DIC_MOUSE
ID DIC_MOUSE Reviewed; 287 AA.
AC Q9QZD8; Q543J6; Q99LJ9; Q9D8G8;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Mitochondrial dicarboxylate carrier {ECO:0000303|PubMed:10567211};
DE Short=DIC;
DE AltName: Full=Solute carrier family 25 member 10;
GN Name=Slc25a10 {ECO:0000303|PubMed:16027120, ECO:0000303|PubMed:30943427};
GN Synonyms=Dic;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10567211; DOI=10.1042/bj3440313;
RA Das K., Lewis R.Y., Combatsiaris T.P., Lin Y., Shapiro L., Charron M.J.,
RA Scherer P.E.;
RT "Predominant expression of the mitochondrial dicarboxylate carrier in white
RT adipose tissue.";
RL Biochem. J. 344:313-320(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Liver, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=16027120; DOI=10.1074/jbc.m503152200;
RA Mizuarai S., Miki S., Araki H., Takahashi K., Kotani H.;
RT "Identification of dicarboxylate carrier Slc25a10 as malate transporter in
RT de novo fatty acid synthesis.";
RL J. Biol. Chem. 280:32434-32441(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=30943427; DOI=10.1016/j.bbamcr.2019.03.016;
RA Cai T., Hua B., Luo D., Xu L., Cheng Q., Yuan G., Yan Z., Sun N., Hua L.,
RA Lu C.;
RT "The circadian protein CLOCK regulates cell metabolism via the
RT mitochondrial carrier SLC25A10.";
RL Biochim. Biophys. Acta 1866:1310-1321(2019).
RN [8]
RP FUNCTION, TRANSPORT ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=33746082; DOI=10.1016/j.jhep.2021.03.006;
RA An Y.A., Chen S., Deng Y., Wang Z.V., Funcke J.B., Shah M., Shan B.,
RA Gordillo R., Yoshino J., Klein S., Kusminski C.M., Scherer P.E.;
RT "The mitochondrial dicarboxylate carrier prevents hepatic lipotoxicity by
RT inhibiting white adipocyte lipolysis.";
RL J. Hepatol. 75:387-399(2021).
CC -!- FUNCTION: Catalyzes the electroneutral exchange or flux of
CC physiologically important metabolites such as dicarboxylates (malonate,
CC malate, succinate), inorganic sulfur-containing anions, and phosphate,
CC across mitochondrial inner membrane (PubMed:33746082). Plays an
CC important role in gluconeogenesis, fatty acid metabolism, urea
CC synthesis, and sulfur metabolism, particularly in liver, by supplying
CC the substrates for the different metabolic processes (PubMed:33746082,
CC PubMed:16027120, PubMed:30943427). Regulates fatty acid release from
CC adipocytes, and contributes to systemic insulin sensitivity
CC (PubMed:33746082). {ECO:0000269|PubMed:16027120,
CC ECO:0000269|PubMed:30943427, ECO:0000269|PubMed:33746082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + phosphate(out) = (S)-malate(out) +
CC phosphate(in); Xref=Rhea:RHEA:71607, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + malonate(out) = (S)-malate(out) +
CC malonate(in); Xref=Rhea:RHEA:71611, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:15792; Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) +
CC succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in);
CC Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189;
CC Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonate(out) + phosphate(in) = malonate(in) + phosphate(out);
CC Xref=Rhea:RHEA:71623, ChEBI:CHEBI:15792, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) + succinate(out) = phosphate(out) +
CC succinate(in); Xref=Rhea:RHEA:71627, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in);
CC Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000250|UniProtKB:O89035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonate(out) + succinate(in) = malonate(in) + succinate(out);
CC Xref=Rhea:RHEA:71667, ChEBI:CHEBI:15792, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000269|PubMed:33746082};
CC -!- ACTIVITY REGULATION: Regulated by circadian protein CLOCK (Circadian
CC Locomotor Output Cycles Kaput). {ECO:0000269|PubMed:30943427}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:10567211}; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at very high levels in white adipose
CC tissue (PubMed:10567211, PubMed:33746082). And at low levels in brown
CC adipose tissue, kidney and liver (PubMed:10567211).
