIEL DDEPSIPMGH
