DTX26_ARATH
ID DTX26_ARATH Reviewed; 489 AA.
AC Q1PDX9; Q9LX95;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein DETOXIFICATION 26 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX26 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 26 {ECO:0000305};
DE Short=MATE protein 26 {ECO:0000305};
GN Name=DTX26 {ECO:0000303|PubMed:11739388};
GN OrderedLocusNames=At5g10420 {ECO:0000312|Araport:AT5G10420};
GN ORFNames=F12B17_230 {ECO:0000312|EMBL:CAB89401.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAB89401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353995; CAB89401.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91538.1; -; Genomic_DNA.
DR EMBL; DQ446939; ABE66150.1; -; mRNA.
DR PIR; T49997; T49997.
DR RefSeq; NP_196604.2; NM_121080.3.
DR AlphaFoldDB; Q1PDX9; -.
DR SMR; Q1PDX9; -.
DR IntAct; Q1PDX9; 6.
DR STRING; 3702.AT5G10420.1; -.
DR PaxDb; Q1PDX9; -.
DR PRIDE; Q1PDX9; -.
DR ProteomicsDB; 224285; -.
DR EnsemblPlants; AT5G10420.1; AT5G10420.1; AT5G10420.
DR GeneID; 830906; -.
DR Gramene; AT5G10420.1; AT5G10420.1; AT5G10420.
DR KEGG; ath:AT5G10420; -.
DR Araport; AT5G10420; -.
DR TAIR; locus:2142544; AT5G10420.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR InParanoid; Q1PDX9; -.
DR OMA; FTIQRDW; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q1PDX9; -.
DR PRO; PR:Q1PDX9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDX9; baseline and differential.
DR Genevisible; Q1PDX9; 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: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..489
FT /note="Protein DETOXIFICATION 26"
FT /id="PRO_0000434067"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 53589 MW; CE78D338AB5F8DB4 CRC64;
MDKKSGGTKA IEEATVPLLE CHNAAEEGGG MKREIWIETK KIWYIVGPSI FTGLATYSIL
IITQAFAGHL GDLELAAISI INNFTLGFNY GLLLGMASAL ETLCGQAFGA REYYMLGVYM
QRYWIILFLC CILLLPMYLF ATPILKFIGQ SDDIAELTGT IALWVIPVHF AFAFFFPLNR
FLQCQLKNKV IAISAGVSLA VHILVCWFFV YGYKLGIIGT MASVNVPWWL NIFILFLYST
RGGCTLTWTG FSSEAFTGLL ELTKLSASSG IMLCLENWYY KILMLMTGNL VNAKIAVDSL
SICMSVNGWE MMIPLAFFAG TGVRVANELG AGNGKGARFA TIVSITLSLM IGLFFTVIIV
IFHDQIGSIF SSSEAVLNAV DNLSVLLAFT VLLNSVQPVL SGVAVGSGWQ SYVAYINLGC
YYLIGLPFGL TMGWIFKFGV KGIWAGMIFG GTAIQTLILI IITTRCDWDN EAHKSSVRIK
KWLVSDAGN
