DIC1_YEAST
ID DIC1_YEAST Reviewed; 298 AA.
AC Q06143; D6VYY7; P87332;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitochondrial dicarboxylate transporter;
DE AltName: Full=DTP;
DE AltName: Full=Dicarboxylate carrier 1;
GN Name=DIC1; OrderedLocusNames=YLR348C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9020177; DOI=10.1074/jbc.272.7.4516;
RA Kakhniashvili D., Mayor J.A., Gremse D.A., Xu Y., Kaplan R.S.;
RT "Identification of a novel gene encoding the yeast mitochondrial
RT dicarboxylate transport protein via overexpression, purification, and
RT characterization of its protein product.";
RL J. Biol. Chem. 272:4516-4521(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=8831951; DOI=10.1016/0300-9084(96)89505-8;
RA Lancar-Benba J., Foucher B., Saint-Macary M.;
RT "Characterization, purification and properties of the yeast mitochondrial
RT dicarboxylate carrier (Saccharomyces cerevisiae).";
RL Biochimie 78:195-200(1996).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9559855; DOI=10.1023/a:1022426900735;
RA Mayor J.A., Kakhniashvili D., Gremse D.A., Campbell C., Kramer R.,
RA Schroers A., Kaplan R.S.;
RT "Bacterial overexpression of putative yeast mitochondrial transport
RT proteins.";
RL J. Bioenerg. Biomembr. 29:541-547(1997).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10027973; DOI=10.1046/j.1365-2958.1999.01197.x;
RA Palmieri L., Vozza A., Hoenlinger A., Dietmeier K., Palmisano A., Zara V.,
RA Palmieri F.;
RT "The mitochondrial dicarboxylate carrier is essential for the growth of
RT Saccharomyces cerevisiae on ethanol or acetate as the sole carbon source.";
RL Mol. Microbiol. 31:569-577(1999).
RN [7]
RP TRANSLOCATION ACROSS THE MITOCHONDRIAL OUTER MEMBRANE.
RX PubMed=11502005; DOI=10.1006/jmbi.2001.4833;
RA Zara V., Palmisano I., Rassow J., Palmieri F.;
RT "Biogenesis of the dicarboxylate carrier (DIC): translocation across the
RT mitochondrial outer membrane and subsequent release from the TOM channel
RT are membrane potential-independent.";
RL J. Mol. Biol. 310:965-971(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [11]
RP DOMAIN, AND TRANSLOCATION ACROSS THE MITOCHONDRIAL OUTER MEMBRANE.
RX PubMed=15591051; DOI=10.1074/jbc.m412269200;
RA Brandner K., Rehling P., Truscott K.N.;
RT "The carboxyl-terminal third of the dicarboxylate carrier is crucial for
RT productive association with the inner membrane twin-pore translocase.";
RL J. Biol. Chem. 280:6215-6221(2005).
CC -!- FUNCTION: Mitochondrial dicarboxylic transporter catalyzing the
CC exchange of dicarboxylic acids like malate and succinate for inorganic
CC phosphate. Required for growth on ethanol and acetate.
CC {ECO:0000269|PubMed:10027973, ECO:0000269|PubMed:8831951,
CC ECO:0000269|PubMed:9020177, ECO:0000269|PubMed:9559855}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.55 mM for malonate {ECO:0000269|PubMed:10027973,
CC ECO:0000269|PubMed:9020177, ECO:0000269|PubMed:9559855};
CC Vmax=3 umol/min/mg enzyme {ECO:0000269|PubMed:10027973,
CC ECO:0000269|PubMed:9020177, ECO:0000269|PubMed:9559855};
CC -!- SUBUNIT: Homodimer. Binds to the TIM22 translocation complex during
CC import. {ECO:0000269|PubMed:10027973}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10027973, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10027973, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- DOMAIN: The C-terminal Solcar repeat is required for association with
CC the TIM22 translocation complex during import.
CC {ECO:0000269|PubMed:15591051}.
CC -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; U79459; AAB71336.1; -; Genomic_DNA.
DR EMBL; U19028; AAB67266.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09653.1; -; Genomic_DNA.
DR PIR; S51351; S51351.
DR RefSeq; NP_013452.1; NM_001182237.1.
DR AlphaFoldDB; Q06143; -.
DR SMR; Q06143; -.
DR BioGRID; 31611; 118.
DR DIP; DIP-8816N; -.
DR IntAct; Q06143; 1.
DR STRING; 4932.YLR348C; -.
DR TCDB; 2.A.29.2.3; the mitochondrial carrier (mc) family.
DR MaxQB; Q06143; -.
DR PaxDb; Q06143; -.
DR PRIDE; Q06143; -.
DR EnsemblFungi; YLR348C_mRNA; YLR348C; YLR348C.
DR GeneID; 851063; -.
DR KEGG; sce:YLR348C; -.
DR SGD; S000004340; DIC1.
DR VEuPathDB; FungiDB:YLR348C; -.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000156783; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q06143; -.
DR OMA; QLRPVKY; -.
DR BioCyc; YEAST:G3O-32424-MON; -.
DR Reactome; R-SCE-1614517; Sulfide oxidation to sulfate.
DR Reactome; R-SCE-428643; Organic anion transporters.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; Q06143; -.
DR PRO; PR:Q06143; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06143; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0005310; F:dicarboxylic acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006835; P:dicarboxylic acid transport; IDA:SGD.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphate transport; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Mitochondrial dicarboxylate transporter"
FT /id="PRO_0000233005"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 11..95
FT /note="Solcar 1"
FT REPEAT 103..195
FT /note="Solcar 2"
FT REPEAT 205..289
FT /note="Solcar 3"
SQ SEQUENCE 298 AA; 32992 MW; C66A1F963450453D CRC64;
MSTNAKESAG KNIKYPWWYG GAAGIFATMV THPLDLAKVR LQAAPMPKPT LFRMLESILA
NEGVVGLYSG LSAAVLRQCT YTTVRFGAYD LLKENVIPRE QLTNMAYLLP CSMFSGAIGG
LAGNFADVVN IRMQNDSALE AAKRRNYKNA IDGVYKIYRY EGGLKTLFTG WKPNMVRGIL
MTASQVVTYD VFKNYLVTKL DFDASKNYTH LTASLLAGLV ATTVCSPADV MKTRIMNGSG
DHQPALKILA DAVRKEGPSF MFRGWLPSFT RLGPFTMLIF FAIEQLKKHR VGMPKEDK
