PTR19_ARATH
ID PTR19_ARATH Reviewed; 585 AA.
AC Q8H157; O81393; Q8W4N9; Q9CAR8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Protein NRT1/ PTR FAMILY 4.6;
DE Short=AtNPF4.6;
DE AltName: Full=Nitrate transporter 1.2;
DE AltName: Full=Nitrate transporter NTL1;
DE AltName: Full=Protein ABA-IMPORTING TRANSPORTER 1;
GN Name=NPF4.6; Synonyms=AIT1, NRT1.2, NTL1, NTR1:2;
GN OrderedLocusNames=At1g69850; ORFNames=T17F3.12;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION BY NITRATE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10449574; DOI=10.2307/3870969;
RA Huang N.C., Liu K.H., Lo H.J., Tsay Y.F.;
RT "Cloning and functional characterization of an Arabidopsis nitrate
RT transporter gene that encodes a constitutive component of low-affinity
RT uptake.";
RL Plant Cell 11:1381-1392(1999).
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 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 [6]
RP INDUCTION BY NEMATODES.
RX PubMed=16478044; DOI=10.1094/mpmi-18-1247;
RA Hammes U.Z., Schachtman D.P., Berg R.H., Nielsen E., Koch W.,
RA McIntyre L.M., Taylor C.G.;
RT "Nematode-induced changes of transporter gene expression in Arabidopsis
RT roots.";
RL Mol. Plant Microbe Interact. 18:1247-1257(2005).
RN [7]
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 [8]
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 [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22645333; DOI=10.1073/pnas.1203567109;
RA Kanno Y., Hanada A., Chiba Y., Ichikawa T., Nakazawa M., Matsui M.,
RA Koshiba T., Kamiya Y., Seo M.;
RT "Identification of an abscisic acid transporter by functional screening
RT using the receptor complex as a sensor.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9653-9658(2012).
RN [10]
RP FUNCTION.
RX PubMed=24084651; DOI=10.4161/psb.26624;
RA Kanno Y., Kamiya Y., Seo M.;
RT "Nitrate does not compete with abscisic acid as a substrate of
RT AtNPF4.6/NRT1.2/AIT1 in Arabidopsis.";
RL Plant Signal. Behav. 8:0-0(2013).
RN [11]
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: Low-affinity proton-dependent nitrate transporter. Involved
CC in constitutive nitrate uptake. Not involved in histidine or dipeptides
CC transport. Involved in (+)-abscisic acid (ABA) transport, but not in
CC gibberellin, indole-3-acetic acid or jasmonic acid import. Mediates
CC cellular ABA uptake. Nitrate does not compete with abscisic acid as a
CC substrate of NPF4.6 (PubMed:24084651). {ECO:0000269|PubMed:10449574,
CC ECO:0000269|PubMed:22645333, ECO:0000269|PubMed:24084651}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 mM for nitrate {ECO:0000269|PubMed:10449574,
CC ECO:0000269|PubMed:22645333};
CC KM=5 uM for (+)-abscisic acid (in insect cells)
CC {ECO:0000269|PubMed:10449574, ECO:0000269|PubMed:22645333};
CC -!- INTERACTION:
CC Q8H157; Q9FJ50: PYL11; NbExp=3; IntAct=EBI-4433263, EBI-2363233;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22645333};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22645333}.
CC -!- TISSUE SPECIFICITY: Expressed in root hairs and in epidermis of both
CC root tips and mature regions of roots. Detected in shoots, stems,
CC flowers, siliques and imbibed seeds. Expressed in vascular tissues in
CC cotyledons, trus leaves, hypocotyls, roots and inflorescence stems.
CC {ECO:0000269|PubMed:10449574, ECO:0000269|PubMed:17481610,
CC ECO:0000269|PubMed:22645333}.
CC -!- INDUCTION: Not regulated by nitrate. Down-regulated upon nematode
CC infection. {ECO:0000269|PubMed:10449574, ECO:0000269|PubMed:12668777,
CC ECO:0000269|PubMed:16478044}.
CC -!- DISRUPTION PHENOTYPE: Reduced effect of ABA on seed germination and
CC postgermination growth and increased number of open stomata.
CC {ECO:0000269|PubMed:22645333}.
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=AAG52554.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF073361; AAC28086.1; -; mRNA.
DR EMBL; AC010675; AAG52554.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34991.1; -; Genomic_DNA.
DR EMBL; BT000720; AAN31862.1; -; mRNA.
DR EMBL; AY062453; AAL32531.1; -; mRNA.
DR EMBL; BT002561; AAO00921.1; -; mRNA.
DR PIR; T51361; T51361.
DR RefSeq; NP_564978.1; NM_105653.5.
DR AlphaFoldDB; Q8H157; -.
DR SMR; Q8H157; -.
DR BioGRID; 28542; 22.
DR IntAct; Q8H157; 22.
DR STRING; 3702.AT1G69850.1; -.
DR TCDB; 2.A.17.3.16; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; Q8H157; -.
DR PRIDE; Q8H157; -.
DR ProteomicsDB; 226427; -.
DR EnsemblPlants; AT1G69850.1; AT1G69850.1; AT1G69850.
DR GeneID; 843321; -.
DR Gramene; AT1G69850.1; AT1G69850.1; AT1G69850.
DR KEGG; ath:AT1G69850; -.
DR Araport; AT1G69850; -.
DR TAIR; locus:2196739; AT1G69850.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_0_1; -.
DR InParanoid; Q8H157; -.
DR OMA; CGALSCT; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q8H157; -.
DR SABIO-RK; Q8H157; -.
DR PRO; PR:Q8H157; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H157; baseline and differential.
DR Genevisible; Q8H157; 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:0090440; F:abscisic acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0080168; P:abscisic acid transport; IDA:TAIR.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP: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 Cell membrane; Membrane; Nitrate assimilation; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..585
FT /note="Protein NRT1/ PTR FAMILY 4.6"
FT /id="PRO_0000399953"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 29
FT /note="M -> V (in Ref. 4; AAL32531/AAO00921)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="F -> L (in Ref. 1; AAC28086)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="A -> G (in Ref. 1; AAC28086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 63982 MW; 8AC024843574D3CC CRC64;
MEVEEEVSRW EGYADWRNRA AVKGRHGGML AASFVLVVEI LENLAYLANA SNLVLYLREY
MHMSPSKSAN DVTNFMGTAF LLALLGGFLS DAFFSTFQIF LISASIEFLG LIILTIQART
PSLMPPSCDS PTCEEVSGSK AAMLFVGLYL VALGVGGIKG SLASHGAEQF DESTPKGRKQ
RSTFFNYFVF CLACGALVAV TFVVWLEDNK GWEWGFGVST IAIFVSILIF LSGSRFYRNK
IPCGSPLTTI LKVLLAASVK CCSSGSSSNA VASMSVSPSN HCVSKGKKEV ESQGELEKPR
QEEALPPRAQ LTNSLKVLNG AADEKPVHRL LECTVQQVED VKIVLKMLPI FACTIMLNCC
LAQLSTFSVQ QAASMNTKIG SLKIPPASLP IFPVVFIMIL APIYDHLIIP FARKATKTET
GVTHLQRIGV GLVLSILAMA VAALVEIKRK GVAKDSGLLD SKETLPVTFL WIALQYLFLG
SADLFTLAGL LEYFFTEAPS SMRSLATSLS WASLAMGYYL SSVIVSIVNS ITGSSGNTPW
LRGKSINRYK LDYFYWLMCV LSAANFLHYL FWAMRYKYRS TGSRS
