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Protein DETOXIFICATION 43 (AtDTX43) (Multidrug and toxic compound extrusion protein 43) (MATE protein 43) (Protein FERRIC REDUCTASE DEFECTIVE 3) (AtFRD3) (Protein MANGANESE ACCUMULATOR 1)

 DTX43_ARATH             Reviewed;         526 AA.
Q9SFB0;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-JUN-2017, entry version 109.
RecName: Full=Protein DETOXIFICATION 43 {ECO:0000303|PubMed:11739388};
Short=AtDTX43 {ECO:0000303|PubMed:11739388};
AltName: Full=Multidrug and toxic compound extrusion protein 43 {ECO:0000305};
Short=MATE protein 43 {ECO:0000305};
AltName: Full=Protein FERRIC REDUCTASE DEFECTIVE 3 {ECO:0000303|PubMed:12172022};
Short=AtFRD3 {ECO:0000303|PubMed:12172022};
AltName: Full=Protein MANGANESE ACCUMULATOR 1 {ECO:0000303|PubMed:8754685};
Name=DTX43 {ECO:0000303|PubMed:11739388};
Synonyms=FRD3 {ECO:0000303|PubMed:12172022},
MAN1 {ECO:0000303|PubMed:8754685};
OrderedLocusNames=At3g08040 {ECO:0000312|Araport:AT3G08040};
ORFNames=F17A17.38 {ECO:0000312|EMBL:AAF21214.1},
T8G24.8 {ECO:0000312|EMBL:AAG50830.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ALA-54,
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY IRON.
STRAIN=cv. Columbia;
PubMed=12172022; DOI=10.1105/tpc.001495;
Rogers E.E., Guerinot M.L.;
"FRD3, a member of the multidrug and toxin efflux family, controls
iron deficiency responses in Arabidopsis.";
Plant Cell 14:1787-1799(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
MUTANT MAN1, AND DISRUPTION PHENOTYPE.
PubMed=8754685; DOI=10.1104/pp.111.3.849;
Delhaize E.;
"A metal-accumulator mutant of Arabidopsis thaliana.";
Plant Physiol. 111:849-855(1996).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11739388; DOI=10.1074/jbc.M108777200;
Li L., He Z., Pandey G.K., Tsuchiya T., Luan S.;
"Functional cloning and characterization of a plant efflux carrier for
multidrug and heavy metal detoxification.";
J. Biol. Chem. 277:5360-5368(2002).
[7]
GENE FAMILY.
PubMed=12603313; DOI=10.1046/j.1432-1033.2003.03418.x;
Hvorup R.N., Winnen B., Chang A.B., Jiang Y., Zhou X.F.,
Saier M.H. Jr.;
"The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter
superfamily.";
Eur. J. Biochem. 270:799-813(2003).
[8]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15310833; DOI=10.1104/pp.104.045633;
Green L.S., Rogers E.E.;
"FRD3 controls iron localization in Arabidopsis.";
Plant Physiol. 136:2523-2531(2004).
[9]
FUNCTION.
PubMed=17351051; DOI=10.1104/pp.107.097162;
Durrett T.P., Gassmann W., Rogers E.E.;
"The FRD3-mediated efflux of citrate into the root vasculature is
necessary for efficient iron translocation.";
Plant Physiol. 144:197-205(2007).
[10]
FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
PubMed=18826429; DOI=10.1111/j.1365-313X.2008.03696.x;
Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
"Aluminum-activated citrate and malate transporters from the MATE and
ALMT families function independently to confer Arabidopsis aluminum
tolerance.";
Plant J. 57:389-399(2009).
[11]
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=21742986; DOI=10.1105/tpc.111.088088;
Roschzttardtz H., Seguela-Arnaud M., Briat J.F., Vert G., Curie C.;
"The FRD3 citrate effluxer promotes iron nutrition between
symplastically disconnected tissues throughout Arabidopsis
development.";
Plant Cell 23:2725-2737(2011).
[12]
INDUCTION BY ABA.
PubMed=24111973; DOI=10.1111/pce.12203;
Lei G.J., Zhu X.F., Wang Z.W., Dong F., Dong N.Y., Zheng S.J.;
"Abscisic acid alleviates iron deficiency by promoting root iron
reutilization and transport from root to shoot in Arabidopsis.";
Plant Cell Environ. 37:852-863(2014).
-!- FUNCTION: Citrate transporter responsible for loading citrate into
xylem tissues, which helps facilitate iron transport to shoots
(PubMed:12172022, PubMed:15310833, PubMed:17351051,
PubMed:18826429). Mediates the citrate release in the apoplastic
spaces during plant development allowing iron nutrition between
symplastically disconnected tissues (PubMed:21742986).
{ECO:0000269|PubMed:12172022, ECO:0000269|PubMed:15310833,
ECO:0000269|PubMed:17351051, ECO:0000269|PubMed:18826429,
ECO:0000269|PubMed:21742986}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15310833};
Multi-pass membrane protein {ECO:0000269|PubMed:15310833}.
-!- TISSUE SPECIFICITY: Expressed in roots in the pericycle and cells
internal to the pericycle and surrounding the vascular tissue
(PubMed:12172022, PubMed:15310833). Also expressed in seed and
flower (PubMed:21742986). {ECO:0000269|PubMed:12172022,
ECO:0000269|PubMed:15310833, ECO:0000269|PubMed:21742986}.
-!- DEVELOPMENTAL STAGE: Expressed during embryogenesis and during the
early stages of germination. {ECO:0000269|PubMed:21742986}.
