ID TPC_MOUSE Reviewed; 318 AA.
AC Q9DAM5; A2A9V6; Q3T9C4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 159.
DE RecName: Full=Mitochondrial thiamine pyrophosphate carrier;
DE AltName: Full=Solute carrier family 25 member 19;
GN Name=Slc25a19;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Kidney;
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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND MUTAGENESIS OF GLY-177.
RX PubMed=17035501; DOI=10.1073/pnas.0607661103;
RA Lindhurst M.J., Fiermonte G., Song S., Struys E., De Leonardis F.,
RA Schwartzberg P.L., Chen A., Castegna A., Verhoeven N., Mathews C.K.,
RA Palmieri F., Biesecker L.G.;
RT "Knockout of Slc25a19 causes mitochondrial thiamine pyrophosphate
RT depletion, embryonic lethality, CNS malformations, and anemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15927-15932(2006).
CC -!- FUNCTION: Mitochondrial transporter mediating uptake of thiamine
CC diphosphate into mitochondria. It is not clear if the antiporter
CC activity is affected by the membrane potential or by the proton
CC electrochemical gradient. {ECO:0000250|UniProtKB:Q9HC21}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiamine diphosphate(in) + thiamine phosphate(out) = thiamine
CC diphosphate(out) + thiamine phosphate(in); Xref=Rhea:RHEA:73383,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q9HC21};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9HC21}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are embryonically lethal, with
CC death occurring on or before day 11 of the embryo development. Knockout
CC of Slc25a19 causes mitochondrial thiamine pyrophosphate depletion,
CC embryonic lethality, CNS malformations and anemia.
CC {ECO:0000269|PubMed:17035501}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Previously identified as the mitochondrial deoxyribonucleotide
CC carrier. However other experiments later demonstrated that SLC25A19 is
CC a thiamine diphosphate transporter and not a mitochondrial
CC deoxyribonucleotide carrier. {ECO:0000250|UniProtKB:Q9HC21}.
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DR EMBL; AK005710; BAB24199.1; -; mRNA.
DR EMBL; AK172622; BAE43100.1; -; mRNA.
DR EMBL; AL645470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018167; AAH18167.1; -; mRNA.
DR CCDS; CCDS25644.1; -.
DR RefSeq; NP_001239313.1; NM_001252384.1.
DR RefSeq; NP_001239324.1; NM_001252395.1.
DR RefSeq; NP_080347.1; NM_026071.3.
DR RefSeq; XP_006534042.1; XM_006533979.3.
DR RefSeq; XP_017170203.1; XM_017314714.1.
DR AlphaFoldDB; Q9DAM5; -.
DR SMR; Q9DAM5; -.
DR BioGRID; 212072; 1.
DR STRING; 10090.ENSMUSP00000137534; -.
DR PhosphoSitePlus; Q9DAM5; -.
DR EPD; Q9DAM5; -.
DR MaxQB; Q9DAM5; -.
DR PaxDb; 10090-ENSMUSP00000021089; -.
DR ProteomicsDB; 258828; -.
DR Pumba; Q9DAM5; -.
DR Antibodypedia; 46024; 134 antibodies from 18 providers.
DR DNASU; 67283; -.
DR Ensembl; ENSMUST00000021089.11; ENSMUSP00000021089.5; ENSMUSG00000020744.14.
DR Ensembl; ENSMUST00000178003.8; ENSMUSP00000137534.2; ENSMUSG00000020744.14.
DR GeneID; 67283; -.
DR KEGG; mmu:67283; -.
DR UCSC; uc007mig.2; mouse.
DR AGR; MGI:1914533; -.
DR CTD; 60386; -.
DR MGI; MGI:1914533; Slc25a19.
DR VEuPathDB; HostDB:ENSMUSG00000020744; -.
DR eggNOG; KOG0752; Eukaryota.
DR GeneTree; ENSGT00550000074902; -.
DR HOGENOM; CLU_015166_10_3_1; -.
DR InParanoid; Q9DAM5; -.
DR OMA; MYVCYGA; -.
DR OrthoDB; 261981at2759; -.
DR PhylomeDB; Q9DAM5; -.
DR TreeFam; TF313047; -.
DR Reactome; R-MMU-196819; Vitamin B1 (thiamin) metabolism.
DR BioGRID-ORCS; 67283; 19 hits in 78 CRISPR screens.
DR ChiTaRS; Slc25a19; mouse.
DR PRO; PR:Q9DAM5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DAM5; Protein.
DR Bgee; ENSMUSG00000020744; Expressed in retinal neural layer and 230 other cell types or tissues.
DR ExpressionAtlas; Q9DAM5; baseline and differential.
DR Genevisible; Q9DAM5; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:MGI.
DR GO; GO:0030974; P:thiamine pyrophosphate transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR24089:SF59; MITOCHONDRIAL THIAMINE PYROPHOSPHATE CARRIER; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Antiport; Membrane; Mitochondrion; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..318
FT /note="Mitochondrial thiamine pyrophosphate carrier"
FT /id="PRO_0000090613"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 13..106
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 116..202
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 214..309
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT MOTIF 241..246
FT /note="Substrate recognition"
FT /evidence="ECO:0000250"
SQ SEQUENCE 318 AA; 35618 MW; 006DC5B11FA12A5B CRC64;
MVGYDAKADV RSNSKLEVAV AGSVSGFVTR ALISPLDVIK IRFQLQIERL CPSDPNAKYH
GIFQAAKQIL QEEGPRAFWK GHVPAQILSI GYGAVQFLAF EELTELLYQA NLYQTHQFSA
HFVCGGLSAG TATLTVHPVD VLRTRLAAQG EPKIYNNLRE AIRTMYKTEG PFVFYKGLTP
TVIAIFPYAG LQFSCYRSLK RAYDWLIPPD GKQTGNLKNL LCGCGSGVIS KTFTYPLDLI
KKRLQVGGFE HARSAFGQVR SYRGLLDLTQ QVLQEEGTRG FFKGLSPSLM KAALSTGFMF
FWYELFCNLF HCIRREDR
//
