DTX43_ARATH
ID DTX43_ARATH Reviewed; 526 AA.
AC Q9SFB0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Protein DETOXIFICATION 43 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX43 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 43 {ECO:0000305};
DE Short=MATE protein 43 {ECO:0000305};
DE AltName: Full=Protein FERRIC REDUCTASE DEFECTIVE 3 {ECO:0000303|PubMed:12172022};
DE Short=AtFRD3 {ECO:0000303|PubMed:12172022};
DE AltName: Full=Protein MANGANESE ACCUMULATOR 1 {ECO:0000303|PubMed:8754685};
GN Name=DTX43 {ECO:0000303|PubMed:11739388};
GN Synonyms=FRD3 {ECO:0000303|PubMed:12172022},
GN MAN1 {ECO:0000303|PubMed:8754685};
GN OrderedLocusNames=At3g08040 {ECO:0000312|Araport:AT3G08040};
GN ORFNames=F17A17.38 {ECO:0000312|EMBL:AAF21214.1},
GN T8G24.8 {ECO:0000312|EMBL:AAG50830.1};
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, MUTAGENESIS OF ALA-54, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY IRON.
RC STRAIN=cv. Columbia;
RX PubMed=12172022; DOI=10.1105/tpc.001495;
RA Rogers E.E., Guerinot M.L.;
RT "FRD3, a member of the multidrug and toxin efflux family, controls iron
RT deficiency responses in Arabidopsis.";
RL Plant Cell 14:1787-1799(2002).
RN [2]
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 [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 MUTANT MAN1, AND DISRUPTION PHENOTYPE.
RX PubMed=8754685; DOI=10.1104/pp.111.3.849;
RA Delhaize E.;
RT "A metal-accumulator mutant of Arabidopsis thaliana.";
RL Plant Physiol. 111:849-855(1996).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11739388; DOI=10.1074/jbc.m108777200;
RA Li L., He Z., Pandey G.K., Tsuchiya T., Luan S.;
RT "Functional cloning and characterization of a plant efflux carrier for
RT multidrug and heavy metal detoxification.";
RL J. Biol. Chem. 277:5360-5368(2002).
RN [7]
RP GENE FAMILY.
RX PubMed=12603313; DOI=10.1046/j.1432-1033.2003.03418.x;
RA Hvorup R.N., Winnen B., Chang A.B., Jiang Y., Zhou X.F., Saier M.H. Jr.;
RT "The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter
RT superfamily.";
RL Eur. J. Biochem. 270:799-813(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15310833; DOI=10.1104/pp.104.045633;
RA Green L.S., Rogers E.E.;
RT "FRD3 controls iron localization in Arabidopsis.";
RL Plant Physiol. 136:2523-2531(2004).
RN [9]
RP FUNCTION.
RX PubMed=17351051; DOI=10.1104/pp.107.097162;
RA Durrett T.P., Gassmann W., Rogers E.E.;
RT "The FRD3-mediated efflux of citrate into the root vasculature is necessary
RT for efficient iron translocation.";
RL Plant Physiol. 144:197-205(2007).
RN [10]
RP FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
RX PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT families function independently to confer Arabidopsis aluminum tolerance.";
RL Plant J. 57:389-399(2009).
RN [11]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=21742986; DOI=10.1105/tpc.111.088088;
RA Roschzttardtz H., Seguela-Arnaud M., Briat J.F., Vert G., Curie C.;
RT "The FRD3 citrate effluxer promotes iron nutrition between symplastically
RT disconnected tissues throughout Arabidopsis development.";
RL Plant Cell 23:2725-2737(2011).
RN [12]
RP INDUCTION BY ABA.
RX PubMed=24111973; DOI=10.1111/pce.12203;
RA Lei G.J., Zhu X.F., Wang Z.W., Dong F., Dong N.Y., Zheng S.J.;
RT "Abscisic acid alleviates iron deficiency by promoting root iron
RT reutilization and transport from root to shoot in Arabidopsis.";
RL Plant Cell Environ. 37:852-863(2014).
CC -!- FUNCTION: Citrate transporter responsible for loading citrate into
CC xylem tissues, which helps facilitate iron transport to shoots
CC (PubMed:12172022, PubMed:15310833, PubMed:17351051, PubMed:18826429).
CC Mediates the citrate release in the apoplastic spaces during plant
CC development allowing iron nutrition between symplastically disconnected
CC tissues (PubMed:21742986). {ECO:0000269|PubMed:12172022,
CC ECO:0000269|PubMed:15310833, ECO:0000269|PubMed:17351051,
CC ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:21742986}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15310833};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15310833}.
