MPC1_MOUSE
ID MPC1_MOUSE Reviewed; 109 AA.
AC P63030; Q9D6C0; Q9JLG5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Mitochondrial pyruvate carrier 1;
DE AltName: Full=Brain protein 44-like protein;
GN Name=Mpc1; Synonyms=Brp44l;
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].
RC TISSUE=Testis;
RX PubMed=11252172; DOI=10.1007/s003350010259;
RA Trachtulec Z., Forejt J.;
RT "Synteny of orthologous genes conserved in mammals, snake, fly, nematode,
RT and fission yeast.";
RL Mamm. Genome 12:227-231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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].
RC STRAIN=FVB/N; TISSUE=Colon;
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 PROTEIN SEQUENCE OF 47-54 AND 98-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22628554; DOI=10.1126/science.1218530;
RA Herzig S., Raemy E., Montessuit S., Veuthey J.L., Zamboni N.,
RA Westermann B., Kunji E.R., Martinou J.C.;
RT "Identification and functional expression of the mitochondrial pyruvate
RT carrier.";
RL Science 337:93-96(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72, 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).
CC -!- FUNCTION: Mediates the uptake of pyruvate into mitochondria.
CC {ECO:0000269|PubMed:22628554}.
CC -!- SUBUNIT: The functional 150 kDa pyruvate import complex is a heteromer
CC of MPC1 and MPC2. {ECO:0000269|PubMed:22628554}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:22628554}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22628554}.
CC -!- SIMILARITY: Belongs to the mitochondrial pyruvate carrier (MPC) (TC
CC 2.A.105) family. {ECO:0000305}.
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DR EMBL; AF181116; AAF25816.1; -; mRNA.
DR EMBL; AK002241; BAB21958.1; -; mRNA.
DR EMBL; AK002266; BAB21976.1; -; mRNA.
DR EMBL; AK004013; BAB23124.1; -; mRNA.
DR EMBL; AK013391; BAB28826.1; -; mRNA.
DR EMBL; AK014421; BAB29340.1; -; mRNA.
DR EMBL; BC024365; AAH24365.1; -; mRNA.
DR CCDS; CCDS49944.1; -.
DR RefSeq; NP_061289.1; NM_018819.4.
DR AlphaFoldDB; P63030; -.
DR SMR; P63030; -.
DR BioGRID; 207746; 2.
DR STRING; 10090.ENSMUSP00000119443; -.
DR GuidetoPHARMACOLOGY; 3022; -.
DR iPTMnet; P63030; -.
DR PhosphoSitePlus; P63030; -.
DR SwissPalm; P63030; -.
DR jPOST; P63030; -.
DR PaxDb; P63030; -.
DR PeptideAtlas; P63030; -.
DR PRIDE; P63030; -.
DR ProteomicsDB; 291434; -.
DR Antibodypedia; 49022; 146 antibodies from 25 providers.
DR DNASU; 55951; -.
DR Ensembl; ENSMUST00000046754; ENSMUSP00000045654; ENSMUSG00000023861.
DR Ensembl; ENSMUST00000155364; ENSMUSP00000119443; ENSMUSG00000023861.
DR GeneID; 55951; -.
DR KEGG; mmu:55951; -.
DR UCSC; uc033hao.1; mouse.
DR CTD; 51660; -.
DR MGI; MGI:1915240; Mpc1.
DR VEuPathDB; HostDB:ENSMUSG00000023861; -.
DR eggNOG; KOG1590; Eukaryota.
DR GeneTree; ENSGT00510000046988; -.
DR InParanoid; P63030; -.
DR OMA; CTTHFWG; -.
DR OrthoDB; 1584711at2759; -.
DR PhylomeDB; P63030; -.
DR TreeFam; TF314444; -.
DR BioGRID-ORCS; 55951; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Mpc1; mouse.
DR PRO; PR:P63030; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P63030; protein.
DR Bgee; ENSMUSG00000023861; Expressed in proximal tubule and 96 other tissues.
DR ExpressionAtlas; P63030; baseline and differential.
DR Genevisible; P63030; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; IGI:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IMP:MGI.
DR GO; GO:0006850; P:mitochondrial pyruvate transmembrane transport; IGI:MGI.
DR InterPro; IPR005336; MPC.
DR Pfam; PF03650; MPC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q3ZCG2"
FT CHAIN 2..109
FT /note="Mitochondrial pyruvate carrier 1"
FT /id="PRO_0000212798"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZCG2"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 64
FT /note="L -> Q (in Ref. 2; BAB29340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12455 MW; E0536878BAA68124 CRC64;
MAGALVRKAA DYVRSKDFRD YLMSTHFWGP VANWGLPIAA INDMKKSPEI ISGRMTFALC
CYSLTFMRFA YKVQPRNWLL FACHVTNEVA QLIQGGRLIN YEMSKRPSA
