DTX47_ARATH
ID DTX47_ARATH Reviewed; 543 AA.
AC Q945F0; Q67ZP3; Q9SVJ0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein DETOXIFICATION 47, chloroplastic {ECO:0000303|PubMed:11739388};
DE Short=AtDTX47 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 47 {ECO:0000305};
DE Short=MATE protein 47 {ECO:0000305};
DE AltName: Full=Protein ENHANCED DISEASE SUSCEPTIBILITY 5 {ECO:0000303|PubMed:9090877};
DE Short=Protein EDS5 {ECO:0000303|PubMed:9090877};
DE AltName: Full=Protein IMPORTANT FOR THE ARR PATHWAY 1 {ECO:0000303|PubMed:19694953};
DE Short=Protein IAP1 {ECO:0000303|PubMed:19694953};
DE AltName: Full=Protein SALICYLIC ACID INDUCTION DEFICIENT 1 {ECO:0000303|PubMed:10449575};
DE Short=Protein SID1 {ECO:0000303|PubMed:10449575};
DE AltName: Full=Protein SUSCEPTIBLE TO CORONATINE-DEFICIENT PST DC3000 3;
DE Short=Protein SCORD3 {ECO:0000303|PubMed:21998587};
DE Flags: Precursor;
GN Name=DTX47 {ECO:0000303|PubMed:11739388};
GN Synonyms=EDS5 {ECO:0000303|PubMed:9090877},
GN IAP1 {ECO:0000303|PubMed:19694953}, SCORD3 {ECO:0000303|PubMed:27862469},
GN SID1 {ECO:0000303|PubMed:10449575};
GN OrderedLocusNames=At4g39030 {ECO:0000312|Araport:AT4G39030};
GN ORFNames=F19H22.130 {ECO:0000312|EMBL:CAB38823.1};
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, AND INDUCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11826312; DOI=10.1105/tpc.010376;
RA Nawrath C., Heck S., Parinthawong N., Metraux J.-P.;
RT "EDS5, an essential component of salicylic acid-dependent signaling for
RT disease resistance in Arabidopsis, is a member of the MATE transporter
RT family.";
RL Plant Cell 14:275-286(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP MUTANT EDS5-1, AND DISRUPTION PHENOTYPE.
RX PubMed=9090877; DOI=10.2307/3870484;
RA Rogers E.E., Ausubel F.M.;
RT "Arabidopsis enhanced disease susceptibility mutants exhibit enhanced
RT susceptibility to several bacterial pathogens and alterations in PR-1 gene
RT expression.";
RL Plant Cell 9:305-316(1997).
RN [6]
RP MUTANT SID1, AND DISRUPTION PHENOTYPE.
RX PubMed=10449575; DOI=10.2307/3870970;
RA Nawrath C., Metraux J.P.;
RT "Salicylic acid induction-deficient mutants of Arabidopsis express PR-2 and
RT PR-5 and accumulate high levels of camalexin after pathogen inoculation.";
RL Plant Cell 11:1393-1404(1999).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11884688; DOI=10.1105/tpc.010481;
RA Kus J.V., Zaton K., Sarkar R., Cameron R.K.;
RT "Age-related resistance in Arabidopsis is a developmentally regulated
RT defense response to Pseudomonas syringae.";
RL Plant Cell 14:479-490(2002).
RN [9]
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 [10]
RP MUTANT IAP1-1, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19694953; DOI=10.1111/j.1364-3703.2009.00557.x;
RA Carviel J.L., Al-Daoud F., Neumann M., Mohammad A., Provart N.J.,
RA Moeder W., Yoshioka K., Cameron R.K.;
RT "Forward and reverse genetics to identify genes involved in the age-related
RT resistance response in Arabidopsis thaliana.";
RL Mol. Plant Pathol. 10:621-634(2009).
RN [11]
RP MUTANT SCORD3, AND DISRUPTION PHENOTYPE.
RX PubMed=21998587; DOI=10.1371/journal.ppat.1002291;
RA Zeng W., Brutus A., Kremer J.M., Withers J.C., Gao X., Jones A.D., He S.Y.;
RT "A genetic screen reveals Arabidopsis stomatal and/or apoplastic defenses
RT against Pseudomonas syringae pv. tomato DC3000.";
RL PLoS Pathog. 7:E1002291-E1002291(2011).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23757404; DOI=10.1104/pp.113.218156;
RA Serrano M., Wang B., Aryal B., Garcion C., Abou-Mansour E., Heck S.,
RA Geisler M., Mauch F., Nawrath C., Metraux J.P.;
RT "Export of salicylic acid from the chloroplast requires the multidrug and
RT toxin extrusion-like transporter EDS5.";
RL Plant Physiol. 162:1815-1821(2013).
RN [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23333976; DOI=10.4161/psb.23603;
RA Yamasaki K., Motomura Y., Yagi Y., Nomura H., Kikuchi S., Nakai M.,
RA Shiina T.;
RT "Chloroplast envelope localization of EDS5, an essential factor for
RT salicylic acid biosynthesis in Arabidopsis thaliana.";
RL Plant Signal. Behav. 8:E23603-E23603(2013).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24594657; DOI=10.1371/journal.pone.0088608;
RA Carviel J.L., Wilson D.C., Isaacs M., Carella P., Catana V., Golding B.,
RA Weretilnyk E.A., Cameron R.K.;
RT "Investigation of intercellular salicylic acid accumulation during
RT compatible and incompatible Arabidopsis-pseudomonas syringae interactions
RT using a fast neutron-generated mutant allele of EDS5 identified by genetic
RT mapping and whole-genome sequencing.";
RL PLoS ONE 9:E88608-E88608(2014).
