DTX48_ARATH
ID DTX48_ARATH Reviewed; 532 AA.
AC Q9SLV0; Q67YZ2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein DETOXIFICATION 48 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX48 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 48 {ECO:0000305};
DE Short=MATE protein 48 {ECO:0000305};
DE AltName: Full=Protein ABNORMAL SHOOT 4 {ECO:0000303|PubMed:26160579};
DE AltName: Full=Protein BUSH-AND-CHLOROTIC-DWARF 1 {ECO:0000303|PubMed:22150160};
DE Short=Protein BCD1 {ECO:0000303|PubMed:22150160};
DE AltName: Full=Protein ZRIZI {ECO:0000303|PubMed:21257605};
GN Name=DTX48 {ECO:0000303|PubMed:11739388};
GN Synonyms=ABS4 {ECO:0000303|PubMed:26160579},
GN BCD1 {ECO:0000303|PubMed:22150160}, ZF14 {ECO:0000312|EMBL:BAA87939.1},
GN ZRZ {ECO:0000303|PubMed:21257605};
GN OrderedLocusNames=At1g58340 {ECO:0000312|Araport:AT1G58340};
GN ORFNames=F19C14.5 {ECO:0000312|EMBL:BAA87939.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
RN [2]
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 [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 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).
RN [7]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21257605; DOI=10.1093/pcp/pcr007;
RA Burko Y., Geva Y., Refael-Cohen A., Shleizer-Burko S., Shani E., Berger Y.,
RA Halon E., Chuck G., Moshelion M., Ori N.;
RT "From organelle to organ: ZRIZI MATE-Type transporter is an organelle
RT transporter that enhances organ initiation.";
RL Plant Cell Physiol. 52:518-527(2011).
RN [8]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22150160; DOI=10.1042/bj20111311;
RA Seo P.J., Park J., Park M.J., Kim Y.S., Kim S.G., Jung J.H., Park C.M.;
RT "A Golgi-localized MATE transporter mediates iron homoeostasis under
RT osmotic stress in Arabidopsis.";
RL Biochem. J. 442:551-561(2012).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26160579; DOI=10.1093/jxb/erv344;
RA Wang R., Liu X., Liang S., Ge Q., Li Y., Shao J., Qi Y., An L., Yu F.;
RT "A subgroup of MATE transporter genes regulates hypocotyl cell elongation
RT in Arabidopsis.";
RL J. Exp. Bot. 66:6327-6343(2015).
CC -!- FUNCTION: Functions as a multidrug and toxin extrusion transporter.
CC Contributes to iron homeostasis during stress responses and senescence
CC (PubMed:22150160). Could be involved in specifying the lateral organ
CC initiation rate (PubMed:21257605). May act as a negative regulator of
CC hypocotyl cell elongation in the light (PubMed:26160579).
CC {ECO:0000269|PubMed:21257605, ECO:0000269|PubMed:22150160,
CC ECO:0000269|PubMed:26160579}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22150160}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22150160}. Late endosome membrane
CC {ECO:0000269|PubMed:26160579}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26160579}.
CC -!- TISSUE SPECIFICITY: Highly expressed in shoot apices relative to leaves
CC (PubMed:21257605). At vegetative stages, highly expressed at the
CC stipules. At reproductive stages, most highly expressed in the mature
CC pollen. Also expressed in the tips of sepals (PubMed:26160579).
CC {ECO:0000269|PubMed:21257605, ECO:0000269|PubMed:26160579}.
CC -!- INDUCTION: Induced by excessive iron, but repressed by iron deficiency.
CC Induced by heat, darkness, osmotic stresses and acid abscisic (ABA).
CC {ECO:0000269|PubMed:22150160}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21257605, ECO:0000269|PubMed:22150160}.
CC -!- MISCELLANEOUS: Plants overexpressing DTX48 in initiating leaves are
CC short, produce leaves much faster than wild-type plants and show
CC enhanced growth of axillary buds (PubMed:21257605). Overexpression of
CC DTX48 alters shoot developmental programs leading to a loss of apical
CC dominance phenotype (PubMed:26160579). {ECO:0000269|PubMed:21257605,
CC ECO:0000269|PubMed:26160579}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AB028198; BAA87939.1; -; mRNA.
DR EMBL; AC008051; AAF82254.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33537.1; -; Genomic_DNA.
DR EMBL; AK176206; BAD43969.1; -; mRNA.
DR EMBL; AK176326; BAD44089.1; -; mRNA.
DR PIR; T52442; T52442.
DR RefSeq; NP_564731.1; NM_104614.5.
DR AlphaFoldDB; Q9SLV0; -.
DR SMR; Q9SLV0; -.
DR IntAct; Q9SLV0; 32.
DR STRING; 3702.AT1G58340.1; -.
DR TCDB; 2.A.66.1.51; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q9SLV0; -.
DR PRIDE; Q9SLV0; -.
DR ProteomicsDB; 220722; -.
DR EnsemblPlants; AT1G58340.1; AT1G58340.1; AT1G58340.
DR GeneID; 842203; -.
DR Gramene; AT1G58340.1; AT1G58340.1; AT1G58340.
DR KEGG; ath:AT1G58340; -.
DR Araport; AT1G58340; -.
DR TAIR; locus:2016615; AT1G58340.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9SLV0; -.
DR OMA; AMISMIF; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9SLV0; -.
DR PRO; PR:Q9SLV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SLV0; baseline and differential.
DR Genevisible; Q9SLV0; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:TAIR.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0006826; P:iron ion transport; IGI:TAIR.
DR GO; GO:1905428; P:regulation of plant organ formation; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
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 Endosome; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..532
FT /note="Protein DETOXIFICATION 48"
FT /id="PRO_0000434082"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 496..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 66
FT /note="S -> P (in Ref. 4; BAD43969/BAD44089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 57847 MW; 8640D6256B2FAC76 CRC64;
MCNSKPSSAS SSLLSCKDKT HISKLETCDT DNPHYSEFRD TDSLDLKRWP SFLEGLEEVK
AIGKISGPTA MTGLLMYSRA MISMLFLGYL GELELAGGSL SIGFANITGY SVISGLSMGM
EPICGQAYGA KQMKLLGLTL QRTVLLLLSC SVPISFSWLN MRRILLWCGQ DEEISSVAQQ
FLLFAIPDLF LLSLLHPLRI YLRTQNITLP VTYSTAVSVL LHVPLNYLLV VKLEMGVAGV
AIAMVLTNLN LVVLLSSFVY FTSVHSDTWV PITIDSLKGW SALLSLAIPT CVSVCLEWWW
YEFMIILCGL LANPRATVAS MGILIQTTAL VYVFPSSLSL GVSTRISNEL GAKRPAKARV
SMIISLFCAI ALGLMAMVFA VLVRHHWGRL FTTDAEILQL TSIALPIVGL CELGNCPQTT
GCGVLRGCAR PTLGANINLG SFYFVGMPVA ILFGFVFKQG FPGLWFGLLA AQATCASLML
CALLRTDWKV QAERAEELTS QTPGKSPPLL PIASSKSRST SGTEDMMRTM LV
