DTX56_ARATH
ID DTX56_ARATH Reviewed; 491 AA.
AC O49660;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein DETOXIFICATION 56 {ECO:0000303|PubMed:11739388};
DE Short=AtDTX56 {ECO:0000303|PubMed:11739388};
DE AltName: Full=Multidrug and toxic compound extrusion protein 56 {ECO:0000305};
DE Short=MATE protein 56 {ECO:0000305};
DE AltName: Full=Protein RESISTANT TO HIGH CARBON DIOXIDE 1 {ECO:0000303|PubMed:25599916};
GN Name=DTX56 {ECO:0000303|PubMed:11739388};
GN Synonyms=RHC1 {ECO:0000303|PubMed:25599916};
GN OrderedLocusNames=At4g22790 {ECO:0000312|Araport:AT4G22790};
GN ORFNames=T12H17.180 {ECO:0000312|EMBL:CAA16564.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH BCA4 AND HT1.
RX PubMed=25599916; DOI=10.1038/ncomms7057;
RA Tian W., Hou C., Ren Z., Pan Y., Jia J., Zhang H., Bai F., Zhang P.,
RA Zhu H., He Y., Luo S., Li L., Luan S.;
RT "A molecular pathway for CO(2) response in Arabidopsis guard cells.";
RL Nat. Commun. 6:6057-6057(2015).
CC -!- FUNCTION: Could function as a HCO(3)(-) -sensing component in the CO(2)
CC signaling pathway in guard cells. Acts as an upsteam repressor of HT1.
CC Plays a role in stomatal response to CO(2).
CC {ECO:0000269|PubMed:25599916}.
CC -!- SUBUNIT: Interacts with BCA4 and HT1. {ECO:0000269|PubMed:25599916}.
CC -!- INTERACTION:
CC O49660; Q94CE4: BCA4; NbExp=2; IntAct=EBI-11174814, EBI-4430840;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25599916};
CC Multi-pass membrane protein {ECO:0000269|PubMed:25599916}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in guard cells.
CC {ECO:0000269|PubMed:25599916}.
CC -!- DISRUPTION PHENOTYPE: Defective in stomatal responses to Co(2). Showed
CC more rapid leaf expansion under high CO(2) condition as compared with
CC the wild type. {ECO:0000269|PubMed:25599916}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL021635; CAA16564.1; -; Genomic_DNA.
DR EMBL; AL161558; CAB79234.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84658.1; -; Genomic_DNA.
DR EMBL; BT002796; AAO22621.1; -; mRNA.
DR PIR; T04574; T04574.
DR RefSeq; NP_194010.1; NM_118408.2.
DR AlphaFoldDB; O49660; -.
DR SMR; O49660; -.
DR IntAct; O49660; 3.
DR STRING; 3702.AT4G22790.1; -.
DR PaxDb; O49660; -.
DR PRIDE; O49660; -.
DR ProteomicsDB; 220725; -.
DR EnsemblPlants; AT4G22790.1; AT4G22790.1; AT4G22790.
DR GeneID; 828378; -.
DR Gramene; AT4G22790.1; AT4G22790.1; AT4G22790.
DR KEGG; ath:AT4G22790; -.
DR Araport; AT4G22790; -.
DR TAIR; locus:2132619; AT4G22790.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_0_1; -.
DR InParanoid; O49660; -.
DR OMA; CGAMEPV; -.
DR OrthoDB; 743037at2759; -.
DR PhylomeDB; O49660; -.
DR PRO; PR:O49660; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49660; baseline and differential.
DR Genevisible; O49660; 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:0005886; C:plasma membrane; IDA:TAIR.
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:0071244; P:cellular response to carbon dioxide; IMP:TAIR.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP: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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="Protein DETOXIFICATION 56"
FT /id="PRO_0000434090"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 491 AA; 53702 MW; C8B91B9AF0F5BAA5 CRC64;
MSETSKSESL DPEVSEGLCS KTLMQSIVHE LKLQMRIGLP LVVMNLLWFG KMTTTSVFLG
RQGELNLAGG SLGFSFANVT GFSVLYGISA AMEPICGQAF GAKNFKLLHK TLFMAVLLLL
LISVPISFLW LNVHKILTGF GQREDISFIA KKYLLYLLPE LPILSFLCPL KAYLSSQGVT
LPIMFTTAAA TSLHIPINIV LSKARGIEGV AMAVWITDFI VVILLTGYVI VVERMKENKW
KQGGWLNQSA QDWLTLIKLS GPCCLTVCLE WWCYEILVLL TGRLPNPVQA VSILIIVFNF
DYLLYAVMLS LGTCVATRVS NELGANNPKG AYRAAYTTLI VGIISGCIGA LVMIAFRGFW
GSLYTHHDQL ILNGVKKMML IMAVIEVVNF PLMVCGEIVR GTAKPSLGMY ANLSGFYLLA
LPLGATLAFK AKQGLQGFLI GLFVGISLCL SILLIFIARI DWEKEAGKAQ ILTCNTEDEQ
TSQGSGQDSH S
