DTX31_ARATH
ID DTX31_ARATH Reviewed; 522 AA.
AC Q9LPV4; Q0WSV3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein DETOXIFICATION 31 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX31 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 31 {ECO:0000305};
DE Short=MATE protein 31 {ECO:0000305};
DE AltName: Full=Protein ROOT HAIR SPECIFIC 2 {ECO:0000303|PubMed:19448035};
GN Name=DTX31 {ECO:0000303|PubMed:11739388};
GN Synonyms=RHS2 {ECO:0000303|PubMed:19448035};
GN OrderedLocusNames=At1g12950 {ECO:0000312|Araport:AT1G12950};
GN ORFNames=F13K23.21 {ECO:0000312|EMBL:AAF78500.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19448035; DOI=10.1104/pp.109.140905;
RA Won S.-K., Lee Y.-J., Lee H.-Y., Heo Y.-K., Cho M., Cho H.-T.;
RT "Cis-element- and transcriptome-based screening of root hair-specific genes
RT and their functional characterization in Arabidopsis.";
RL Plant Physiol. 150:1459-1473(2009).
CC -!- FUNCTION: Positively mediates root hair elongation.
CC {ECO:0000269|PubMed:19448035}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Short root hairs. {ECO:0000269|PubMed:19448035}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
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DR EMBL; AC012187; AAF78500.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28953.1; -; Genomic_DNA.
DR EMBL; BT023437; AAY56428.1; -; mRNA.
DR EMBL; AK227815; BAE99795.1; -; mRNA.
DR PIR; D86263; D86263.
DR RefSeq; NP_172755.1; NM_101166.4.
DR AlphaFoldDB; Q9LPV4; -.
DR SMR; Q9LPV4; -.
DR IntAct; Q9LPV4; 2.
DR STRING; 3702.AT1G12950.1; -.
DR PaxDb; Q9LPV4; -.
DR PRIDE; Q9LPV4; -.
DR ProMEX; Q9LPV4; -.
DR ProteomicsDB; 222183; -.
DR EnsemblPlants; AT1G12950.1; AT1G12950.1; AT1G12950.
DR GeneID; 837853; -.
DR Gramene; AT1G12950.1; AT1G12950.1; AT1G12950.
DR KEGG; ath:AT1G12950; -.
DR Araport; AT1G12950; -.
DR TAIR; locus:2010401; AT1G12950.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_4_1; -.
DR InParanoid; Q9LPV4; -.
DR OMA; NTLESFC; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; Q9LPV4; -.
DR PRO; PR:Q9LPV4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPV4; baseline and differential.
DR Genevisible; Q9LPV4; 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:0005774; C:vacuolar 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:0048767; P:root hair elongation; IMP:UniProtKB.
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..522
FT /note="Protein DETOXIFICATION 31"
FT /id="PRO_0000434072"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 290
FT /note="G -> R (in Ref. 4; BAE99795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 56906 MW; ED67895AAFB651AE CRC64;
MEKDNDFKDP FLASTEEEEL DPATQKALME YLGVGSRASS LVSFSSTAVD IPPISGVGDF
VREFRIESRK LWKLAGPAIF TTMSQYSLGA VTQVFAGHIS TLALAAVSIE NSVIAGFSFG
IMLGMGSALE TLCGQAFGAG KVSMLGVYLQ RSWVILSVTA LFLSLIYIFA APILTFIGQT
AAISAMAGIF SIYMIPQIFA YAINFPTAKF LQSQSKIMVM AGISGVVLVI HSFFTWLVMS
RLHWGLPGLA LVLNTSWWVI VVAQLVYIFN CTCGEAWSGF TWEAFHNLWG FVKLSLASAA
MLCLEIWYFM ALVLFAGYLK NAEVSVAALS ICMNILGWAA MVAFGTNAAV SVRVSNELGA
SHPRTAKFSL VVAVILSTAI GMFIAAGLLF FRNEYPVLFV EDEEVRNVVR ELTPMLAFCI
VINNVQPVLS GVAVGAGWQA VVAYVNIACY YLFGVPFGLL LGFKLEYGVM GIWWGMVTGT
FVQSIVLTWM ICKTNWEKEA SMAEERIKEW GGVPAEKETL LN
