DTX41_ARATH
ID DTX41_ARATH Reviewed; 507 AA.
AC Q9LYT3;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Protein DETOXIFICATION 41 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX41 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 41 {ECO:0000305};
DE Short=MATE protein 41 {ECO:0000305};
DE AltName: Full=Protein TANNIN-DEFICIENT SEED 3 {ECO:0000303|PubMed:12376625, ECO:0000303|PubMed:24903359};
DE AltName: Full=Protein TRANSPARENT TESTA 12 {ECO:0000303|PubMed:11283341};
GN Name=DTX41 {ECO:0000303|PubMed:11739388};
GN Synonyms=TDS3 {ECO:0000303|PubMed:12376625, ECO:0000303|PubMed:24903359},
GN TT12 {ECO:0000303|PubMed:11283341};
GN OrderedLocusNames=At3g59030 {ECO:0000312|Araport:AT3G59030};
GN ORFNames=F17J16_80 {ECO:0000312|EMBL:CAB86931.1};
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=11283341; DOI=10.2307/3871345;
RA Debeaujon I., Peeters A.J., Leon-Kloosterziel K.M., Koornneef M.;
RT "The TRANSPARENT TESTA12 gene of Arabidopsis encodes a multidrug secondary
RT transporter-like protein required for flavonoid sequestration in vacuoles
RT of the seed coat endothelium.";
RL Plant Cell 13:853-871(2001).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12376625; DOI=10.1104/pp.006189;
RA Abrahams S., Tanner G.J., Larkin P.J., Ashton A.R.;
RT "Identification and biochemical characterization of mutants in the
RT proanthocyanidin pathway in Arabidopsis.";
RL Plant Physiol. 130:561-576(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, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17601828; DOI=10.1105/tpc.106.046029;
RA Marinova K., Pourcel L., Weder B., Schwarz M., Barron D., Routaboul J.M.,
RA Debeaujon I., Klein M.;
RT "The Arabidopsis MATE transporter TT12 acts as a vacuolar flavonoid/H+
RT -antiporter active in proanthocyanidin-accumulating cells of the seed
RT coat.";
RL Plant Cell 19:2023-2038(2007).
RN [9]
RP FUNCTION.
RX PubMed=19684242; DOI=10.1105/tpc.109.067819;
RA Zhao J., Dixon R.A.;
RT "MATE transporters facilitate vacuolar uptake of epicatechin 3'-O-glucoside
RT for proanthocyanidin biosynthesis in Medicago truncatula and Arabidopsis.";
RL Plant Cell 21:2323-2340(2009).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=20180920; DOI=10.1111/j.1365-313x.2010.04174.x;
RA Kitamura S., Matsuda F., Tohge T., Yonekura-Sakakibara K., Yamazaki M.,
RA Saito K., Narumi I.;
RT "Metabolic profiling and cytological analysis of proanthocyanidins in
RT immature seeds of Arabidopsis thaliana flavonoid accumulation mutants.";
RL Plant J. 62:549-559(2010).
RN [11]
RP REVIEW.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [12]
RP INDUCTION.
RX PubMed=24299194; DOI=10.1111/nph.12620;
RA Xu W., Grain D., Bobet S., Le Gourrierec J., Thevenin J., Kelemen Z.,
RA Lepiniec L., Dubos C.;
RT "Complexity and robustness of the flavonoid transcriptional regulatory
RT network revealed by comprehensive analyses of MYB-bHLH-WDR complexes and
RT their targets in Arabidopsis seed.";
RL New Phytol. 202:132-144(2014).
RN [13]
RP ALLELIC MUTANTS TT12 AND TDS3.
RX PubMed=24903359; DOI=10.1007/s00425-014-2088-0;
RA Appelhagen I., Thiedig K., Nordholt N., Schmidt N., Huep G., Sagasser M.,
RA Weisshaar B.;
RT "Update on transparent testa mutants from Arabidopsis thaliana:
RT characterisation of new alleles from an isogenic collection.";
RL Planta 240:955-970(2014).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=25891958; DOI=10.1111/tpj.12854;
RA Appelhagen I., Nordholt N., Seidel T., Spelt K., Koes R., Quattrochio F.,
RA Sagasser M., Weisshaar B.;
RT "TRANSPARENT TESTA 13 is a tonoplast P3A -ATPase required for vacuolar
RT deposition of proanthocyanidins in Arabidopsis thaliana seeds.";
RL Plant J. 82:840-849(2015).
