TXTP_MOUSE
ID TXTP_MOUSE Reviewed; 311 AA.
AC Q8JZU2; Q3TDH6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tricarboxylate transport protein, mitochondrial {ECO:0000250|UniProtKB:P53007};
DE AltName: Full=Citrate transport protein {ECO:0000250|UniProtKB:P53007};
DE Short=CTP {ECO:0000250|UniProtKB:P53007};
DE AltName: Full=Solute carrier family 25 member 1 {ECO:0000312|MGI:MGI:1345283};
DE AltName: Full=Tricarboxylate carrier protein {ECO:0000250|UniProtKB:P53007};
DE Flags: Precursor;
GN Name=Slc25a1 {ECO:0000312|MGI:MGI:1345283};
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 {ECO:0000312|EMBL:AAH37087.1};
RN [1] {ECO:0000312|EMBL:BAE34965.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34965.1};
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 [2] {ECO:0000312|Ensembl:ENSMUSP00000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000003622};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDK97495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4] {ECO:0000312|EMBL:AAH37087.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH37087.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH37087.1};
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 [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18775783; DOI=10.1016/j.mcn.2008.07.027;
RA Maynard T.M., Meechan D.W., Dudevoir M.L., Gopalakrishna D., Peters A.Z.,
RA Heindel C.C., Sugimoto T.J., Wu Y., Lieberman J.A., Lamantia A.S.;
RT "Mitochondrial localization and function of a subset of 22q11 deletion
RT syndrome candidate genes.";
RL Mol. Cell. Neurosci. 39:439-451(2008).
RN [6]
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).
CC -!- FUNCTION: Citrate transporter that mediates the exchange of
CC mitochondrial citrate for cytosolic malate. Also able to mediate the
CC exchange of citrate for isocitrate, phosphoenolpyruvate, cis- but not
CC trans-aconitate and to a lesser extend maleate and succinate. Important
CC for the bioenergetics of hepatic cells as it provides a carbon source
CC for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic
CC pathway. Required for proper neuromuscular junction formation.
CC {ECO:0000250|UniProtKB:P53007}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18775783}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed minimally but ubiquitously throughout the
CC adult brain. Detected at higher levels in the olfactory bulb, neocortex
CC and cerebellum. Also expressed in a subset of large cells in the globus
CC pallidus. {ECO:0000269|PubMed:18775783}.
CC -!- DEVELOPMENTAL STAGE: Expression reaches a maximum between 16 dpc and P0
CC and then declines in adulthood. {ECO:0000269|PubMed:18775783}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000255|RuleBase:RU000488}.
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DR EMBL; AK159289; BAE34965.1; -; mRNA.
DR EMBL; AK170191; BAE41625.1; -; mRNA.
DR EMBL; AC078895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97495.1; -; Genomic_DNA.
DR EMBL; BC037087; AAH37087.1; -; mRNA.
DR CCDS; CCDS28014.1; -.
DR RefSeq; NP_694790.1; NM_153150.2.
DR AlphaFoldDB; Q8JZU2; -.
DR SMR; Q8JZU2; -.
DR BioGRID; 199216; 4.
DR IntAct; Q8JZU2; 2.
DR MINT; Q8JZU2; -.
DR STRING; 10090.ENSMUSP00000003622; -.
DR iPTMnet; Q8JZU2; -.
DR PhosphoSitePlus; Q8JZU2; -.
DR SwissPalm; Q8JZU2; -.
DR EPD; Q8JZU2; -.
DR jPOST; Q8JZU2; -.
DR MaxQB; Q8JZU2; -.
DR PaxDb; Q8JZU2; -.
DR PeptideAtlas; Q8JZU2; -.
DR PRIDE; Q8JZU2; -.
DR ProteomicsDB; 298046; -.
DR Antibodypedia; 22859; 155 antibodies from 23 providers.
DR DNASU; 13358; -.
DR Ensembl; ENSMUST00000003622; ENSMUSP00000003622; ENSMUSG00000003528.
DR GeneID; 13358; -.
DR KEGG; mmu:13358; -.
DR UCSC; uc007ymp.2; mouse.
DR CTD; 6576; -.
DR MGI; MGI:1345283; Slc25a1.
DR VEuPathDB; HostDB:ENSMUSG00000003528; -.
DR eggNOG; KOG0756; Eukaryota.
DR GeneTree; ENSGT00550000074856; -.
DR HOGENOM; CLU_015166_5_1_1; -.
DR InParanoid; Q8JZU2; -.
DR OMA; CPAFIVG; -.
DR OrthoDB; 1523221at2759; -.
DR PhylomeDB; Q8JZU2; -.
DR TreeFam; TF105786; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR BioGRID-ORCS; 13358; 14 hits in 74 CRISPR screens.
DR PRO; PR:Q8JZU2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8JZU2; protein.
DR Bgee; ENSMUSG00000003528; Expressed in epididymal fat pad and 254 other tissues.
DR ExpressionAtlas; Q8JZU2; baseline and differential.
DR Genevisible; Q8JZU2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0071913; F:citrate secondary active transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006843; P:mitochondrial citrate transmembrane transport; IBA:GO_Central.
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; Phosphoprotein;
KW Reference proteome; Repeat; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P32089"
FT CHAIN 14..311
FT /note="Tricarboxylate transport protein, mitochondrial"
FT /id="PRO_0000430571"
FT TRANSMEM 29..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 23..111
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 122..208
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 218..303
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53007"
FT CONFLICT 78
FT /note="H -> Y (in Ref. 1; BAE41625)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> D (in Ref. 1; BAE41625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 33931 MW; E7910B52F006991D CRC64;
MAAPRGPRAL SAAAPGSGKP KLTHPGKAIL AGGLAGGIEI CITFPTEYVK TQLQLDERAN
PPRYRGIGDC VRQTVRSHGV LGLYRGLSSL LYGSIPKAAV RFGMFEFLSN HMRDAQGRLD
SRRGLLCGLG AGVAEAVVVV CPMETIKVKF IHDQTSSNPK YRGFFHGVRE IIREQGLKGT
YQGLTATVLK QGSNQAIRFF VMTSLRNWYQ GDNHNKPMNP LITGVFGATA GAASVFGNTP
LDVIKTRMQG LEAHKYRNTL DCGLKILKNE GPKAFYKGTV PRLGRVCLDV AIVFIIYDEV
VKLLNKVWKT D
