DTX29_ARATH
ID DTX29_ARATH Reviewed; 500 AA.
AC Q38956; Q96278;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein DETOXIFICATION 29 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX29 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 29 {ECO:0000305};
DE Short=MATE protein 29 {ECO:0000305};
GN Name=DTX29 {ECO:0000303|PubMed:11739388};
GN OrderedLocusNames=At3g26590 {ECO:0000312|Araport:AT3G26590};
GN ORFNames=MFE16.12 {ECO:0000312|EMBL:BAB01841.1};
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; TISSUE=Shoot {ECO:0000312|EMBL:CAA66405.1};
RX PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA Quigley F., Dao P., Cottet A., Mache R.;
RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT III.";
RL Nucleic Acids Res. 24:4313-4318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23903016; DOI=10.1093/pcp/pct107;
RA Yoshida K., Ohnishi M., Fukao Y., Okazaki Y., Fujiwara M., Song C.,
RA Nakanishi Y., Saito K., Shimmen T., Suzaki T., Hayashi F., Fukaki H.,
RA Maeshima M., Mimura T.;
RT "Studies on vacuolar membrane microdomains isolated from Arabidopsis
RT suspension-cultured cells: local distribution of vacuolar membrane
RT proteins.";
RL Plant Cell Physiol. 54:1571-1584(2013).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019,
CC ECO:0000269|PubMed:23903016}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:23903016}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66405.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X97826; CAA66405.1; ALT_FRAME; mRNA.
DR EMBL; AB028611; BAB01841.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77183.1; -; Genomic_DNA.
DR EMBL; AY057664; AAL15295.1; -; mRNA.
DR EMBL; BT002302; AAN73299.1; -; mRNA.
DR EMBL; X98130; CAA66809.1; -; Genomic_DNA.
DR RefSeq; NP_189291.1; NM_113567.4.
DR AlphaFoldDB; Q38956; -.
DR SMR; Q38956; -.
DR IntAct; Q38956; 1.
DR STRING; 3702.AT3G26590.1; -.
DR PaxDb; Q38956; -.
DR PRIDE; Q38956; -.
DR ProteomicsDB; 224282; -.
DR EnsemblPlants; AT3G26590.1; AT3G26590.1; AT3G26590.
DR GeneID; 822267; -.
DR Gramene; AT3G26590.1; AT3G26590.1; AT3G26590.
DR KEGG; ath:AT3G26590; -.
DR Araport; AT3G26590; -.
DR TAIR; locus:2088822; AT3G26590.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR InParanoid; Q38956; -.
DR OMA; HRRCAWR; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q38956; -.
DR PRO; PR:Q38956; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38956; baseline and differential.
DR Genevisible; Q38956; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..500
FT /note="Protein DETOXIFICATION 29"
FT /id="PRO_0000434070"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 54321 MW; 1E09804384351A79 CRC64;
MAKDKDITET LLTAAEERSD LPFLSVDDIP PITTVGGFVR EFNVETKKLW YLAGPAIFTS
VNQYSLGAIT QVFAGHISTI ALAAVSVENS VVAGFSFGIM LGMGSALETL CGQAFGAGKL
SMLGVYLQRS WVILNVTALI LSLLYIFAAP ILASIGQTAA ISSAAGIFSI YMIPQIFAYA
INFPTAKFLQ SQSKIMVMAV ISAVALVIHV PLTWFVIVKL QWGMPGLAVV LNASWCFIDM
AQLVYIFSGT CGEAWSGFSW EAFHNLWSFV RLSLASAVML CLEVWYFMAI ILFAGYLKNA
EISVAALSIC MNILGWTAMI AIGMNTAVSV RVSNELGANH PRTAKFSLLV AVITSTLIGF
IVSMILLIFR DQYPSLFVKD EKVIILVKEL TPILALSIVI NNVQPVLSGV AVGAGWQAVV
AYVNIACYYV FGIPFGLLLG YKLNYGVMGI WCGMLTGTVV QTIVLTWMIC KTNWDTEASM
AEDRIREWGG EVSEIKQLIN