CC -!- FUNCTION: Acts as a flavonoid/H(+)-antiporter that control the vacuolar
CC sequestration of flavonoids in the seed coat endothelium
CC (PubMed:11283341, PubMed:17601828). Could transport the anthocyanin
CC cyanidin-3-O-glucoside (PubMed:17601828) and epicatechin 3'-O-glucoside
CC (PubMed:19684242) in vitro. {ECO:0000269|PubMed:11283341,
CC ECO:0000269|PubMed:17601828, ECO:0000269|PubMed:19684242}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17601828,
CC ECO:0000269|PubMed:25891958}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17601828, ECO:0000269|PubMed:25891958}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in reproductive tissues, from buds to
CC siliques. Restricted to the endothelium layer of the ovule and the seed
CC coat. {ECO:0000269|PubMed:11283341, ECO:0000269|PubMed:17601828}.
CC -!- DEVELOPMENTAL STAGE: Expressed with a peak at the early globular stage
CC and until the late heart-torpedo stage of embryo development.
CC {ECO:0000269|PubMed:11283341}.
CC -!- INDUCTION: Positively regulated by the TT2-TT8-TTG1 complex.
CC {ECO:0000269|PubMed:24299194}.
CC -!- DISRUPTION PHENOTYPE: Pale brown seeds due to a strong reduction of
CC proanthocyanidin deposition in vacuoles of endothelial cells.
CC {ECO:0000269|PubMed:11283341, ECO:0000269|PubMed:12376625,
CC ECO:0000269|PubMed:17601828, ECO:0000269|PubMed:20180920}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AJ294464; CAC36941.1; -; mRNA.
DR EMBL; AL163527; CAB86931.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79863.1; -; Genomic_DNA.
DR EMBL; AY088768; AAM67348.1; -; mRNA.
DR PIR; T47785; T47785.
DR RefSeq; NP_191462.1; NM_115765.4.
DR AlphaFoldDB; Q9LYT3; -.
DR SMR; Q9LYT3; -.
DR BioGRID; 10387; 11.
DR IntAct; Q9LYT3; 10.
DR STRING; 3702.AT3G59030.1; -.
DR TCDB; 2.A.66.1.57; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q9LYT3; -.
DR PaxDb; Q9LYT3; -.
DR ProteomicsDB; 221881; -.
DR EnsemblPlants; AT3G59030.1; AT3G59030.1; AT3G59030.
DR GeneID; 825072; -.
DR Gramene; AT3G59030.1; AT3G59030.1; AT3G59030.
DR KEGG; ath:AT3G59030; -.
DR Araport; AT3G59030; -.
DR TAIR; locus:2077725; AT3G59030.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR InParanoid; Q9LYT3; -.
DR OMA; IAHACDE; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9LYT3; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q9LYT3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYT3; baseline and differential.
DR Genevisible; Q9LYT3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015299; F:solute:proton antiporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010231; P:maintenance of seed dormancy; IMP:TAIR.
DR GO; GO:0010023; P:proanthocyanidin biosynthetic process; 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 Antiport; Flavonoid biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..507
FT /note="Protein DETOXIFICATION 41"
FT /id="PRO_0000164260"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..92
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..170
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..312
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..389
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..453
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 55147 MW; D1A90B316A2AEF4D CRC64;
MSSTETYEPL LTRLHSDSQI TERSSPEIEE FLRRRGSTVT PRWWLKLAVW ESKLLWTLSG
ASIVVSVLNY MLSFVTVMFT GHLGSLQLAG ASIATVGIQG LAYGIMLGMA SAVQTVCGQA
YGARQYSSMG IICQRAMVLH LAAAVFLTFL YWYSGPILKT MGQSVAIAHE GQIFARGMIP
QIYAFALACP MQRFLQAQNI VNPLAYMSLG VFLLHTLLTW LVTNVLDFGL LGAALILSFS
WWLLVAVNGM YILMSPNCKE TWTGFSTRAF RGIWPYFKLT VASAVMLCLE IWYNQGLVII
SGLLSNPTIS LDAISICMYY LNWDMQFMLG LSAAISVRVS NELGAGNPRV AMLSVVVVNI
TTVLISSVLC VIVLVFRVGL SKAFTSDAEV IAAVSDLFPL LAVSIFLNGI QPILSGVAIG
SGWQAVVAYV NLVTYYVIGL PIGCVLGFKT SLGVAGIWWG MIAGVILQTL TLIVLTLKTN
WTSEVENAAQ RVKTSATENQ EMANAGV
