DIC_RAT
ID DIC_RAT Reviewed; 286 AA.
AC O89035;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitochondrial dicarboxylate carrier {ECO:0000303|PubMed:8985166};
DE Short=DIC;
DE AltName: Full=Solute carrier family 25 member 10;
GN Name=Slc25a10 {ECO:0000312|EMBL:AAH81734.1, ECO:0000312|RGD:621430};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:CAA11278.1};
RX PubMed=8985166; DOI=10.1016/s0014-5793(96)01350-6;
RA Palmieri L., Palmieri F., Runswick M.J., Walker J.E.;
RT "Identification by bacterial expression and functional reconstitution of
RT the yeast genomic sequence encoding the mitochondrial dicarboxylate carrier
RT protein.";
RL FEBS Lett. 399:299-302(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND TRANSPORT
RP ACTIVITY.
RC TISSUE=Liver {ECO:0000312|EMBL:CAA11278.1};
RX PubMed=9733776; DOI=10.1074/jbc.273.38.24754;
RA Fiermonte G., Palmieri L., Dolce V., Lasorsa F.M., Palmieri F.,
RA Runswick M.J., Walker J.E.;
RT "The sequence, bacterial expression, and functional reconstitution of the
RT rat mitochondrial dicarboxylate transporter cloned via distant homologs in
RT yeast and Caenorhabditis elegans.";
RL J. Biol. Chem. 273:24754-24759(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH81734.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15632090; DOI=10.1101/gr.2889405;
RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA Istrail S., Li P., Sutton G.;
RT "Gene and alternative splicing annotation with AIR.";
RL Genome Res. 15:54-66(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDM06845.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=29211846; DOI=10.1093/hmg/ddx419;
RA Punzi G., Porcelli V., Ruggiu M., Hossain M.F., Menga A., Scarcia P.,
RA Castegna A., Gorgoglione R., Pierri C.L., Laera L., Lasorsa F.M.,
RA Paradies E., Pisano I., Marobbio C.M.T., Lamantea E., Ghezzi D.,
RA Tiranti V., Giannattasio S., Donati M.A., Guerrini R., Palmieri L.,
RA Palmieri F., De Grassi A.;
RT "SLC25A10 biallelic mutations in intractable epileptic encephalopathy with
RT complex I deficiency.";
RL Hum. Mol. Genet. 27:499-504(2018).
RN [8]
RP FUNCTION, TRANSPORT ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=3355813; DOI=10.1016/0005-2728(88)90030-8;
RA Bisaccia F., Indiveri C., Palmieri F.;
RT "Purification and reconstitution of two anion carriers from rat liver
RT mitochondria: the dicarboxylate and the 2-oxoglutarate carrier.";
RL Biochim. Biophys. Acta 933:229-240(1988).
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:3355813, PubMed:9733776,
CC PubMed:29211846). Plays an important role in gluconeogenesis, fatty
CC acid metabolism, urea synthesis, and sulfur metabolism, particularly in
CC liver, by supplying the substrates for the different metabolic
CC processes (PubMed:9733776). Regulates fatty acid release from
CC adipocytes, and contributes to systemic insulin sensitivity (By
CC similarity). {ECO:0000250|UniProtKB:Q9QZD8,
CC ECO:0000269|PubMed:29211846, ECO:0000269|PubMed:3355813,
CC ECO:0000269|PubMed:9733776}.
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:0000269|PubMed:29211846,
CC ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813,
CC ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813,
CC ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813,
CC ECO:0000269|PubMed:9733776};
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:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776};
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:0000250|UniProtKB:Q9QZD8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:3355813}; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed most strongly in liver, then kidney, and
CC at lower levels in heart and brain. {ECO:0000269|PubMed:9733776}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; BC081734; AAH81734.1; -; mRNA.
DR EMBL; AJ223355; CAA11278.1; -; mRNA.
DR EMBL; CH473948; EDM06845.1; -; Genomic_DNA.
DR RefSeq; NP_596909.1; NM_133418.1.
DR SMR; O89035; -.
DR IntAct; O89035; 2.
DR STRING; 10116.ENSRNOP00000051846; -.
DR TCDB; 2.A.29.2.2; the mitochondrial carrier (mc) family.
DR PRIDE; O89035; -.
DR Ensembl; ENSRNOT00000054963.3; ENSRNOP00000051846.1; ENSRNOG00000036693.3.
DR GeneID; 170943; -.
DR KEGG; rno:170943; -.
DR CTD; 1468; -.
DR RGD; 621430; Slc25a10.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000156783; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR OMA; FGAYEVG; -.
DR OrthoDB; 984118at2759; -.
DR TreeFam; TF312920; -.
DR Reactome; R-RNO-1614517; Sulfide oxidation to sulfate.
DR Reactome; R-RNO-428643; Organic anion transporters.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000036693; Expressed in kidney and 20 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0015297; F:antiporter activity; IDA:RGD.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015291; F:secondary active transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
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; IDA:RGD.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015744; P:succinate transport; IDA:RGD.
DR GO; GO:0008272; P:sulfate transport; IDA:RGD.
DR GO; GO:0015709; P:thiosulfate transport; IDA:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Antiport; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Mitochondrial dicarboxylate carrier"
FT /id="PRO_0000456253"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 100..187
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 196..279
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZD8"
SQ SEQUENCE 286 AA; 31455 MW; 5013459FAD08DBDC CRC64;
MAEARTSRWY FGGLASCGAA CCTHPLDLLK VHLQTQQEVK LRMTGMALQV VRTDGFLALY
NGLSASLCRQ MTYSLTRFAI YETMRDYMTK DSQGPLPFYS KVLLGGISGL TGGFVGTPAD
LVNVRMQNDM KLPLSQRRNY SHALDGLYRV AREEGLKKLF SGATMASSRG ALVTVGQLSC
YDQAKQLVLS TGYLSDNIFT HFLSSFIAGG CATFLCQPLD VLKTRLMNSK GEYQGVFHCA
VETAKLGPQA FFKGLVPAGV RLVPHTVLTF MFLEQLRKHF GIKVAT
