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Protein

Protein NRT1/ PTR FAMILY 2.10

Gene

NPF2.10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

High-affinity, proton-dependent glucosinolate-specific transporter. Involved in the distribution of glucosinolates within the leaf, including import into the glucosinolate-rich S-cells located adjacent to the phloem. Involved in bidirectional long-distance transport of aliphatic but not indole glucosinolates. May be involved in removal of glucosinolates from the xylem in roots.2 Publications

Kineticsi

  1. KM=20 µM for 4-methylthiobutyl glucosinolate1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiR-ATH-427975. Proton/oligopeptide cotransporters.

    Protein family/group databases

    TCDBi2.A.17.3.17. the proton-dependent oligopeptide transporter (pot/ptr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein NRT1/ PTR FAMILY 2.10
    Short name:
    AtNPF2.10
    Alternative name(s):
    Protein GLUCOSINOLATE TRANSPORTER-1
    Gene namesi
    Name:NPF2.10
    Synonyms:GTR1
    Ordered Locus Names:At3g47960
    ORF Names:T17F15.170
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G47960.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei77 – 9721HelicalSequence analysisAdd
    BLAST
    Transmembranei105 – 12521HelicalSequence analysisAdd
    BLAST
    Transmembranei136 – 15621HelicalSequence analysisAdd
    BLAST
    Transmembranei175 – 19521HelicalSequence analysisAdd
    BLAST
    Transmembranei221 – 24121HelicalSequence analysisAdd
    BLAST
    Transmembranei249 – 26921HelicalSequence analysisAdd
    BLAST
    Transmembranei367 – 38721HelicalSequence analysisAdd
    BLAST
    Transmembranei410 – 43021HelicalSequence analysisAdd
    BLAST
    Transmembranei451 – 47121HelicalSequence analysisAdd
    BLAST
    Transmembranei499 – 51921HelicalSequence analysisAdd
    BLAST
    Transmembranei535 – 55521HelicalSequence analysisAdd
    BLAST
    Transmembranei582 – 60221HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No effect on the total glucosinolate levels in seeds. Gtr1 and gtr2 double mutant has no detectable glucosinolate in seeds.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Protein NRT1/ PTR FAMILY 2.10PRO_0000399978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ944G5.
    PRIDEiQ944G5.

    PTM databases

    iPTMnetiQ944G5.

    Expressioni

    Tissue specificityi

    Expressed in stems, flowers, siliques, roots, shoots and leaves. Expressed in veins and in adjacent mesophyll cells in leaves, and in the root vasculature with highest expression in lateral branching points.3 Publications

    Inductioni

    Up-regulated by wounding.1 Publication

    Gene expression databases

    GenevisibleiQ944G5. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi9271. 9 interactions.
    STRINGi3702.AT3G47960.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ944G5.
    SMRiQ944G5. Positions 64-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 476Poly-Thr

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1237. Eukaryota.
    COG3104. LUCA.
    HOGENOMiHOG000237399.
    InParanoidiQ944G5.
    OMAiWFASTIY.

    Family and domain databases

    InterProiIPR020846. MFS_dom.
    IPR000109. POT_fam.
    [Graphical view]
    PANTHERiPTHR11654. PTHR11654. 1 hit.
    PfamiPF00854. PTR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q944G5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKSRVILNHR DRRDKNHNNN NTNHYTQVDT MERKPLEVEP STTTTNTDVV
    60 70 80 90 100
    DSFEEEQRKI VYRGWKVMPF IIGNETFEKL GIIGTLSNLL VYLTSVFNLK
    110 120 130 140 150
    SYTAATIINA FSGTINFGTF IAAFLCDTYF GRYKTLSVAV IACFLGSFVI
    160 170 180 190 200
    LLTAAIPSLH PVACGNKISC EGPSVGQILF LLMGLGFLVV GAGGIRPCNL
    210 220 230 240 250
    AFGADQFNPK SESGKKGINS FFNWYFFTFT FAQIISLTAV VYIQSNVSWT
    260 270 280 290 300
    IGLIIPVALM FLACVIFFAG DRLYVKVKAS GSPLAGIARV IAAAIKKRGL
    310 320 330 340 350
    KPVKQPWVNL YNHIPSNYAN TTLKYTDQFR FLDKAAIMTP EEKLNSDGTA
    360 370 380 390 400
    SDPWKLCTLQ QVEEVKCIVR VIPIWFASTI YYLAITIQMT YPVFQALQSD
    410 420 430 440 450
    RRLGSGGFRI PAATYVVFLM TGMTVFIIFY DRVLVPSLRR VTGLETGISL
    460 470 480 490 500
    LQRIGAGFTF AIMSLLVSGF IEERRRNFAL TKPTLGMAPR TGEISSMSAL
    510 520 530 540 550
    WLIPQLTLAG IAEAFAAIGQ MEFYYKQFPE NMKSFAGSIF YVGAGVSSYL
    560 570 580 590 600
    ASFLISTVHR TTAHSPSGNW LAEDLNKAKL DYFYFMLTGL MVVNMAYFLL
    610 620 630
    MARWYRYKGG NDEDITEIET NEEETKQQQL QDKNSV
    Length:636
    Mass (Da):71,040
    Last modified:July 27, 2011 - v3
    Checksum:i6C5E5410ED6CFBF1
    GO