CC -!- FUNCTION: Functions as a multidrug and toxin extrusion transporter in
CC the export of salicylic acid (SA) from the chloroplast to the cytoplasm
CC (PubMed:23757404). Plays an essential function in plant defense via the
CC pathogen-induced salicylic acid (SA) accumulation (PubMed:11826312,
CC PubMed:24594657). Acts also as a key component of the Age-related
CC resistance (ARR) pathway (PubMed:11884688, PubMed:19694953,
CC PubMed:24594657). {ECO:0000269|PubMed:11826312,
CC ECO:0000269|PubMed:11884688, ECO:0000269|PubMed:19694953,
CC ECO:0000269|PubMed:23757404, ECO:0000269|PubMed:24594657}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:23333976, ECO:0000269|PubMed:23757404}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:23333976,
CC ECO:0000269|PubMed:23757404}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the epidermal cells.
CC {ECO:0000269|PubMed:23333976}.
CC -!- INDUCTION: By salicylic acid, UV-C light and pathogens.
CC {ECO:0000269|PubMed:11826312}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to several bacterial
CC pathogens and alterations in PR-1 gene expression (PubMed:9090877). No
CC salicylic acid (SA) accumulation after pathogen inoculation and more
CC susceptibility to both virulent and avirulent forms of Pseudomonas
CC syringae and Peronospora parasitica (PubMed:10449575, PubMed:24594657).
CC Age-related resistance (ARR)-defective (PubMed:11884688,
CC PubMed:19694953). Defect in stomatal response during bacterial
CC infection (PubMed:21998587). {ECO:0000269|PubMed:10449575,
CC ECO:0000269|PubMed:11884688, ECO:0000269|PubMed:19694953,
CC ECO:0000269|PubMed:21998587, ECO:0000269|PubMed:24594657,
CC ECO:0000269|PubMed:9090877}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF416569; AAL27003.1; -; mRNA.
DR EMBL; AL035679; CAB38823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161594; CAB80566.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87009.1; -; Genomic_DNA.
DR EMBL; AK175482; BAD43245.1; -; mRNA.
DR EMBL; AK176074; BAD43837.1; -; mRNA.
DR EMBL; AK176272; BAD44035.1; -; mRNA.
DR EMBL; AK176334; BAD44097.1; -; mRNA.
DR RefSeq; NP_195614.2; NM_120063.6.
DR AlphaFoldDB; Q945F0; -.
DR SMR; Q945F0; -.
DR BioGRID; 15338; 26.
DR IntAct; Q945F0; 24.
DR STRING; 3702.AT4G39030.1; -.
DR TCDB; 2.A.66.1.11; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR SwissPalm; Q945F0; -.
DR PaxDb; Q945F0; -.
DR PRIDE; Q945F0; -.
DR ProteomicsDB; 221828; -.
DR EnsemblPlants; AT4G39030.1; AT4G39030.1; AT4G39030.
DR GeneID; 830058; -.
DR Gramene; AT4G39030.1; AT4G39030.1; AT4G39030.
DR KEGG; ath:AT4G39030; -.
DR Araport; AT4G39030; -.
DR TAIR; locus:2120267; AT4G39030.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_15_2_1; -.
DR InParanoid; Q945F0; -.
DR OMA; IVSAYMM; -.
DR OrthoDB; 1486027at2759; -.
DR PhylomeDB; Q945F0; -.
DR PRO; PR:Q945F0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q945F0; baseline and differential.
DR Genevisible; Q945F0; AT.
DR GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IDA: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; 1.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Coiled coil; Immunity; Innate immunity; Membrane;
KW Plant defense; Plastid; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..543
FT /note="Protein DETOXIFICATION 47, chloroplastic"
FT /id="PRO_0000164259"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 55..94
FT /evidence="ECO:0000255"
SQ SEQUENCE 543 AA; 59528 MW; DF2EEFE0942A51C5 CRC64;
MLIKSQRLTL FSPLLSKTRR IPVNSHQTLV AESVITRRTL GAITATPSFH KNPVVIRRRI
KLERVTRNCV RIDREIDEEE EEEEKERGDL VKQSIWEQMK EIVKFTGPAM GMWICGPLMS
LIDTVVIGQG SSIELAALGP GTVLCDHMSY VFMFLSVATS NMVATSLAKQ DKKEAQHQIS
VLLFIGLVCG LMMLLLTRLF GPWAVTAFTR GKNIEIVPAA NKYIQIRGLA WPFILVGLVA
QSASLGMKNS WGPLKALAAA TIINGLGDTI LCLFLGQGIA GAAWATTASQ IVSAYMMMDS
LNKEGYNAYS FAIPSPQELW KISALAAPVF ISIFSKIAFY SFIIYCATSM GTHVLAAHQV
MAQTYRMCNV WGEPLSQTAQ SFMPEMLYGA NRNLPKARTL LKSLMIIGAT LGLVLGVIGT
AVPGLFPGVY THDKVIISEM HRLLIPFFMA LSALPMTVSL EGTLLAGRDL KFVSSVMSSS
FIIGCLTLMF VTRSGYGLLG CWFVLVGFQW GRFGLYLRRL LSPGGILNSD GPSPYTVEKI
KSI
