DTX44_ARATH
ID DTX44_ARATH Reviewed; 521 AA.
AC Q84K71; O80918;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein DETOXIFICATION 44, chloroplastic {ECO:0000303|PubMed:11739388};
DE Short=AtDTX44 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 44 {ECO:0000305};
DE Short=MATE protein 44 {ECO:0000305};
DE Flags: Precursor;
GN Name=DTX44 {ECO:0000303|PubMed:11739388};
GN OrderedLocusNames=At2g38330 {ECO:0000312|Araport:AT2G38330};
GN ORFNames=T19C21.18 {ECO:0000312|EMBL:AAC28771.1};
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=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).
RN [6]
RP INDUCTION BY ALUMINUM, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT families function independently to confer Arabidopsis aluminum tolerance.";
RL Plant J. 57:389-399(2009).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots. {ECO:0000269|PubMed:18826429}.
CC -!- INDUCTION: Not induced by aluminum. {ECO:0000269|PubMed:18826429}.
CC -!- DISRUPTION PHENOTYPE: No reduction in aluminum tolerance.
CC {ECO:0000269|PubMed:18826429}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28771.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004683; AAC28771.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09524.1; -; Genomic_DNA.
DR EMBL; BT004001; AAO42040.1; -; mRNA.
DR EMBL; BT005521; AAO63941.1; -; mRNA.
DR PIR; T02512; T02512.
DR RefSeq; NP_181367.2; NM_129389.3.
DR AlphaFoldDB; Q84K71; -.
DR SMR; Q84K71; -.
DR BioGRID; 3755; 35.
DR IntAct; Q84K71; 35.
DR STRING; 3702.AT2G38330.1; -.
DR TCDB; 2.A.66.1.54; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; Q84K71; -.
DR PRIDE; Q84K71; -.
DR ProteomicsDB; 221883; -.
DR EnsemblPlants; AT2G38330.1; AT2G38330.1; AT2G38330.
DR GeneID; 818413; -.
DR Gramene; AT2G38330.1; AT2G38330.1; AT2G38330.
DR KEGG; ath:AT2G38330; -.
DR Araport; AT2G38330; -.
DR TAIR; locus:2057135; AT2G38330.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_16_2_1; -.
DR InParanoid; Q84K71; -.
DR OMA; FINTQGF; -.
DR OrthoDB; 1474417at2759; -.
DR PhylomeDB; Q84K71; -.
DR PRO; PR:Q84K71; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84K71; baseline and differential.
DR Genevisible; Q84K71; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR CDD; cd13136; MATE_DinF_like; 1.
DR InterPro; IPR044644; DinF-like.
DR InterPro; IPR002528; MATE_fam.
DR PANTHER; PTHR42893; PTHR42893; 1.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..521
FT /note="Protein DETOXIFICATION 44, chloroplastic"
FT /id="PRO_0000405273"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 12..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 54910 MW; 1461B32201721184 CRC64;
MAAVATSFCF SPHRSPSRFG NPNSSIRRTI VCKSSPRDES PAVSTSSQRP EKQQNPLTSQ
NKPDHDHKPD PGIGKIGMEI MSIALPAALA LAADPITSLV DTAFVGHIGS AELAAVGVSV
SVFNLVSKLF NVPLLNVTTS FVAEEQAIAA KDDNDSIETS KKVLPSVSTS LVLAAGVGIA
EAIALSLGSD FLMDVMAIPF DSPMRIPAEQ FLRLRAYGAP PIVVALAAQG AFRGFKDTTT
PLYAVVAGNV LNAVLDPILI FVLGFGISGA AAATVISEYL IAFILLWKLN ENVVLLSPQI
KVGRANQYLK SGGLLIGRTV ALLVPFTLAT SLAAQNGPTQ MAGHQIVLEI WLAVSLLTDA
LAIAAQSLLA TTYSQGEYKQ AREVLFGVLQ VGLATGTGLA AVLFITFEPF SSLFTTDSEV
LKIALSGTLF VAGSQPVNAL AFVLDGLYYG VSDFGFAAYS MVIVGFISSL FMLVAAPTFG
LAGIWTGLFL FMALRLVAGA WRLGTRTGPW KMLWSAPEKP E