    Sequence cautioni

    The sequence AAK44017.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAL16236.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921Y → C in AAL16236 (PubMed:14593172).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL049658 Genomic DNA. Translation: CAB41143.1.
    CP002686 Genomic DNA. Translation: AEE78351.1.
    AF370202 mRNA. Translation: AAK44017.1. Different initiation.
    AF428467 mRNA. Translation: AAL16236.1. Different initiation.
    PIRiT06687.
    RefSeqiNP_566896.2. NM_114665.3.
    UniGeneiAt.20263.
    At.71210.

    Genome annotation databases

    EnsemblPlantsiAT3G47960.1; AT3G47960.1; AT3G47960.
    GeneIDi823951.
    GrameneiAT3G47960.1; AT3G47960.1; AT3G47960.
    KEGGiath:AT3G47960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL049658 Genomic DNA. Translation: CAB41143.1.
    CP002686 Genomic DNA. Translation: AEE78351.1.
    AF370202 mRNA. Translation: AAK44017.1. Different initiation.
    AF428467 mRNA. Translation: AAL16236.1. Different initiation.
    PIRiT06687.
    RefSeqiNP_566896.2. NM_114665.3.
    UniGeneiAt.20263.
    At.71210.

    3D structure databases

    ProteinModelPortaliQ944G5.
    SMRiQ944G5. Positions 64-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi9271. 9 interactions.
    STRINGi3702.AT3G47960.1.

    Protein family/group databases

    TCDBi2.A.17.3.17. the proton-dependent oligopeptide transporter (pot/ptr) family.

    PTM databases

    iPTMnetiQ944G5.

    Proteomic databases

    PaxDbiQ944G5.
    PRIDEiQ944G5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G47960.1; AT3G47960.1; AT3G47960.
    GeneIDi823951.
    GrameneiAT3G47960.1; AT3G47960.1; AT3G47960.
    KEGGiath:AT3G47960.

    Organism-specific databases

    TAIRiAT3G47960.

    Phylogenomic databases

    eggNOGiKOG1237. Eukaryota.
    COG3104. LUCA.
    HOGENOMiHOG000237399.
    InParanoidiQ944G5.
    OMAiWFASTIY.

    Enzyme and pathway databases

    ReactomeiR-ATH-427975. Proton/oligopeptide cotransporters.

    Miscellaneous databases

    PROiQ944G5.

    Gene expression databases

    GenevisibleiQ944G5. AT.

    Family and domain databases

    InterProiIPR020846. MFS_dom.
    IPR000109. POT_fam.
    [Graphical view]
    PANTHERiPTHR11654. PTHR11654. 1 hit.
    PfamiPF00854. PTR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      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] OF 2-636.
      Strain: cv. Columbia.
    4. "Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
      Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
      Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. La-0.
    5. "Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
      Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
      Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "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.
    7. "The Arabidopsis nitrate transporter NRT1.8 functions in nitrate removal from the xylem sap and mediates cadmium tolerance."
      Li J.Y., Fu Y.L., Pike S.M., Bao J., Tian W., Zhang Y., Chen C.Z., Zhang Y., Li H.M., Huang J., Li L.G., Schroeder J.I., Gassmann W., Gong J.M.
      Plant Cell 22:1633-1646(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    8. "NRT/PTR transporters are essential for translocation of glucosinolate defence compounds to seeds."
      Nour-Eldin H.H., Andersen T.G., Burow M., Madsen S.R., Jorgensen M.E., Olsen C.E., Dreyer I., Hedrich R., Geiger D., Halkier B.A.
      Nature 488:531-534(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY WOUNDING.
    9. "Integration of biosynthesis and long-distance transport establish organ-specific glucosinolate profiles in vegetative Arabidopsis."
      Andersen T.G., Nour-Eldin H.H., Fuller V.L., Olsen C.E., Burow M., Halkier B.A.
      Plant Cell 25:3133-3145(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiPTR44_ARATH
    AccessioniPrimary (citable) accession number: Q944G5
    Secondary accession number(s): Q94K82, Q9SU59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2010
    Last sequence update: July 27, 2011
    Last modified: February 17, 2016
    This is version 62 of the entry and version 3 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.