DTX18_ARATH
ID DTX18_ARATH Reviewed; 469 AA.
AC Q9LUH3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein DETOXIFICATION 18 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX18 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 18 {ECO:0000305};
DE Short=MATE protein 18 {ECO:0000305};
DE AltName: Full=Protein LIKE ALF5 {ECO:0000303|PubMed:11449055};
GN Name=DTX18 {ECO:0000303|PubMed:11739388};
GN Synonyms=LAL5 {ECO:0000303|PubMed:11449055};
GN OrderedLocusNames=At3g23550 {ECO:0000312|Araport:AT3G23550};
GN ORFNames=MDB19.3 {ECO:0000312|EMBL:BAB02773.1};
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=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 [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=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 [4]
RP IDENTIFICATION.
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 [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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AB023036; BAB02773.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76776.1; -; Genomic_DNA.
DR EMBL; AY070032; AAL49789.1; -; mRNA.
DR EMBL; AY096384; AAM20025.1; -; mRNA.
DR RefSeq; NP_188997.1; NM_113258.5.
DR AlphaFoldDB; Q9LUH3; -.
DR SMR; Q9LUH3; -.
DR STRING; 3702.AT3G23550.1; -.
DR PaxDb; Q9LUH3; -.
DR PRIDE; Q9LUH3; -.
DR ProteomicsDB; 220718; -.
DR EnsemblPlants; AT3G23550.1; AT3G23550.1; AT3G23550.
DR GeneID; 821934; -.
DR Gramene; AT3G23550.1; AT3G23550.1; AT3G23550.
DR KEGG; ath:AT3G23550; -.
DR Araport; AT3G23550; -.
DR TAIR; locus:2088010; AT3G23550.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9LUH3; -.
DR OMA; MCENTEA; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9LUH3; -.
DR PRO; PR:Q9LUH3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUH3; baseline and differential.
DR Genevisible; Q9LUH3; 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:0002229; P:defense response to oomycetes; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IEP: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..469
FT /note="Protein DETOXIFICATION 18"
FT /id="PRO_0000405318"
FT TRANSMEM 40..60
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 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 469 AA; 50792 MW; 3B1ADE7221A60E74 CRC64;
MADPTSKDDH DGEGGRDKSS TFVQKLIDVE EAKTQIIYSL PMIFTNLFYY CIPLTSVMFA
SQLGQLELAG ATLANSWATV TGFAFMTGLS GALETLCGQG FGAKSYRMLG IHLQSSCIVS
LVFTILITIL WFFTESVFLL LRQDPSISKQ AALYMKYLAP GLLAYGFLQN ILRFCQTQCI
VTPLVLFSFL PLVINIGTTY ALVHLAGLGF IGAPIATSIS LWIAFVSLGF YVICSDKFKE
TWTGFSMESF HHVVLNLTLS IPSAAMVCLE YWAFEILVFL AGLMRNPEIT TSLVAICVNT
ESISYMLTCG LSAATSTRVS NELGAGNVKG AKKATSVSVK LSLVLALGVV IAILVGHDAW
VGLFSNSHVI KEGFASLRFF LAASITLDSI QGVLSGVARG CGWQRLATVI NLGTFYLIGM
PISVLCGFKL KLHAKGLWIG LICGMFCQSA SLLLMTIFRK WTKLTAATV