CC {ECO:0000269|PubMed:10567211, ECO:0000269|PubMed:33746082}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AF188712; AAF03412.1; -; mRNA.
DR EMBL; AK008038; BAB25425.1; -; mRNA.
DR EMBL; AK050282; BAC34165.1; -; mRNA.
DR EMBL; AK151645; BAE30575.1; -; mRNA.
DR EMBL; BC003222; AAH03222.1; -; mRNA.
DR CCDS; CCDS25738.1; -.
DR RefSeq; NP_038798.2; NM_013770.2.
DR AlphaFoldDB; Q9QZD8; -.
DR SMR; Q9QZD8; -.
DR BioGRID; 205183; 10.
DR IntAct; Q9QZD8; 1.
DR STRING; 10090.ENSMUSP00000026899; -.
DR iPTMnet; Q9QZD8; -.
DR PhosphoSitePlus; Q9QZD8; -.
DR SwissPalm; Q9QZD8; -.
DR EPD; Q9QZD8; -.
DR jPOST; Q9QZD8; -.
DR MaxQB; Q9QZD8; -.
DR PaxDb; Q9QZD8; -.
DR PeptideAtlas; Q9QZD8; -.
DR PRIDE; Q9QZD8; -.
DR ProteomicsDB; 279867; -.
DR DNASU; 27376; -.
DR Ensembl; ENSMUST00000026899; ENSMUSP00000026899; ENSMUSG00000025792.
DR GeneID; 27376; -.
DR KEGG; mmu:27376; -.
DR UCSC; uc007mtb.2; mouse.
DR CTD; 1468; -.
DR MGI; MGI:1353497; Slc25a10.
DR VEuPathDB; HostDB:ENSMUSG00000025792; -.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000156783; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q9QZD8; -.
DR OMA; FGAYEVG; -.
DR OrthoDB; 984118at2759; -.
DR PhylomeDB; Q9QZD8; -.
DR TreeFam; TF312920; -.
DR Reactome; R-MMU-1614517; Sulfide oxidation to sulfate.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR BioGRID-ORCS; 27376; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc25a10; mouse.
DR PRO; PR:Q9QZD8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QZD8; protein.
DR Bgee; ENSMUSG00000025792; Expressed in right kidney and 249 other tissues.
DR Genevisible; Q9QZD8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0015297; F:antiporter activity; ISO:MGI.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015291; F:secondary active transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015743; P:malate transport; ISO:MGI.
DR GO; GO:0006839; P:mitochondrial transport; ISO:MGI.
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:0006817; P:phosphate ion transport; ISO:MGI.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015744; P:succinate transport; ISO:MGI.
DR GO; GO:0008272; P:sulfate transport; ISO:MGI.
DR GO; GO:0015709; P:thiosulfate transport; ISO:MGI.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002030; Mit_uncoupling_UCP-like.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00784; MTUNCOUPLING.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Antiport; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..287
FT /note="Mitochondrial dicarboxylate carrier"
FT /id="PRO_0000090610"
FT TRANSMEM 9..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 7..87
FT /note="Solcar 1"
FT REPEAT 100..187
FT /note="Solcar 2"
FT REPEAT 196..279
FT /note="Solcar 3"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 6
FT /note="A -> T (in Ref. 1; AAF03412)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="M -> L (in Ref. 1; AAF03412)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="F -> L (in Ref. 2; BAB25425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 31715 MW; E351D1CE18E5B568 CRC64;
MAEARASRWY FGGLASCGAA CCTHPLDLLK VHLQTQQEVK LRMTGMALQV VRTDGFLALY
NGLSASLCRQ MTYSLTRFAI YETMRDYMTK DSQGPLPFYN KVLLGGISGL TGGFVGTPAD
LVNVRMQNDM KLPPSQRRNY SHALDGLYRV AREESLRKLF SGATMASSRG ALVTVGQLSC
YDQAKQLVLS TGYLSDNIFT HFVSSFIAGG CATFLCQPLD VLKTRLMNSK GEYQGVFHCA
METAKLGPQA FFKGLFPAGI RLIPHTVLTF MFLEQLRKHF GIKVPTT
