ID ENT3_ARATH Reviewed; 418 AA.
AC Q9M0Y3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Equilibrative nucleotide transporter 3 {ECO:0000303|PubMed:12810710};
DE Short=AtENT3 {ECO:0000303|PubMed:12810710};
DE AltName: Full=Nucleoside transporter ENT3 {ECO:0000303|PubMed:12810710};
DE AltName: Full=Protein FLUOROURIDINE RESISTANT 1 {ECO:0000303|PubMed:17253988};
GN Name=ENT3 {ECO:0000303|PubMed:12810710};
GN Synonyms=FUR1 {ECO:0000303|PubMed:17253988};
GN OrderedLocusNames=At4g05120 {ECO:0000312|Araport:AT4G05120};
GN ORFNames=C17L7.40, T32N4 {ECO:0000312|EMBL:AF162444};
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12810710; DOI=10.1074/jbc.m304768200;
RA Li G., Liu K., Baldwin S.A., Wang D.;
RT "Equilibrative nucleoside transporters of Arabidopsis thaliana. cDNA
RT cloning, expression pattern, and analysis of transport activities.";
RL J. Biol. Chem. 278:35732-35742(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15228386; DOI=10.1042/bj20040389;
RA Wormit A., Traub M., Floerchinger M., Neuhaus H.E., Moehlmann T.;
RT "Characterization of three novel members of the Arabidopsis thaliana
RT equilibrative nucleoside transporter (ENT) family.";
RL Biochem. J. 383:19-26(2004).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLY-281.
RX PubMed=17253988; DOI=10.1111/j.1365-313x.2006.02998.x;
RA Traub M., Floerchinger M., Piecuch J., Kunz H.H., Weise-Steinmetz A.,
RA Deitmer J.W., Ekkehard Neuhaus H., Moehlmann T.;
RT "The fluorouridine insensitive 1 (fur1) mutant is defective in
RT equilibrative nucleoside transporter 3 (ENT3), and thus represents an
RT important pyrimidine nucleoside uptake system in Arabidopsis thaliana.";
RL Plant J. 49:855-864(2007).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22372734; DOI=10.1111/j.1438-8677.2012.00562.x;
RA Cornelius S., Traub M., Bernard C., Salzig C., Lang P., Moehlmann T.;
RT "Nucleoside transport across the plasma membrane mediated by equilibrative
RT nucleoside transporter 3 influences metabolism of Arabidopsis seedlings.";
RL Plant Biol. 14:696-705(2012).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26779190; DOI=10.3389/fpls.2015.01158;
RA Daumann M., Fischer M., Niopek-Witz S., Girke C., Moehlmann T.;
RT "Apoplastic nucleoside accumulation in Arabidopsis leads to reduced
RT photosynthetic performance and increased susceptibility against Botrytis
RT cinerea.";
RL Front. Plant Sci. 6:1158-1158(2015).
CC -!- FUNCTION: Nucleoside transporter that functions as a pyrimidine
CC nucleoside carrier in all organs. Has high affinity for adenosine and
CC uridine when expressed in a heterologous system (yeast). Mediates
CC proton-dependent adenosine or uridine transport in Xenopus oocytes.
CC {ECO:0000269|PubMed:12810710, ECO:0000269|PubMed:15228386,
CC ECO:0000269|PubMed:17253988, ECO:0000269|PubMed:22372734}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 uM for adenosine {ECO:0000269|PubMed:12810710,
CC ECO:0000269|PubMed:15228386, ECO:0000269|PubMed:17253988};
CC KM=3.2 uM for uridine {ECO:0000269|PubMed:12810710,
CC ECO:0000269|PubMed:15228386, ECO:0000269|PubMed:17253988};
CC KM=18 uM for guanosine {ECO:0000269|PubMed:12810710,
CC ECO:0000269|PubMed:15228386, ECO:0000269|PubMed:17253988};
CC KM=10.8 uM for cytidine {ECO:0000269|PubMed:12810710,
CC ECO:0000269|PubMed:15228386, ECO:0000269|PubMed:17253988};
CC Vmax=270 pmol/min/mg enzyme toward adenosine
CC {ECO:0000269|PubMed:12810710, ECO:0000269|PubMed:15228386,
CC ECO:0000269|PubMed:17253988};
CC Vmax=233 pmol/min/mg enzyme toward uridine
CC {ECO:0000269|PubMed:12810710, ECO:0000269|PubMed:15228386,
CC ECO:0000269|PubMed:17253988};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12810710};
CC Multi-pass membrane protein {ECO:0000305|PubMed:12810710}. Note=Plasma
CC membrane. {ECO:0000305|PubMed:12810710}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, vasculature of roots and
CC leaves, and meristems of leaf primordia. Expressed in flowers and
CC siliques. {ECO:0000269|PubMed:12810710, ECO:0000269|PubMed:17253988,
CC ECO:0000269|PubMed:22372734}.