CC -!- TISSUE SPECIFICITY: Expressed in roots in the pericycle and cells
CC internal to the pericycle and surrounding the vascular tissue
CC (PubMed:12172022, PubMed:15310833). Also expressed in seed and flower
CC (PubMed:21742986). {ECO:0000269|PubMed:12172022,
CC ECO:0000269|PubMed:15310833, ECO:0000269|PubMed:21742986}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis and during the
CC early stages of germination. {ECO:0000269|PubMed:21742986}.
CC -!- INDUCTION: Two-fold induction by iron deficiency. Not induced by
CC aluminum (PubMed:12172022, PubMed:18826429). Induced by abscisic acid
CC (ABA) (PubMed:24111973). {ECO:0000269|PubMed:12172022,
CC ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:24111973}.
CC -!- DISRUPTION PHENOTYPE: Chlorotic (PubMed:12172022, PubMed:8754685,
CC PubMed:18826429, PubMed:21742986). Constitutive expression of strategy
CC I iron deficiency response and accumulation of iron, manganese and zinc
CC in shoots. No reduction in aluminum tolerance (PubMed:12172022,
CC PubMed:18826429). Accumulation of Mn, Cu, Zn and Mg in leaves and
CC accumulation of Fe in roots (PubMed:8754685). Altered pollen
CC development (PubMed:21742986). {ECO:0000269|PubMed:12172022,
CC ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:21742986,
CC ECO:0000269|PubMed:8754685}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AF448231; AAL86700.1; -; mRNA.
DR EMBL; AC013483; AAF21214.1; -; Genomic_DNA.
DR EMBL; AC074395; AAG50830.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74634.1; -; Genomic_DNA.
DR EMBL; AY056439; AAL08295.1; -; mRNA.
DR EMBL; AY057517; AAL09757.1; -; mRNA.
DR EMBL; AY133652; AAM91482.1; -; mRNA.
DR EMBL; BT006370; AAP21178.1; -; mRNA.
DR RefSeq; NP_187461.1; NM_111683.2.
DR AlphaFoldDB; Q9SFB0; -.
DR SMR; Q9SFB0; -.
DR BioGRID; 5330; 1.
DR IntAct; Q9SFB0; 1.
DR STRING; 3702.AT3G08040.1; -.
DR TCDB; 2.A.66.1.24; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q9SFB0; -.
DR PaxDb; Q9SFB0; -.
DR PRIDE; Q9SFB0; -.
DR ProteomicsDB; 222227; -.
DR EnsemblPlants; AT3G08040.1; AT3G08040.1; AT3G08040.
DR GeneID; 819995; -.
DR Gramene; AT3G08040.1; AT3G08040.1; AT3G08040.
DR KEGG; ath:AT3G08040; -.
DR Araport; AT3G08040; -.
DR TAIR; locus:2077477; AT3G08040.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_16_2_1; -.
DR InParanoid; Q9SFB0; -.
DR OrthoDB; 665325at2759; -.
DR PhylomeDB; Q9SFB0; -.
DR PRO; PR:Q9SFB0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFB0; baseline and differential.
DR Genevisible; Q9SFB0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0030001; P:metal ion transport; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR CDD; cd13136; MATE_DinF_like; 1.
DR InterPro; IPR044644; DinF-like.
DR InterPro; IPR002528; MATE_fam.
DR PANTHER; PTHR42893; PTHR42893; 1.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..526
FT /note="Protein DETOXIFICATION 43"
FT /id="PRO_0000405272"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 133..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 54
FT /note="A->D: In fdr3-1; loss of function."
FT /evidence="ECO:0000269|PubMed:12172022"
SQ SEQUENCE 526 AA; 55946 MW; 94B1B91625DD762D CRC64;
MTETGDDLAT VKKPIPFLVI FKDLRHVFSR DTTGREILGI AFPAALALAA DPIASLIDTA
FVGRLGAVQL AAVGVSIAIF NQASRITIFP LVSLTTSFVA EEDTMEKMKE EANKANLVHA
ETILVQDSLE KGISSPTSND TNQPQQPPAP DTKSNSGNKS NKKEKRTIRT ASTAMILGLI
LGLVQAIFLI FSSKLLLGVM GVKPNSPMLS PAHKYLSIRA LGAPALLLSL AMQGIFRGFK
DTKTPLFATV VADVINIVLD PIFIFVLRLG IIGAAIAHVI SQYFMTLILF VFLAKKVNLI
PPNFGDLQFG RFLKNGLLLL ARTIAVTFCQ TLAAAMAARL GTTPMAAFQI CLQVWLTSSL
LNDGLAVAGQ AILACSFAEK DYNKVTAVAS RVLQMGFVLG LGLSVFVGLG LYFGAGVFSK
DPAVIHLMAI GIPFIAATQP INSLAFVLDG VNFGASDFAY TAYSMVGVAA ISIAAVIYMA
KTNGFIGIWI ALTIYMALRA ITGIARMATG TGPWRFLRGR SSSSSS
