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Protein DETOXIFICATION 50 (AtDTX50) (DETOXIFICATION EFFLUX CARRIER 50) (Multidrug and toxic compound extrusion protein 50) (MATE protein 50) (Protein ABNORMAL SHOOT 3-like 1)

 DTX50_ARATH             Reviewed;         505 AA.
Q9FJ87; Q7FLS2;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 102.
RecName: Full=Protein DETOXIFICATION 50 {ECO:0000303|PubMed:11739388};
Short=AtDTX50 {ECO:0000303|PubMed:11739388};
AltName: Full=DETOXIFICATION EFFLUX CARRIER 50 {ECO:0000303|PubMed:24851876};
AltName: Full=Multidrug and toxic compound extrusion protein 50 {ECO:0000305};
Short=MATE protein 50 {ECO:0000305};
AltName: Full=Protein ABNORMAL SHOOT 3-like 1 {ECO:0000303|PubMed:26160579};
Name=DTX50 {ECO:0000303|PubMed:11739388};
Synonyms=ABS3L1 {ECO:0000303|PubMed:26160579};
OrderedLocusNames=At5g52050 {ECO:0000312|Araport:AT5G52050};
ORFNames=MSG15.13 {ECO:0000312|EMBL:BAB11053.1};
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9872454; DOI=10.1093/dnares/5.5.297;
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VII.
Sequence features of the regions of 1,013,767 bp covered by sixteen
physically assigned P1 and TAC clones.";
DNA Res. 5:297-308(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
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).
[5]
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).
[6]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABA, SUBCELLULAR LOCATION,
AND DISRUPTION PHENOTYPE.
PubMed=24851876; DOI=10.1093/mp/ssu063;
Zhang H., Zhu H., Pan Y., Yu Y., Luan S., Li L.;
"A DTX/MATE-type transporter facilitates abscisic acid efflux and
modulates ABA sensitivity and drought tolerance in Arabidopsis.";
Mol. Plant 7:1522-1532(2014).
[7]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=26160579; DOI=10.1093/jxb/erv344;
Wang R., Liu X., Liang S., Ge Q., Li Y., Shao J., Qi Y., An L., Yu F.;
"A subgroup of MATE transporter genes regulates hypocotyl cell
elongation in Arabidopsis.";
J. Exp. Bot. 66:6327-6343(2015).
-!- FUNCTION: Functions as a multidrug and toxin extrusion transporter
in the export of abscisic acid (ABA) in guard cells. Plays a role
in ABA-mediated growth inhibition and responses to drought
conditions (PubMed:24851876). May act as a negative regulator of
hypocotyl cell elongation in the light (PubMed:26160579).
{ECO:0000269|PubMed:24851876, ECO:0000269|PubMed:26160579}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24851876};
Multi-pass membrane protein {ECO:0000269|PubMed:24851876}. Late
endosome membrane {ECO:0000269|PubMed:26160579}; Multi-pass
membrane protein {ECO:0000269|PubMed:26160579}.
-!- TISSUE SPECIFICITY: Preferentially expressed in rosette leaves.
Detected mainly in the vascular tissues and guard cells
(PubMed:24851876). Mostly detected at reproductive stages in young
anthers, in mature pollens and during pollen germination on the
pistil. Also expressed in developing seeds (PubMed:26160579).
{ECO:0000269|PubMed:24851876, ECO:0000269|PubMed:26160579}.
-!- INDUCTION: By abscisic acid. {ECO:0000269|PubMed:24851876}.
-!- DISRUPTION PHENOTYPE: Smaller and yellowish rosette leaves.
Enhanced sensitivity to abscisic acid (ABA) in growth inhibition
and seed germination. Accumulation of ABA in leaves. Enhanced
tolerance to drought with lower stomatal conductance.
{ECO:0000269|PubMed:24851876}.
-!- MISCELLANEOUS: Overexpression of DTX50 alters shoot developmental
programs leading to a loss of apical dominance phenotype.
{ECO:0000269|PubMed:26160579}.
-!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
(TC 2.A.66.1) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB015478; BAB11053.1; -; Genomic_DNA.
EMBL; CP002688; AED96166.1; -; Genomic_DNA.
EMBL; AK117985; BAC42620.2; -; mRNA.
RefSeq; NP_200018.1; NM_124584.3.
UniGene; At.29643; -.
ProteinModelPortal; Q9FJ87; -.
STRING; 3702.AT5G52050.1; -.
PaxDb; Q9FJ87; -.
EnsemblPlants; AT5G52050.1; AT5G52050.1; AT5G52050.
GeneID; 835280; -.
Gramene; AT5G52050.1; AT5G52050.1; AT5G52050.
KEGG; ath:AT5G52050; -.
Araport; AT5G52050; -.
TAIR; locus:2173098; AT5G52050.
eggNOG; KOG1347; Eukaryota.
eggNOG; COG0534; LUCA.
HOGENOM; HOG000177026; -.
KO; K03327; -.
OMA; CLTGPMV; -.
OrthoDB; EOG09360B5W; -.
PhylomeDB; Q9FJ87; -.
Reactome; R-ATH-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
PRO; PR:Q9FJ87; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FJ87; baseline and differential.
Genevisible; Q9FJ87; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0090440; F:abscisic acid transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0015297; F:antiporter activity; IEA:InterPro.
GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central.
GO; GO:0080168; P:abscisic acid transport; IMP:UniProtKB.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:2000070; P:regulation of response to water deprivation; IMP:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
InterPro; IPR002528; MATE_fam.
Pfam; PF01554; MatE; 2.
TIGRFAMs; TIGR00797; matE; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Endosome; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 505 Protein DETOXIFICATION 50.
/FTId=PRO_0000434084.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TRANSMEM 78 98 Helical. {ECO:0000255}.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TRANSMEM 194 214 Helical. {ECO:0000255}.
TRANSMEM 219 239 Helical. {ECO:0000255}.
TRANSMEM 275 295 Helical. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TRANSMEM 380 400 Helical. {ECO:0000255}.
TRANSMEM 424 444 Helical. {ECO:0000255}.
TRANSMEM 446 466 Helical. {ECO:0000255}.
CONFLICT 348 348 G -> V (in Ref. 3; BAC42620).
{ECO:0000305}.
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


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