CC -!- INDUCTION: By nitrogen deficiency and 5-fluorouracil plus methotrexate.
CC {ECO:0000269|PubMed:12810710}.
CC -!- DISRUPTION PHENOTYPE: The isolated apoplastic sap extracted from the
CC double mutant missing both NSH3 and ENT3 lacks the ability to catalyze
CC the conversion of inosine in hypoxanthine; this double mutant is unable
CC to grow on medium containing inosine as sole nitrogen source, in
CC addition plants are more sensitive to the necrotrophic fungus Botrytis
CC cinerea BMM but are resistant to the cytotoxic adenosine analog 2-
CC chloro-adenosine (CADO) and to 5-fluoro-uridine.
CC {ECO:0000269|PubMed:26779190}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; AF426400; AAL25096.1; -; mRNA.
DR EMBL; AF162444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161502; CAB81054.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82481.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68013.1; -; Genomic_DNA.
DR EMBL; AK175753; BAD43516.1; -; mRNA.
DR PIR; D85064; D85064.
DR RefSeq; NP_001329797.1; NM_001340534.1.
DR RefSeq; NP_192421.1; NM_116751.4.
DR AlphaFoldDB; Q9M0Y3; -.
DR SMR; Q9M0Y3; -.
DR STRING; 3702.Q9M0Y3; -.
DR TCDB; 2.A.57.1.7; the equilibrative nucleoside transporter (ent) family.
DR PaxDb; 3702-AT4G05120-1; -.
DR ProteomicsDB; 222288; -.
DR EnsemblPlants; AT4G05120.1; AT4G05120.1; AT4G05120.
DR EnsemblPlants; AT4G05120.2; AT4G05120.2; AT4G05120.
DR GeneID; 825857; -.
DR Gramene; AT4G05120.1; AT4G05120.1; AT4G05120.
DR Gramene; AT4G05120.2; AT4G05120.2; AT4G05120.
DR KEGG; ath:AT4G05120; -.
DR Araport; AT4G05120; -.
DR TAIR; AT4G05120; FUR1.
DR eggNOG; KOG1479; Eukaryota.
DR HOGENOM; CLU_021611_5_1_1; -.
DR InParanoid; Q9M0Y3; -.
DR OMA; KIMFINS; -.
DR OrthoDB; 239997at2759; -.
DR PhylomeDB; Q9M0Y3; -.
DR PRO; PR:Q9M0Y3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0Y3; baseline and differential.
DR Genevisible; Q9M0Y3; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015858; P:nucleoside transport; IMP:TAIR.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10332; EQUILIBRATIVE NUCLEOSIDE TRANSPORTER; 1.
DR PANTHER; PTHR10332:SF38; EQUILIBRATIVE NUCLEOTIDE TRANSPORTER 3-RELATED; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..418
FT /note="Equilibrative nucleotide transporter 3"
FT /id="PRO_0000419156"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 281
FT /note="G->R: In fur1; confers growth resistance to the
FT toxic compound fluorouridine."
FT /evidence="ECO:0000269|PubMed:17253988"
SQ SEQUENCE 418 AA; 46208 MW; 432E1368C893A836 CRC64;
MADRYENQPP EKLQGKYQAM VVCCILGIGS LVSWNSMLTI ADYYYKVFPD YHPSRVLTLV
YQPFALGTIL ILAYHESKIN TRKRNLIGYI LFTISTFLLI VLDLATKGRG GIGPYIGLCA
VVASFGLADA TVQGGMIGDL SLMCPELVQS FMGGLAVSGA LTSALRLITK AAFEKTNDGP
RKGAMMFLAI STCIELLCVF LYAYVFPKLP IVKYYRRKAA SEGSKTVSAD LAAAGIQNQS
DLTDDDSKNQ RLSNKELLIQ NIDYAVNLFL IYVCTLSIFP GFLYENTGQH GLGDWYALVL
VAMYNCWDLV GRYTPLVKWL KIENRKLITI AVLSRYLLIP AFYFTAKYGD QGWMIMLISV
LGLTNGHLTV CIMTIAPKGY KGPEQNALGN LLVIFLLGGI FAGVALDWLW LIGKKNAF
//
