DTC_ARATH
ID DTC_ARATH Reviewed; 298 AA.
AC Q9C5M0; Q8SFL2;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial dicarboxylate/tricarboxylate transporter DTC;
DE AltName: Full=Dicarboxylate/tricarboxylate carrier;
GN Name=DTC; OrderedLocusNames=At5g19760; ORFNames=T29J13.180;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=11978797; DOI=10.1074/jbc.m202702200;
RA Picault N., Palmieri L., Pisano I., Hodges M., Palmieri F.;
RT "Identification of a novel transporter for dicarboxylates and
RT tricarboxylates in plant mitochondria. Bacterial expression,
RT reconstitution, functional characterization, and tissue distribution.";
RL J. Biol. Chem. 277:24204-24211(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12586869; DOI=10.1104/pp.009985;
RA Millar A.H., Heazlewood J.L.;
RT "Genomic and proteomic analysis of mitochondrial carrier proteins in
RT Arabidopsis.";
RL Plant Physiol. 131:443-453(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Catalyzes the transport of dicarboxylates, such as
CC oxoglutarate, oxaloacetate, malate, and succinate, and of
CC tricarboxylates, such as citrate, isocitrate, cis-aconitate, and trans-
CC aconitate by a counter-exchange mechanism across the inner
CC mitochondrial membrane. Substrate preference in reconstituted
CC proteoliposomes is oxaloacetate > malonate > malate > maleate >
CC succinate > oxoglutarate > citrate > trans-aconitate > cis-aconitate >
CC sulfate > isocitrate. May be important for plant metabolic functions
CC requiring organic acid flux to or from the mitochondria, such as
CC nitrogen assimilation, export of reducing equivalents from the
CC mitochondria, and fatty acid elongation. {ECO:0000269|PubMed:11978797}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for oxoglutarate (for the recombinant protein in
CC reconstituted proteoliposomes at pH 6.0)
CC {ECO:0000269|PubMed:11978797};
CC KM=0.36 mM for malate (for the recombinant protein in reconstituted
CC proteoliposomes at pH 6.0) {ECO:0000269|PubMed:11978797};
CC KM=0.15 mM for citrate (for the recombinant protein in reconstituted
CC proteoliposomes at pH 6.0) {ECO:0000269|PubMed:11978797};
CC Vmax=2.9 mmol/min/g enzyme toward oxoglutarate (for the recombinant
CC protein in reconstituted proteoliposomes at pH 6.0)
CC {ECO:0000269|PubMed:11978797};
CC Vmax=4.2 mmol/min/g enzyme toward malate (for the recombinant protein
CC in reconstituted proteoliposomes at pH 6.0)
CC {ECO:0000269|PubMed:11978797};
CC Vmax=1.7 mmol/min/g enzyme toward citrate (for the recombinant
CC protein in reconstituted proteoliposomes at pH 6.0)
CC {ECO:0000269|PubMed:11978797};
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:11978797};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12586869}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:12586869}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flower buds and at lower levels
CC in roots, leaves and stems. {ECO:0000269|PubMed:11978797}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AJ311780; CAC84549.1; -; mRNA.
DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92746.1; -; Genomic_DNA.
DR EMBL; AF360153; AAK25863.1; -; mRNA.
DR EMBL; AY056307; AAL07156.1; -; mRNA.
DR EMBL; AY085901; AAM63113.1; -; mRNA.
DR EMBL; AK226470; BAE98612.1; -; mRNA.
DR RefSeq; NP_197477.1; NM_121981.5.
DR AlphaFoldDB; Q9C5M0; -.
DR SMR; Q9C5M0; -.
DR BioGRID; 17372; 21.
DR IntAct; Q9C5M0; 2.
DR MINT; Q9C5M0; -.
DR STRING; 3702.AT5G19760.1; -.
DR PaxDb; Q9C5M0; -.
DR PRIDE; Q9C5M0; -.
DR ProteomicsDB; 222760; -.
DR DNASU; 832096; -.
DR EnsemblPlants; AT5G19760.1; AT5G19760.1; AT5G19760.
DR GeneID; 832096; -.
DR Gramene; AT5G19760.1; AT5G19760.1; AT5G19760.
DR KEGG; ath:AT5G19760; -.
DR Araport; AT5G19760; -.
DR TAIR; locus:2183254; AT5G19760.
DR eggNOG; KOG0759; Eukaryota.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q9C5M0; -.
DR OMA; FLHTPFM; -.
DR OrthoDB; 892773at2759; -.
DR PhylomeDB; Q9C5M0; -.
DR PRO; PR:Q9C5M0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5M0; baseline and differential.
DR Genevisible; Q9C5M0; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005310; F:dicarboxylic acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015142; F:tricarboxylic acid transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015742; P:alpha-ketoglutarate transport; IEA:GOC.
DR GO; GO:0006835; P:dicarboxylic acid transport; IDA:TAIR.
DR GO; GO:0071423; P:malate transmembrane transport; IEA:GOC.
DR GO; GO:0035674; P:tricarboxylic acid transmembrane transport; IDA:TAIR.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Mitochondrial dicarboxylate/tricarboxylate
FT transporter DTC"
FT /id="PRO_0000420761"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 12..93
FT /note="Solcar 1"
FT REPEAT 103..194
FT /note="Solcar 2"
FT REPEAT 202..292
FT /note="Solcar 3"
SQ SEQUENCE 298 AA; 31912 MW; 2609F4FE1D991628 CRC64;
MAEEKKAPIS VWTTVKPFVN GGASGMLATC VIQPIDMIKV RIQLGQGSAA SITTNMLKNE
GVGAFYKGLS AGLLRQATYT TARLGSFKLL TAKAIESNDG KPLPLYQKAL CGLTAGAIGA
CVGSPADLAL IRMQADNTLP LAQRRNYTNA FHALTRISAD EGVLALWKGC GPTVVRAMAL
NMGMLASYDQ SAEYMRDNLG FGEMSTVVGA SAVSGFCAAA CSLPFDFVKT QIQKMQPDAQ
GKYPYTGSLD CAMKTLKEGG PLKFYSGFPV YCVRIAPHVM MTWIFLNQIT KFQKKIGM
