DTX1_ARATH
ID DTX1_ARATH Reviewed; 476 AA.
AC Q9SIA5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein DETOXIFICATION 1 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX1 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 1 {ECO:0000305};
DE Short=MATE protein 1 {ECO:0000305};
GN Name=DTX1 {ECO:0000303|PubMed:11739388}; Synonyms=TX1;
GN OrderedLocusNames=At2g04040 {ECO:0000312|Araport:AT2G04040};
GN ORFNames=F3L12.13 {ECO:0000312|EMBL:AAD28687.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION, FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
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 [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).
CC -!- FUNCTION: Efflux carrier for plant-derived alkaloids, antibiotics,
CC heavy metal and other toxic compounds. Involved in cadmium
CC detoxification. Requires probably a proton-motive force for the efflux.
CC {ECO:0000269|PubMed:11739388}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739388};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11739388}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in flowers and
CC stems. {ECO:0000269|PubMed:11739388}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- CAUTION: Mistakenly referred to as AT2G04070 in PubMed:11739388.
CC {ECO:0000305}.
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DR EMBL; AC007178; AAD28687.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05791.1; -; Genomic_DNA.
DR EMBL; BT022022; AAY25434.1; -; mRNA.
DR EMBL; BT026371; ABH04478.1; -; mRNA.
DR EMBL; AK227153; BAE99196.1; -; mRNA.
DR PIR; A84454; A84454.
DR RefSeq; NP_178491.1; NM_126443.5.
DR AlphaFoldDB; Q9SIA5; -.
DR SMR; Q9SIA5; -.
DR BioGRID; 339; 37.
DR IntAct; Q9SIA5; 37.
DR STRING; 3702.AT2G04040.1; -.
DR TCDB; 2.A.66.1.8; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q9SIA5; -.
DR PRIDE; Q9SIA5; -.
DR ProteomicsDB; 221824; -.
DR EnsemblPlants; AT2G04040.1; AT2G04040.1; AT2G04040.
DR GeneID; 814938; -.
DR Gramene; AT2G04040.1; AT2G04040.1; AT2G04040.
DR KEGG; ath:AT2G04040; -.
DR Araport; AT2G04040; -.
DR TAIR; locus:2050190; AT2G04040.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9SIA5; -.
DR OMA; WIVESAF; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9SIA5; -.
DR PRO; PR:Q9SIA5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIA5; baseline and differential.
DR Genevisible; Q9SIA5; 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:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:TAIR.
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:0015691; P:cadmium ion transport; IDA:TAIR.
DR GO; GO:0051238; P:sequestering of metal ion; IDA:TAIR.
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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Protein DETOXIFICATION 1"
FT /id="PRO_0000405319"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 51845 MW; 1A6952FD82B14424 CRC64;
MEEPFLLRDE LLVPSQVTWH TNPLTVELKR VSRLAAPMAT VTIAQYLLPV ISVMVAGHNG
ELQLSGVALA NSFTNVTGFS IMCGLVGALE TLCGQAYGAK QYEKIGTYAY SAIASNIPIC
FLISILWLYI EKILISLGQD PEISRIAGSY AFWLIPALFG QAIVIPLSRF LLTQGLVIPL
LFTAVTTLLF HVLVCWTLVF LFGLGCNGPA MATSVSFWFY AVILSCYVRF SSSCEKTRGF
VSRDFVSSIK QFFQYGIPSA AMICLEWWLF EILILCSGLL PNPKLETSVL SICLTIETLH
YVISAGVAAA VSTRVSNNLG AGNPQVARVS VLAGLCLWIV ESAFFSILLF TCRNIIGYAF
SNSKEVLDYV ADLTPLLCLS FILDGFTAVL NGVARGSGWQ HIGAWNNTVS YYLVGAPVGI
YLAFSRELNG KGLWCGVVVG STVQATILAI VTASINWKEQ AEKARKRIVS TENRLA
