DTX19_ARATH
ID DTX19_ARATH Reviewed; 477 AA.
AC Q9LUH2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein DETOXIFICATION 19 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX19 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 19 {ECO:0000305};
DE Short=MATE protein 19 {ECO:0000305};
DE AltName: Full=Protein ABERRANT LATERAL ROOT FORMATION 5 {ECO:0000303|PubMed:11449055};
GN Name=DTX19 {ECO:0000303|PubMed:11739388};
GN Synonyms=ALF5 {ECO:0000303|PubMed:11449055};
GN OrderedLocusNames=At3g23560 {ECO:0000312|Araport:AT3G23560};
GN ORFNames=MDB19.4 {ECO:0000312|EMBL:BAB02774.1};
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, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11449055; DOI=10.2307/3871390;
RA Diener A.C., Gaxiola R.A., Fink G.R.;
RT "Arabidopsis ALF5, a multidrug efflux transporter gene family member,
RT confers resistance to toxins.";
RL Plant Cell 13:1625-1638(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 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: Required for protection of the roots from inhibitory
CC compounds. When expressed in a heterologous system, confers resistance
CC to tetramethylammonium chloride. {ECO:0000269|PubMed:11449055}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the root epidermis and cortex. Not
CC expressed in hypocotyl. Detected in the elongation zone of young roots,
CC but not in the meristematic region. {ECO:0000269|PubMed:11449055}.
CC -!- DISRUPTION PHENOTYPE: Aberrant lateral root formation due to
CC hypersensitivity to toxic compounds. {ECO:0000269|PubMed:11449055}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AF337954; AAK21273.1; -; mRNA.
DR EMBL; AB023036; BAB02774.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76777.1; -; Genomic_DNA.
DR EMBL; AY062511; AAL32589.1; -; mRNA.
DR RefSeq; NP_566730.1; NM_113259.4.
DR AlphaFoldDB; Q9LUH2; -.
DR SMR; Q9LUH2; -.
DR BioGRID; 7267; 37.
DR IntAct; Q9LUH2; 36.
DR STRING; 3702.AT3G23560.1; -.
DR TCDB; 2.A.66.1.6; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q9LUH2; -.
DR PRIDE; Q9LUH2; -.
DR ProteomicsDB; 220719; -.
DR EnsemblPlants; AT3G23560.1; AT3G23560.1; AT3G23560.
DR GeneID; 821935; -.
DR Gramene; AT3G23560.1; AT3G23560.1; AT3G23560.
DR KEGG; ath:AT3G23560; -.
DR Araport; AT3G23560; -.
DR TAIR; locus:2088020; AT3G23560.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9LUH2; -.
DR OMA; FAIMSKQ; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9LUH2; -.
DR PRO; PR:Q9LUH2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUH2; baseline and differential.
DR Genevisible; Q9LUH2; 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: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:0009636; P:response to toxic substance; ISS: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 Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..477
FT /note="Protein DETOXIFICATION 19"
FT /id="PRO_0000405317"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 51852 MW; 1FE6F206DBD1B9F5 CRC64;
MADPATSSPL LDDHVGGEDE RGRRSRSSTL VQKVIDVEEA KAQMIYSLPM ILTNVFYYCI
PITSVMFASH LGQLELAGAT LANSWATVSG FAFMVGLSGS LETLCGQGFG AKRYRMLGVH
LQSSCIVSLV FSILITIFWF FTESIFGLLR QDPSISKQAA LYMKYQAPGL LAYGFLQNIL
RFCQTQSIIA PLVIFSFVPL VINIATAYVL VYVAGLGFIG APIATSISLW IAFLSLGTYV
MCSEKFKETW TGFSLESFRY IVINLTLSLP SAAMVCLEYW AFEILVFLAG VMPNPEINTS
LVAICVNTEA ISYMLTYGLS AAASTRVSNE LGAGNVKGAK KATSVSVKLS LVLALGVVIV
LLVGHDGWVG LFSDSYVIKE EFASLRFFLA ASITLDSIQG VLSGVARGCG WQRLVTVINL
ATFYLIGMPI AAFCGFKLKF YAKGLWIGLI CGIFCQSSSL LLMTIFRKWT KLNVATV
