DTX54_ARATH
ID DTX54_ARATH Reviewed; 510 AA.
AC Q9LE20;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein DETOXIFICATION 54 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX54 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 54 {ECO:0000305};
DE Short=MATE protein 54 {ECO:0000305};
DE AltName: Full=Protein NOVEL ION CARRIER 2 {ECO:0000303|Ref.1};
DE Short=Protein NIC2 {ECO:0000303|Ref.1};
GN Name=DTX54 {ECO:0000303|PubMed:11739388};
GN Synonyms=NIC2 {ECO:0000312|EMBL:AAO85439.1};
GN OrderedLocusNames=At1g71870 {ECO:0000312|Araport:AT1G71870};
GN ORFNames=F14O23.25 {ECO:0000312|EMBL:AAF43240.1},
GN F17M19.2 {ECO:0000312|EMBL:AAG52224.1};
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].
RA Pellengahr K., Poree F., Dolniak B., Kursawe M., Mueller-Roeber B.;
RT "Four membrane transport proteins of the Arabidopsis MATE family influence
RT the Na(+) and Li(+) tolerance in yeast.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 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).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RA Dolniak B.;
RT "Functional characterisation of NIC2, a member of the MATE family from
RT Arabidopsis thaliana (L.) Heynh.";
RL Thesis (2005), University of Postdam, Germany.
CC -!- FUNCTION: May function as a multidrug and toxin extrusion transporter
CC in the export of IAA-conjugates from the cytoplasm into peroxisomes.
CC {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|Ref.6}; Multi-
CC pass membrane protein {ECO:0000269|Ref.6}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissue of all organs.
CC {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AF489857; AAO85439.1; -; mRNA.
DR EMBL; AC012654; AAF43240.1; -; Genomic_DNA.
DR EMBL; AC021665; AAG52224.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35246.1; -; Genomic_DNA.
DR PIR; D96741; D96741.
DR RefSeq; NP_177332.1; NM_105845.2.
DR AlphaFoldDB; Q9LE20; -.
DR SMR; Q9LE20; -.
DR STRING; 3702.AT1G71870.1; -.
DR PaxDb; Q9LE20; -.
DR PRIDE; Q9LE20; -.
DR ProteomicsDB; 222169; -.
DR EnsemblPlants; AT1G71870.1; AT1G71870.1; AT1G71870.
DR GeneID; 843518; -.
DR Gramene; AT1G71870.1; AT1G71870.1; AT1G71870.
DR KEGG; ath:AT1G71870; -.
DR Araport; AT1G71870; -.
DR TAIR; locus:2013006; AT1G71870.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9LE20; -.
DR OMA; MASTYCI; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9LE20; -.
DR PRO; PR:Q9LE20; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LE20; baseline and differential.
DR Genevisible; Q9LE20; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
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; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Protein DETOXIFICATION 54"
FT /id="PRO_0000434088"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..468
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 510 AA; 54793 MW; 2B5D52278F1E96CF CRC64;
MEDKIQSDDF TSHKNPTLPQ VIEELKELWA MVLPITAMNC LVYVRAVVSV LFLGRLGSLE
LAGGALSIGF TNITGYSVMV GLASGLEPVC SQAYGSKNWD LLTLSLHRMV VILLMASLPI
SLLWINLGPI MLFMGQNPEI TATAAEYCLY ALPDLLTNTL LQPLRVYLRS QRVTKPMMWC
TLAAVAFHVP LNYWLVMVKH WGVPGVAIAS VVTNLIMVVL LVGYVWVSGM LQKRVSGDGD
GGSTTMVAVV AQSSSVMELV GGLGPLMRVA VPSCLGICLE WWWYEIVIVM GGYLENPKLA
VAATGILIQT TSLMYTVPMA LAGCVSARVG NELGAGRPYK ARLAANVALA CAFVVGALNV
AWTVILKERW AGLFTGYEPL KVLVASVMPI VGLCELGNCP QTTGCGILRG TGRPAVGAHV
NLGSFYFVGT PVAVGLAFWL KIGFSGLWFG LLSAQAACVV SILYAVLART DWEGEAVKAM
RLTSLEMRKV GQDEESSLLL LDDEKLGDVL
