DTX42_ARATH
ID DTX42_ARATH Reviewed; 515 AA.
AC Q9SYD6; Q3ECS6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein DETOXIFICATION 42 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX42 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Aluminum-activated citrate transporter {ECO:0000303|PubMed:18826429};
DE AltName: Full=AtMATE {ECO:0000303|PubMed:18826429};
DE AltName: Full=FRD-like protein {ECO:0000303|PubMed:12172022};
DE AltName: Full=Multidrug and toxic compound extrusion protein 42 {ECO:0000305};
DE Short=MATE protein 42 {ECO:0000305};
GN Name=DTX42 {ECO:0000303|PubMed:11739388};
GN Synonyms=FRDL {ECO:0000303|PubMed:12172022},
GN MATE {ECO:0000303|PubMed:18826429};
GN OrderedLocusNames=At1g51340 {ECO:0000312|Araport:AT1G51340};
GN ORFNames=F11M15.20 {ECO:0000312|EMBL:AAD30646.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 3).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 IDENTIFICATION.
RC STRAIN=cv. Columbia;
RX PubMed=12172022; DOI=10.1105/tpc.001495;
RA Rogers E.E., Guerinot M.L.;
RT "FRD3, a member of the multidrug and toxin efflux family, controls iron
RT deficiency responses in Arabidopsis.";
RL Plant Cell 14:1787-1799(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).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=16098107; DOI=10.1111/j.1365-313x.2005.02473.x;
RA Hori K., Watanabe Y.;
RT "UPF3 suppresses aberrant spliced mRNA in Arabidopsis.";
RL Plant J. 43:530-540(2005).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ALUMINUM, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT families function independently to confer Arabidopsis aluminum tolerance.";
RL Plant J. 57:389-399(2009).
RN [10]
RP INDUCTION BY ALUMINUM, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=22413742; DOI=10.1111/j.1365-313x.2012.04994.x;
RA Liu J., Luo X., Shaff J., Liang C., Jia X., Li Z., Magalhaes J.,
RA Kochian L.V.;
RT "A promoter-swap strategy between the AtALMT and AtMATE genes increased
RT Arabidopsis aluminum resistance and improved carbon-use efficiency for
RT aluminum resistance.";
RL Plant J. 71:327-337(2012).
CC -!- FUNCTION: Citrate transporter critical for aluminum tolerance.
CC Responsible for citrate exudation into the rhizosphere to protect roots
CC from aluminum toxicity. {ECO:0000269|PubMed:18826429,
CC ECO:0000269|PubMed:22413742}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SYD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SYD6-2; Sequence=VSP_040657;
CC Name=3;
CC IsoId=Q9SYD6-3; Sequence=VSP_057894, VSP_057895;
CC -!- TISSUE SPECIFICITY: Expressed in roots, but not in shoots
CC (PubMed:18826429, PubMed:22413742). Detected in the mature regions of
CC the root, extending from above the root-hair region to the root-shoot
CC junction (PubMed:22413742). {ECO:0000269|PubMed:18826429,
CC ECO:0000269|PubMed:22413742}.
CC -!- INDUCTION: Up-regulated by aluminum (PubMed:18826429, PubMed:22413742).
CC The STOP1 transcription factor is required for MATE expression
CC (PubMed:18826429). {ECO:0000269|PubMed:18826429,
CC ECO:0000269|PubMed:22413742}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Strong reduction of aluminum-activated citrate release and
CC small decrease in aluminum tolerance. {ECO:0000269|PubMed:18826429}.
CC -!- MISCELLANEOUS: Acts in parallel but independently of ALMT1, an
CC aluminum-activated root malate transporter.
CC {ECO:0000303|PubMed:18826429}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice
CC site. Aberrant spliced mRNA with a premature translation termination
CC codon (PTC) that could be the target of the NMD degradation pathway.
CC {ECO:0000269|PubMed:16098107}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30646.1; Type=Erroneous gene model prediction; Evidence={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; AC006085; AAD30646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32652.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32653.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60202.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60203.1; -; Genomic_DNA.
DR EMBL; AY059793; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX818238; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D96551; D96551.