-!- INDUCTION: Two-fold induction by iron deficiency. Not induced by
aluminum (PubMed:12172022, PubMed:18826429). Induced by abscisic
acid (ABA) (PubMed:24111973). {ECO:0000269|PubMed:12172022,
ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:24111973}.
-!- DISRUPTION PHENOTYPE: Chlorotic (PubMed:12172022, PubMed:8754685,
PubMed:18826429, PubMed:21742986). Constitutive expression of
strategy I iron deficiency response and accumulation of iron,
manganese and zinc in shoots. No reduction in aluminum tolerance
(PubMed:12172022, PubMed:18826429). Accumulation of Mn, Cu, Zn and
Mg in leaves and accumulation of Fe in roots (PubMed:8754685).
Altered pollen development (PubMed:21742986).
{ECO:0000269|PubMed:12172022, ECO:0000269|PubMed:18826429,
ECO:0000269|PubMed:21742986, ECO:0000269|PubMed:8754685}.
-!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
(TC 2.A.66.1) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF448231; AAL86700.1; -; mRNA.
EMBL; AC013483; AAF21214.1; -; Genomic_DNA.
EMBL; AC074395; AAG50830.1; -; Genomic_DNA.
EMBL; CP002686; AEE74634.1; -; Genomic_DNA.
EMBL; CP002686; AEE74635.1; -; Genomic_DNA.
EMBL; AY056439; AAL08295.1; -; mRNA.
EMBL; AY057517; AAL09757.1; -; mRNA.
EMBL; AY133652; AAM91482.1; -; mRNA.
EMBL; BT006370; AAP21178.1; -; mRNA.
RefSeq; NP_001319499.1; NM_001337758.1.
RefSeq; NP_187461.1; NM_111683.2.
UniGene; At.17333; -.
ProteinModelPortal; Q9SFB0; -.
BioGrid; 5330; 1.
IntAct; Q9SFB0; 1.
STRING; 3702.AT3G08040.1; -.
TCDB; 2.A.66.1.24; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
iPTMnet; Q9SFB0; -.
PaxDb; Q9SFB0; -.
PRIDE; Q9SFB0; -.
EnsemblPlants; AT3G08040.1; AT3G08040.1; AT3G08040.
GeneID; 819995; -.
Gramene; AT3G08040.1; AT3G08040.1; AT3G08040.
KEGG; ath:AT3G08040; -.
Araport; AT3G08040; -.
TAIR; locus:2077477; AT3G08040.
eggNOG; KOG1347; Eukaryota.
eggNOG; COG0534; LUCA.
HOGENOM; HOG000253153; -.
InParanoid; Q9SFB0; -.
OMA; FANQIIF; -.
OrthoDB; EOG09360920; -.
PhylomeDB; Q9SFB0; -.
PRO; PR:Q9SFB0; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9SFB0; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0015297; F:antiporter activity; IEA:InterPro.
GO; GO:0015137; F:citrate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015238; F:drug transmembrane transporter activity; IEA:InterPro.
GO; GO:0046873; F:metal ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0005215; F:transporter activity; ISS:TAIR.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
GO; GO:0071369; P:cellular response to ethylene stimulus; IEP:TAIR.
GO; GO:0071281; P:cellular response to iron ion; IEP:TAIR.
GO; GO:0071732; P:cellular response to nitric oxide; IEP:TAIR.
GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
GO; GO:0030001; P:metal ion transport; IMP:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
InterPro; IPR002528; MATE_fam.
Pfam; PF01554; MatE; 2.
TIGRFAMs; TIGR00797; matE; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Ion channel; Ion transport;
Membrane; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 526 Protein DETOXIFICATION 43.
/FTId=PRO_0000405272.
TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.
TRANSMEM 37 57 Helical. {ECO:0000255}.
TOPO_DOM 58 59 Extracellular. {ECO:0000255}.
TRANSMEM 60 80 Helical. {ECO:0000255}.
TOPO_DOM 81 170 Cytoplasmic. {ECO:0000255}.
TRANSMEM 171 191 Helical. {ECO:0000255}.
TOPO_DOM 192 215 Extracellular. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TOPO_DOM 237 244 Cytoplasmic. {ECO:0000255}.
TRANSMEM 245 267 Helical. {ECO:0000255}.
TOPO_DOM 268 270 Extracellular. {ECO:0000255}.
TRANSMEM 271 293 Helical. {ECO:0000255}.
TOPO_DOM 294 316 Cytoplasmic. {ECO:0000255}.
TRANSMEM 317 337 Helical. {ECO:0000255}.
TOPO_DOM 338 353 Extracellular. {ECO:0000255}.
TRANSMEM 354 374 Helical. {ECO:0000255}.
TOPO_DOM 375 396 Cytoplasmic. {ECO:0000255}.
TRANSMEM 397 417 Helical. {ECO:0000255}.
TOPO_DOM 418 426 Extracellular. {ECO:0000255}.
TRANSMEM 427 447 Helical. {ECO:0000255}.
TOPO_DOM 448 457 Cytoplasmic. {ECO:0000255}.
TRANSMEM 458 478 Helical. {ECO:0000255}.
TOPO_DOM 479 484 Extracellular. {ECO:0000255}.
TRANSMEM 485 505 Helical. {ECO:0000255}.
TOPO_DOM 506 526 Cytoplasmic. {ECO:0000255}.
COMPBIAS 317 320 Poly-Leu.
COMPBIAS 521 526 Poly-Ser.
MUTAGEN 54 54 A->D: In fdr3-1; loss of function.
{ECO:0000269|PubMed:12172022}.
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


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