DTX9_ARATH
ID DTX9_ARATH Reviewed; 482 AA.
AC Q9C9M8; Q9C5H0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein DETOXIFICATION 9 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX9 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 9 {ECO:0000305};
DE Short=MATE protein 9 {ECO:0000305};
GN Name=DTX9 {ECO:0000303|PubMed:11739388};
GN OrderedLocusNames=At1g66760 {ECO:0000312|Araport:AT1G66760};
GN ORFNames=F4N21_11 {ECO:0000312|EMBL:AAG60073.1};
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].
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C9M8-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AC013288; AAG60073.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34553.1; -; Genomic_DNA.
DR EMBL; AF360254; AAK25964.1; -; mRNA.
DR RefSeq; NP_849854.1; NM_179523.4. [Q9C9M8-1]
DR AlphaFoldDB; Q9C9M8; -.
DR SMR; Q9C9M8; -.
DR IntAct; Q9C9M8; 10.
DR STRING; 3702.AT1G66760.2; -.
DR PaxDb; Q9C9M8; -.
DR PRIDE; Q9C9M8; -.
DR ProteomicsDB; 220729; -. [Q9C9M8-1]
DR EnsemblPlants; AT1G66760.2; AT1G66760.2; AT1G66760. [Q9C9M8-1]
DR GeneID; 842994; -.
DR Gramene; AT1G66760.2; AT1G66760.2; AT1G66760. [Q9C9M8-1]
DR KEGG; ath:AT1G66760; -.
DR Araport; AT1G66760; -.
DR TAIR; locus:2033334; AT1G66760.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; Q9C9M8; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9C9M8; -.
DR PRO; PR:Q9C9M8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M8; baseline and differential.
DR Genevisible; Q9C9M8; 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:0009611; P:response to wounding; IEP:TAIR.
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 Alternative splicing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..482
FT /note="Protein DETOXIFICATION 9"
FT /id="PRO_0000434052"
FT TRANSMEM 32..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 264
FT /note="C -> F (in Ref. 3; AAK25964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 53066 MW; 521F5C3DF963403A CRC64;
MKKSIETPLL LNTKQSQDED KEKIRWEKMK KVASMAAPMV AVNMSQYLLQ ATSTMIVGHR
SELALAGIAL GSSFANVTGF GVLFGLSGSL ETLCGQAYGA KQYHKLGSYT FTSIVFLLII
SVPISILWMF MNQILLLLHQ DPQIAELAGV YCLWLVPALF GYSVLESLVR YFQSQSLIYP
MVLSSLAALS FHVPLCWLMV HKFDFGAKGA AASIGISYWL NAVFLWVYMK RSSRCVETRI
YMSKDVFVHT NIFFQFAIPS AMMCCLEWLA FEVITLLSGL LPNSKLETSV ISICLTTSSL
HYNLVNGIGD AASTNVANEL GAGNPRGARD SAAAAIIIAA VESVIVSSSL FLSRSVWPYA
YSNVEEVISY VTDITPILCI SILMDSFLTV LSGIVRGTGW QKIGAYVNIT SYYVIGIPVG
LLLCFHLHFN GKGLWAGLVT GSTLQTLILF LVIGFTNWSK EAIKARERIG DEKVWRHDSL
LN
