DTX50_ARATH
ID DTX50_ARATH Reviewed; 505 AA.
AC Q9FJ87; Q7FLS2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein DETOXIFICATION 50 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX50 {ECO:0000303|PubMed:11739388};
DE AltName: Full=DETOXIFICATION EFFLUX CARRIER 50 {ECO:0000303|PubMed:24851876};
DE AltName: Full=Multidrug and toxic compound extrusion protein 50 {ECO:0000305};
DE Short=MATE protein 50 {ECO:0000305};
DE AltName: Full=Protein ABNORMAL SHOOT 3-like 1 {ECO:0000303|PubMed:26160579};
GN Name=DTX50 {ECO:0000303|PubMed:11739388};
GN Synonyms=ABS3L1 {ECO:0000303|PubMed:26160579};
GN OrderedLocusNames=At5g52050 {ECO:0000312|Araport:AT5G52050};
GN ORFNames=MSG15.13 {ECO:0000312|EMBL:BAB11053.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, TISSUE SPECIFICITY, INDUCTION BY ABA, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24851876; DOI=10.1093/mp/ssu063;
RA Zhang H., Zhu H., Pan Y., Yu Y., Luan S., Li L.;
RT "A DTX/MATE-type transporter facilitates abscisic acid efflux and modulates
RT ABA sensitivity and drought tolerance in Arabidopsis.";
RL Mol. Plant 7:1522-1532(2014).
RN [7]
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 in
CC the export of abscisic acid (ABA) in guard cells. Plays a role in ABA-
CC mediated growth inhibition and responses to drought conditions
CC (PubMed:24851876). May act as a negative regulator of hypocotyl cell
CC elongation in the light (PubMed:26160579).
CC {ECO:0000269|PubMed:24851876, ECO:0000269|PubMed:26160579}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24851876};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24851876}. Late
CC endosome membrane {ECO:0000269|PubMed:26160579}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:26160579}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in rosette leaves.
CC Detected mainly in the vascular tissues and guard cells
CC (PubMed:24851876). Mostly detected at reproductive stages in young
CC anthers, in mature pollens and during pollen germination on the pistil.
CC Also expressed in developing seeds (PubMed:26160579).
CC {ECO:0000269|PubMed:24851876, ECO:0000269|PubMed:26160579}.
CC -!- INDUCTION: By abscisic acid. {ECO:0000269|PubMed:24851876}.
CC -!- DISRUPTION PHENOTYPE: Smaller and yellowish rosette leaves. Enhanced
CC sensitivity to abscisic acid (ABA) in growth inhibition and seed
CC germination. Accumulation of ABA in leaves. Enhanced tolerance to
CC drought with lower stomatal conductance. {ECO:0000269|PubMed:24851876}.
CC -!- MISCELLANEOUS: Overexpression of DTX50 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}.
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; AB015478; BAB11053.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96166.1; -; Genomic_DNA.
DR EMBL; AK117985; BAC42620.2; -; mRNA.
DR RefSeq; NP_200018.1; NM_124584.3.
DR AlphaFoldDB; Q9FJ87; -.
DR SMR; Q9FJ87; -.
DR IntAct; Q9FJ87; 22.
DR STRING; 3702.AT5G52050.1; -.
DR TCDB; 2.A.66.1.58; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q9FJ87; -.
DR PRIDE; Q9FJ87; -.
DR EnsemblPlants; AT5G52050.1; AT5G52050.1; AT5G52050.
DR GeneID; 835280; -.
DR Gramene; AT5G52050.1; AT5G52050.1; AT5G52050.
DR KEGG; ath:AT5G52050; -.
DR Araport; AT5G52050; -.
DR TAIR; locus:2173098; AT5G52050.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9FJ87; -.
DR OMA; CVSGMMV; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9FJ87; -.
DR PRO; PR:Q9FJ87; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ87; baseline and differential.
DR Genevisible; Q9FJ87; AT.
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:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0090440; F:abscisic acid transmembrane transporter activity; IMP: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:0080168; P:abscisic acid transport; IMP:UniProtKB.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP: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 Cell membrane; Endosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..505
FT /note="Protein DETOXIFICATION 50"
FT /id="PRO_0000434084"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 348
FT /note="G -> V (in Ref. 3; BAC42620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 54970 MW; D06568D8215510F2 CRC64;
MSQSNRVRDE VTLPLLQKTS HLKNHSSVLS VFLNEAISIC KISYPLVLTG LFLYVRSFVS
LSFLGGLGDA TLAGGSLAAA FANITGYSLF SGLTMGVESI CSQAFGARRY NYVCASVKRG
IILLLVTSLP VTLLWMNMEK ILLILKQDKK LASEAHIFLL YSVPDLVAQS FLHPLRVYLR
TQSKTLPLSI CTVIASFLHL PITFFLVSYL GLGIKGIALS GVVSNFNLVA FLFLYICFFE
DKLSVNEDEK ITEETCEDSV REWKKLLCLA IPSCISVCLE WWCYEIMILL CGFLLDPKAS
VASMGILIQI TSLVYIFPHS LSLGVSTRVG NELGSNQPKR ARRAAIVGLG LSIALGFTAF
AFTVSVRNTW AMFFTDDKEI MKLTAMALPI VGLCELGNCP QTTGCGVLRG SARPKIGANI
NGVAFYAVGI PVGAVLAFWF GFGFKGLWLG MLAAQITCVI GMMAATCRTD WELEAERAKV
LTTAVDCGSS DDDAKEDMEA GMVDK
