PTR37_ARATH
ID PTR37_ARATH Reviewed; 558 AA.
AC Q9M1E2; C0Z3K4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein NRT1/ PTR FAMILY 2.7;
DE Short=AtNPF2.7;
DE AltName: Full=Nitrate excretion transporter 1;
GN Name=NPF2.7; Synonyms=NAXT1; OrderedLocusNames=At3g45650;
GN ORFNames=F9K21.230;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
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 [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY LIGHT, MEDIUM ACIDIFICATION AND NITRATE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=17993627; DOI=10.1105/tpc.106.048173;
RA Segonzac C., Boyer J.C., Ipotesi E., Szponarski W., Tillard P.,
RA Touraine B., Sommerer N., Rossignol M., Gibrat R.;
RT "Nitrate efflux at the root plasma membrane: identification of an
RT Arabidopsis excretion transporter.";
RL Plant Cell 19:3760-3777(2007).
RN [6]
RP GENE FAMILY.
RX PubMed=20501909; DOI=10.1105/tpc.110.075242;
RA Li J.Y., Fu Y.L., Pike S.M., Bao J., Tian W., Zhang Y., Chen C.Z.,
RA Zhang Y., Li H.M., Huang J., Li L.G., Schroeder J.I., Gassmann W.,
RA Gong J.M.;
RT "The Arabidopsis nitrate transporter NRT1.8 functions in nitrate removal
RT from the xylem sap and mediates cadmium tolerance.";
RL Plant Cell 22:1633-1646(2010).
RN [7]
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).
CC -!- FUNCTION: Transporter involved in a passive nitrate efflux. Not
CC competent for chloride transport. {ECO:0000269|PubMed:17993627}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:17993627};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17993627};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17993627}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M1E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M1E2-2; Sequence=VSP_039951;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and in the cortex of mature
CC roots. Not expressed in root tip meristematic cells.
CC {ECO:0000269|PubMed:17481610, ECO:0000269|PubMed:17993627}.
CC -!- INDUCTION: Not regulated by light or plant N status. Up-regulated at
CC the protein level but not at the transcript level by medium
CC acidification. {ECO:0000269|PubMed:17993627}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17993627}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH57283.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL138657; CAB75494.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78055.1; -; Genomic_DNA.
DR EMBL; AK319168; BAH57283.1; ALT_FRAME; mRNA.
DR PIR; T47505; T47505.
DR RefSeq; NP_190151.1; NM_114434.2. [Q9M1E2-1]
DR AlphaFoldDB; Q9M1E2; -.
DR SMR; Q9M1E2; -.
DR STRING; 3702.AT3G45650.1; -.
DR TCDB; 2.A.17.3.5; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; Q9M1E2; -.
DR PRIDE; Q9M1E2; -.
DR EnsemblPlants; AT3G45650.1; AT3G45650.1; AT3G45650. [Q9M1E2-1]
DR GeneID; 823707; -.
DR Gramene; AT3G45650.1; AT3G45650.1; AT3G45650. [Q9M1E2-1]
DR KEGG; ath:AT3G45650; -.
DR Araport; AT3G45650; -.
DR TAIR; locus:2085647; AT3G45650.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_2_1; -.
DR InParanoid; Q9M1E2; -.
DR OMA; LAMNRHI; -.
DR PhylomeDB; Q9M1E2; -.
DR BRENDA; 7.3.2.4; 399.
DR PRO; PR:Q9M1E2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1E2; baseline and differential.
DR Genevisible; Q9M1E2; 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:0010542; F:nitrate efflux transmembrane transporter activity; 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:0010447; P:response to acidic pH; IMP:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Nitrate assimilation;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..558
FT /note="Protein NRT1/ PTR FAMILY 2.7"
FT /id="PRO_0000399971"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039951"
SQ SEQUENCE 558 AA; 61099 MW; 465C14979F6E1A85 CRC64;
MASSVTGDAE TAISADSSTK RRGGGWITFP FMIATLLGLT IAAWGWLLNL IVYLIEEFNV
KSIAAAQIAN IVSGCICMVP AVAAIASDSF FGTIPVISVS AFISLMGVAL LTLTASLDTL
RPRPCETASI LCQSPSKTQL GVLYTAITLA SIGTGGTRFT LATAGANQYE KTKDQGSFFN
WFFFTTYLAG AISATAIVYT EDNISWTLGF GLSVAANFFS FLVFVSGKRF YKHDKPLGSP
FTSLLCVIFA ALRKRKAVVS TNEKDYHNES ITMPTKSFRF FNRAALKQED EVKPDGTIRN
PWRLCSVQQV EDFKAVIRII PLALATIFLS TPIAMQLSLT VLQGLVMDRR LGPSFKIPAG
SLQVITLLST CLFIIVNDRV LYPFYQKLTG KHLTPLQRVG IGHAFNILSM AVTAIVEAKR
LKIVQKGHFL GSSSVADMSV LWLFPPLVIV GIGEAFHFPG NVALCYQEFP ESMRSTATSI
TSVVIGICFY TSTALIDLIQ RTTAWLPDDI NHGRVDNVYW ILVIGGVLNL GYFLVCSWLY
RYRNLKDDDH KQAANVSH
