DTX2_ARATH
ID DTX2_ARATH Reviewed; 476 AA.
AC Q8GXM8; Q9SIA2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein DETOXIFICATION 2 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX2 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 2 {ECO:0000305};
DE Short=MATE protein 2 {ECO:0000305};
GN Name=DTX2 {ECO:0000303|PubMed:11739388};
GN OrderedLocusNames=At2g04080 {ECO:0000312|Araport:AT2G04080};
GN ORFNames=F3L12.9 {ECO:0000312|EMBL:AAD28684.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28684.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007178; AAD28684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05797.1; -; Genomic_DNA.
DR EMBL; AK118147; BAC42772.1; -; mRNA.
DR EMBL; BT005511; AAO63931.1; -; mRNA.
DR PIR; D84454; D84454.
DR RefSeq; NP_001324727.1; NM_001335215.1.
DR RefSeq; NP_178497.2; NM_126449.5.
DR AlphaFoldDB; Q8GXM8; -.
DR SMR; Q8GXM8; -.
DR BioGRID; 345; 36.
DR IntAct; Q8GXM8; 35.
DR PaxDb; Q8GXM8; -.
DR PRIDE; Q8GXM8; -.
DR ProteomicsDB; 221872; -.
DR EnsemblPlants; AT2G04080.1; AT2G04080.1; AT2G04080.
DR GeneID; 814944; -.
DR Gramene; AT2G04080.1; AT2G04080.1; AT2G04080.
DR KEGG; ath:AT2G04080; -.
DR Araport; AT2G04080; -.
DR TAIR; locus:2050185; AT2G04080.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR InParanoid; Q8GXM8; -.
DR OMA; ATNIPIC; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q8GXM8; -.
DR PRO; PR:Q8GXM8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GXM8; baseline and differential.
DR Genevisible; Q8GXM8; 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: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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..476
FT /note="Protein DETOXIFICATION 2"
FT /id="PRO_0000405322"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 51570 MW; F526E5CCBD787FD1 CRC64;
MEEPFLPRDE QLVSCKSTWQ SGQVTVELKK VSRLAAPMAT VTIAQYLLPV ISVMVAGHIG
ELELAGVALA TSFTNVSGFS IMFGLVGALE TLCGQAYGAE QYEKIGTYTY SAMASNIPIC
FIISILWIYI EKLLITLGQE PDISRVAGSY SLWLVPALFA HAIFLPLTRF LLAQGLVISL
LYSAMTTLLF HIAVCWTLVF ALGLGSNGAA IAISLSFWFY AVILSCHVRF FSSCEKTRGF
VSNDFMSSIK QYFQYGVPSA GLICLEWWLF ELLILCSGLL PNPKLETSVL SICLTIGTLH
YVIPSGVAAA VSTRVSNKLG AGNPQVARVS VLAGLCLWLV ESAFFSTLLF TCRNIIGYTF
SNSKEVVDYV ADISPLLCLS FILDGLTAVL NGVARGCGWQ HIGALINVVA YYLVGAPVGV
YLAFSREWNG KGLWCGVMVG SAVQATLLAI VTASMNWKEQ AEKARKRIIS TENGLV
