DTX51_ARATH
ID DTX51_ARATH Reviewed; 532 AA.
AC Q9SZE2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein DETOXIFICATION 51 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX51 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 51 {ECO:0000305};
DE Short=MATE protein 51 {ECO:0000305};
DE AltName: Full=Protein ABNORMAL SHOOT 3 {ECO:0000303|PubMed:26160579};
DE AltName: Full=Protein ACTIVATED DISEASE SUSCEPTIBILITY 1 {ECO:0000303|PubMed:21762165};
DE Short=Protein ADS1 {ECO:0000303|PubMed:21762165};
DE AltName: Full=Protein ALTERED DEVELOPMENT PROGRAM 1 {ECO:0000303|PubMed:24391508};
DE Short=Protein ADP1 {ECO:0000303|PubMed:24391508};
DE AltName: Full=Protein NOVEL ION CARRIER 4 {ECO:0000303|Ref.1};
DE Short=Protein NIC4 {ECO:0000303|Ref.1};
GN Name=DTX51 {ECO:0000303|PubMed:11739388};
GN Synonyms=ABS3 {ECO:0000303|PubMed:26160579},
GN ADP1 {ECO:0000303|PubMed:24391508}, ADS1 {ECO:0000303|PubMed:21762165},
GN NIC4 {ECO:0000312|EMBL:AAM03452.1};
GN OrderedLocusNames=At4g29140 {ECO:0000312|Araport:AT4G29140};
GN ORFNames=F19B15.170 {ECO:0000312|EMBL:CAB43928.1};
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].
RA Pellengahr K., Poree F., Dolniak B., Kursawe M., Mueller-Roeber B.;
RT "Four membrane transport proteins of the Arabidopsis MATE-family influence
RT the Na(+) and Li(+) tolerance in yeast.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21762165; DOI=10.1111/j.1469-8137.2011.03820.x;
RA Sun X., Gilroy E.M., Chini A., Nurmberg P.L., Hein I., Lacomme C.,
RA Birch P.R., Hussain A., Yun B.W., Loake G.J.;
RT "ADS1 encodes a MATE-transporter that negatively regulates plant disease
RT resistance.";
RL New Phytol. 192:471-482(2011).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=24391508; DOI=10.1371/journal.pgen.1003954;
RA Li R., Li J., Li S., Qin G., Novak O., Pencik A., Ljung K., Aoyama T.,
RA Liu J., Murphy A., Gu H., Tsuge T., Qu L.J.;
RT "ADP1 affects plant architecture by regulating local auxin biosynthesis.";
RL PLoS Genet. 10:E1003954-E1003954(2014).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26160579; DOI=10.1093/jxb/erv344;
RA Wang R., Liu X., Liang S., Ge Q., Li Y., Shao J., Qi Y., An L., Yu F.;
RT "A subgroup of MATE transporter genes regulates hypocotyl cell elongation
RT in Arabidopsis.";
RL J. Exp. Bot. 66:6327-6343(2015).
CC -!- FUNCTION: Functions as a multidrug and toxin extrusion transporter that
CC negatively regulates plant disease resistance (PubMed:21762165). Plays
CC an important role in maintaining normal plant architecture, possibly by
CC regulating local auxin biosynthesis (PubMed:24391508). May act as a
CC negative regulator of hypocotyl cell elongation in the light
CC (PubMed:26160579). {ECO:0000269|PubMed:21762165,
CC ECO:0000269|PubMed:24391508, ECO:0000269|PubMed:26160579}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:24391508};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24391508}. Late
CC endosome membrane {ECO:0000269|PubMed:26160579}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:26160579}.
CC -!- TISSUE SPECIFICITY: Expressed in the meristematic regions. Mainly
CC detected in tissues where cells were actively dividing, such as leaf
CC primordia and young leaves, the junction between lateral root and the
CC primary root, root cap, hydathodes, the junction between secondary
CC inflorescence and the main inflorescence, young stamen and young
CC siliques (PubMed:24391508). Highly expressed at the junction between
CC the hypocotyl and the root, and at the marginal areas of cotyledons and
CC true leaves, coinciding with the locations of the hydathode. Also
CC highly expressed at the basal regions of the newly emerged lateral
CC roots. In the floral organs, mostly expressed at the style of the
CC pistil (PubMed:26160579). {ECO:0000269|PubMed:24391508,
CC ECO:0000269|PubMed:26160579}.
CC -!- DISRUPTION PHENOTYPE: Enhanced resistance to bacterial pathogen
CC PstDC3000 in RNAi mutant. {ECO:0000269|PubMed:21762165}.
CC -!- MISCELLANEOUS: Overexpression of DTX51 alters shoot developmental
CC programs leading to a loss of apical dominance phenotype.
CC {ECO:0000269|PubMed:26160579}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AY082797; AAM03452.1; -; mRNA.
DR EMBL; AL078470; CAB43928.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79672.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85591.1; -; Genomic_DNA.
DR PIR; T08969; T08969.
DR RefSeq; NP_194643.1; NM_119058.3.
DR AlphaFoldDB; Q9SZE2; -.
DR SMR; Q9SZE2; -.
DR IntAct; Q9SZE2; 15.
DR STRING; 3702.AT4G29140.1; -.
DR TCDB; 2.A.66.1.59; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q9SZE2; -.
DR PRIDE; Q9SZE2; -.
DR ProteomicsDB; 221885; -.
DR EnsemblPlants; AT4G29140.1; AT4G29140.1; AT4G29140.
DR GeneID; 829035; -.
DR Gramene; AT4G29140.1; AT4G29140.1; AT4G29140.
DR KEGG; ath:AT4G29140; -.
DR Araport; AT4G29140; -.
DR TAIR; locus:2119941; AT4G29140.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9SZE2; -.
DR OMA; DVKFCLY; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9SZE2; -.
DR PRO; PR:Q9SZE2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZE2; baseline and differential.
DR Genevisible; Q9SZE2; AT.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0046620; P:regulation of organ growth; IMP:UniProtKB.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd13132; MATE_eukaryotic; 1.
DR InterPro; IPR045069; MATE_euk.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 2: Evidence at transcript level;
KW Endosome; Membrane; Plant defense; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..532
FT /note="Protein DETOXIFICATION 51"
FT /id="PRO_0000434085"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 57054 MW; A7872058D2990E2F CRC64;
MCNPSTTTTT TGSENQESRT GLFLDLFSIN SFEPTKRNLR HCENRGSPLM AEAVTEAKSL
FTLAFPIAVT ALVLYLRSAV SMFFLGQLGD LELAAGSLAI AFANITGYSV LSGLALGMEP
LCSQAFGAHR FKLLSLTLHR TVVFLLVCCV PISVLWFNVG KISVYLHQDP DIAKLAQTYL
IFSLPDLLTN TLLHPIRIYL RAQGIIHPVT LASLSGAVFH LPANLFLVSY LRLGLTGVAV
ASSITNIFVV AFLVCYVWAS GLHAPTWTDP TRDCFRGWAP LLRLAGPSCV SVCLEWWWYE
IMIVLCGLLV NPRSTVAAMG VLIQTTSFLY VFPSSLSFAV STRVGNELGA NRPKTAKLTA
TVAIVFAAVT GIIAAAFAYS VRNAWGRIFT GDKEILQLTA AALPILGLCE IGNCPQTVGC
GVVRGTARPS TAANVNLGAF YLVGMPVAVG LGFWAGIGFN GLWVGLLAAQ ISCAGLMMYV
VGTTDWESEA KKAQTLTCAE TVENDIIKAV VASTIDGECD EAEPLIRITV LY
