DTX35_ARATH
ID DTX35_ARATH Reviewed; 488 AA.
AC F4JTB3; Q0WWD0; Q9SZZ2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Protein DETOXIFICATION 35 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX35 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 35 {ECO:0000305};
DE Short=MATE protein 35 {ECO:0000305};
DE AltName: Full=Protein DETOXIFYING EFFLUX CARRIER 35 {ECO:0000303|PubMed:19995827};
DE Short=Protein DTX5 {ECO:0000303|PubMed:19995827};
DE AltName: Full=Protein FLOWER FLAVONOID TRANSPORTER {ECO:0000303|PubMed:19995827};
DE Short=Protein FFT {ECO:0000303|PubMed:19995827};
GN Name=DTX35 {ECO:0000303|PubMed:11739388};
GN Synonyms=FFT {ECO:0000303|PubMed:19995827};
GN OrderedLocusNames=At4g25640 {ECO:0000312|Araport:AT4G25640};
GN ORFNames=L73G19.20 {ECO:0000312|EMBL:CAB43695.1};
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 [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 [2]
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 [3]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [7]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19995827; DOI=10.1093/jxb/erp312;
RA Thompson E.P., Wilkins C., Demidchik V., Davies J.M., Glover B.J.;
RT "An Arabidopsis flavonoid transporter is required for anther dehiscence and
RT pollen development.";
RL J. Exp. Bot. 61:439-451(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20505354; DOI=10.4161/psb.5.7.11894;
RA Thompson E.P., Davies J.M., Glover B.J.;
RT "Identifying the transporters of different flavonoids in plants.";
RL Plant Signal. Behav. 5:860-863(2010).
CC -!- FUNCTION: Multidrug and toxin efflux transporter involved in flavonoid
CC metabolism. Required for proper reproductive development.
CC {ECO:0000269|PubMed:19995827}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17151019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4JTB3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescence tissues,
CC especially in floral epidermal guard cells including those of the
CC anthers, stigma, siliques and nectaries. Also detected in the
CC meristematic zone of the root apex and in the elongation zone through
CC to the fully expanded cells of the differentiation zone.
CC {ECO:0000269|PubMed:19995827}.
CC -!- DISRUPTION PHENOTYPE: Affected flavonoid levels in the plant. Altered
CC root growth, seed development and germination, and pollen development
CC and release (PubMed:19995827). Enhanced growth and early flowering in
CC comparison to the wild type (PubMed:20505354).
CC {ECO:0000269|PubMed:19995827, ECO:0000269|PubMed:20505354}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81374.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL050400; CAB43695.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81374.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85086.1; -; Genomic_DNA.
DR EMBL; AK226424; BAE98568.1; -; mRNA.
DR PIR; T09556; T09556.
DR RefSeq; NP_001329321.1; NM_001341758.1.
DR RefSeq; NP_194294.2; NM_118696.5. [F4JTB3-1]
DR AlphaFoldDB; F4JTB3; -.
DR SMR; F4JTB3; -.
DR STRING; 3702.AT4G25640.2; -.
DR PaxDb; F4JTB3; -.
DR ProteomicsDB; 222223; -. [F4JTB3-1]
DR EnsemblPlants; AT4G25640.1; AT4G25640.1; AT4G25640. [F4JTB3-1]
DR GeneID; 828669; -.
DR Gramene; AT4G25640.1; AT4G25640.1; AT4G25640. [F4JTB3-1]
DR KEGG; ath:AT4G25640; -.
DR Araport; AT4G25640; -.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR OMA; TRDHFAV; -.
DR PRO; PR:F4JTB3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTB3; baseline and differential.
DR Genevisible; F4JTB3; 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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:UniProtKB.
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:0009813; P:flavonoid 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 1: Evidence at protein level;
KW Alternative splicing; Flavonoid biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..488
FT /note="Protein DETOXIFICATION 35"
FT /id="PRO_0000434076"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 127
FT /note="C -> Y (in Ref. 3; BAE98568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 53225 MW; 7563337664C7DD51 CRC64;
MDPTAPLLTH GGEVEEDYAP ARSWTDVKRV LSTESAKLWM IAAPVGFNII CQYGVSSVTN
IFVGHIGEVE LSAVSISLSV IGTFSFGFLL GMGSALETLC GQAYGAGQVN MLGVYMQRSW
IILFVSCFFL LPIYIFATPV LRLLGQAEEI AVPAGQFTLL TIPQLFSLAF NFPTSKFLQA
QSKVVAIAWI GFVALSLHVI MLWLFIIEFG WGTNGAALAF NITNWGTAIA QIVYVIGWCN
EGWTGLSWLA FKEIWAFVRL SIASAVMLCL EIWYMMSIIV LTGRLDNAVI AVDSLSICMN
INGLEAMLFI GINAAISVRV SNELGLGRPR AAKYSVYVTV FQSLLIGLVF MVAIIIARDH
FAIIFTSSKV LQRAVSKLAY LLGITMVLNS VQPVVSGVAV GGGWQGLVAY INLGCYYIFG
LPFGYLLGYI ANFGVMGLWS GMIAGTALQT LLLLIVLYKT NWNKEVEETM ERMKKWGGSE
TTSKDILA