DR RefSeq; NP_001319195.1; NM_001333481.1. [Q9SYD6-1]
DR RefSeq; NP_001322504.1; NM_001333482.1. [Q9SYD6-1]
DR RefSeq; NP_564588.2; NM_104012.3. [Q9SYD6-2]
DR RefSeq; NP_974000.1; NM_202271.2. [Q9SYD6-1]
DR AlphaFoldDB; Q9SYD6; -.
DR SMR; Q9SYD6; -.
DR BioGRID; 26782; 1.
DR STRING; 3702.AT1G51340.2; -.
DR PaxDb; Q9SYD6; -.
DR PRIDE; Q9SYD6; -.
DR EnsemblPlants; AT1G51340.1; AT1G51340.1; AT1G51340. [Q9SYD6-2]
DR EnsemblPlants; AT1G51340.2; AT1G51340.2; AT1G51340. [Q9SYD6-1]
DR EnsemblPlants; AT1G51340.3; AT1G51340.3; AT1G51340. [Q9SYD6-1]
DR EnsemblPlants; AT1G51340.5; AT1G51340.5; AT1G51340. [Q9SYD6-1]
DR GeneID; 841557; -.
DR Gramene; AT1G51340.1; AT1G51340.1; AT1G51340. [Q9SYD6-2]
DR Gramene; AT1G51340.2; AT1G51340.2; AT1G51340. [Q9SYD6-1]
DR Gramene; AT1G51340.3; AT1G51340.3; AT1G51340. [Q9SYD6-1]
DR Gramene; AT1G51340.5; AT1G51340.5; AT1G51340. [Q9SYD6-1]
DR KEGG; ath:AT1G51340; -.
DR Araport; AT1G51340; -.
DR TAIR; locus:2008236; AT1G51340.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_16_2_1; -.
DR InParanoid; Q9SYD6; -.
DR OMA; MDGIWLA; -.
DR PhylomeDB; Q9SYD6; -.
DR PRO; PR:Q9SYD6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYD6; baseline and differential.
DR Genevisible; Q9SYD6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035618; C:root hair; IDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015746; P:citrate transport; IMP:UniProtKB.
DR GO; GO:0010044; P:response to aluminum ion; IEP:UniProtKB.
DR CDD; cd13136; MATE_DinF_like; 1.
DR InterPro; IPR044644; DinF-like.
DR InterPro; IPR002528; MATE_fam.
DR PANTHER; PTHR42893; PTHR42893; 1.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Protein DETOXIFICATION 42"
FT /id="PRO_0000405271"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..24
FT /note="MMSEDGYNTDFPRNPLYIFFSDFR -> MATTQIFQETLYTFSLVI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040657"
FT VAR_SEQ 361..362
FT /note="YA -> QY (in isoform 3)"
FT /id="VSP_057894"
FT VAR_SEQ 363..515
FT /note="Missing (in isoform 3)"
FT /id="VSP_057895"
SQ SEQUENCE 515 AA; 55374 MW; AC850FC0DEA1CF43 CRC64;
MMSEDGYNTD FPRNPLYIFF SDFRSVLKFD ELGLEIARIA LPAALALTAD PIASLVDTAF
IGQIGPVELA AVGVSIALFN QVSRIAIFPL VSITTSFVAE EDACSSQQDT VRDHKECIEI
GINNPTEETI ELIPEKHKDS LSDEFKTSSS IFSISKPPAK KRNIPSASSA LIIGGVLGLF
QAVFLISAAK PLLSFMGVKH DSPMMRPSQR YLSLRSLGAP AVLLSLAAQG VFRGFKDTTT
PLFATVIGDV TNIILDPIFI FVFRLGVTGA ATAHVISQYL MCGILLWKLM GQVDIFNMST
KHLQFCRFMK NGFLLLMRVI AVTFCVTLSA SLAAREGSTS MAAFQVCLQV WLATSLLADG
YAVAGQAILA SAFAKKDYKR AAATASRVLQ LGLVLGFVLA VILGAGLHFG ARVFTKDDKV
LHLISIGLPF VAGTQPINAL AFVFDGVNFG ASDFGYAAAS LVMVAIVSIL CLLFLSSTHG
FIGLWFGLTI YMSLRAAVGF WRIGTGTGPW SFLRS
