PTR44_ARATH
ID PTR44_ARATH Reviewed; 636 AA.
AC Q944G5; Q94K82; Q9SU59;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein NRT1/ PTR FAMILY 2.10;
DE Short=AtNPF2.10;
DE AltName: Full=Protein GLUCOSINOLATE TRANSPORTER-1;
GN Name=NPF2.10; Synonyms=GTR1; OrderedLocusNames=At3g47960;
GN ORFNames=T17F15.170;
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] OF 2-636.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
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 [7]
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 [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=22864417; DOI=10.1038/nature11285;
RA Nour-Eldin H.H., Andersen T.G., Burow M., Madsen S.R., Jorgensen M.E.,
RA Olsen C.E., Dreyer I., Hedrich R., Geiger D., Halkier B.A.;
RT "NRT/PTR transporters are essential for translocation of glucosinolate
RT defence compounds to seeds.";
RL Nature 488:531-534(2012).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23995084; DOI=10.1105/tpc.113.110890;
RA Andersen T.G., Nour-Eldin H.H., Fuller V.L., Olsen C.E., Burow M.,
RA Halkier B.A.;
RT "Integration of biosynthesis and long-distance transport establish organ-
RT specific glucosinolate profiles in vegetative Arabidopsis.";
RL Plant Cell 25:3133-3145(2013).
RN [10]
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: High-affinity, proton-dependent glucosinolate-specific
CC transporter. Involved in the distribution of glucosinolates within the
CC leaf, including import into the glucosinolate-rich S-cells located
CC adjacent to the phloem. Involved in bidirectional long-distance
CC transport of aliphatic but not indole glucosinolates. May be involved
CC in removal of glucosinolates from the xylem in roots.
CC {ECO:0000269|PubMed:22864417, ECO:0000269|PubMed:23995084}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for 4-methylthiobutyl glucosinolate
CC {ECO:0000269|PubMed:22864417};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15308754,
CC ECO:0000269|PubMed:22864417}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15308754, ECO:0000269|PubMed:22864417}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, siliques, roots,
CC shoots and leaves. Expressed in veins and in adjacent mesophyll cells
CC in leaves, and in the root vasculature with highest expression in
CC lateral branching points. {ECO:0000269|PubMed:17481610,
CC ECO:0000269|PubMed:22864417, ECO:0000269|PubMed:23995084}.
CC -!- INDUCTION: Up-regulated by wounding. {ECO:0000269|PubMed:22864417}.
CC -!- DISRUPTION PHENOTYPE: No effect on the total glucosinolate levels in
CC seeds. Gtr1 and gtr2 double mutant has no detectable glucosinolate in
CC seeds. {ECO:0000269|PubMed:22864417}.
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=AAK44017.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL16236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL049658; CAB41143.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78351.1; -; Genomic_DNA.
DR EMBL; AF370202; AAK44017.1; ALT_INIT; mRNA.
DR EMBL; AF428467; AAL16236.1; ALT_INIT; mRNA.
DR PIR; T06687; T06687.
DR RefSeq; NP_566896.2; NM_114665.4.
DR AlphaFoldDB; Q944G5; -.
DR SMR; Q944G5; -.
DR BioGRID; 9271; 9.
DR IntAct; Q944G5; 9.
DR STRING; 3702.AT3G47960.1; -.
DR TCDB; 2.A.17.3.17; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q944G5; -.
DR PaxDb; Q944G5; -.
DR PRIDE; Q944G5; -.
DR ProteomicsDB; 226240; -.
DR EnsemblPlants; AT3G47960.1; AT3G47960.1; AT3G47960.
DR GeneID; 823951; -.
DR Gramene; AT3G47960.1; AT3G47960.1; AT3G47960.
DR KEGG; ath:AT3G47960; -.
DR Araport; AT3G47960; -.
DR TAIR; locus:2097910; AT3G47960.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_2_1; -.
DR InParanoid; Q944G5; -.
DR OMA; KHITATT; -.
DR OrthoDB; 365203at2759; -.
DR PRO; PR:Q944G5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q944G5; baseline and differential.
DR Genevisible; Q944G5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0090448; F:glucosinolate:proton symporter activity; IDA:TAIR.
DR GO; GO:1901349; P:glucosinolate transport; IDA:TAIR.
DR GO; GO:0090449; P:phloem glucosinolate loading; 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 Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..636
FT /note="Protein NRT1/ PTR FAMILY 2.10"
FT /id="PRO_0000399978"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT CONFLICT 92
FT /note="Y -> C (in Ref. 3; AAL16236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 71040 MW; 6C5E5410ED6CFBF1 CRC64;
MKSRVILNHR DRRDKNHNNN NTNHYTQVDT MERKPLEVEP STTTTNTDVV DSFEEEQRKI
VYRGWKVMPF IIGNETFEKL GIIGTLSNLL VYLTSVFNLK SYTAATIINA FSGTINFGTF
IAAFLCDTYF GRYKTLSVAV IACFLGSFVI LLTAAIPSLH PVACGNKISC EGPSVGQILF
LLMGLGFLVV GAGGIRPCNL AFGADQFNPK SESGKKGINS FFNWYFFTFT FAQIISLTAV
VYIQSNVSWT IGLIIPVALM FLACVIFFAG DRLYVKVKAS GSPLAGIARV IAAAIKKRGL
KPVKQPWVNL YNHIPSNYAN TTLKYTDQFR FLDKAAIMTP EEKLNSDGTA SDPWKLCTLQ
QVEEVKCIVR VIPIWFASTI YYLAITIQMT YPVFQALQSD RRLGSGGFRI PAATYVVFLM
TGMTVFIIFY DRVLVPSLRR VTGLETGISL LQRIGAGFTF AIMSLLVSGF IEERRRNFAL
TKPTLGMAPR TGEISSMSAL WLIPQLTLAG IAEAFAAIGQ MEFYYKQFPE NMKSFAGSIF
YVGAGVSSYL ASFLISTVHR TTAHSPSGNW LAEDLNKAKL DYFYFMLTGL MVVNMAYFLL
MARWYRYKGG NDEDITEIET NEEETKQQQL QDKNSV
