MPCP_MOUSE
ID MPCP_MOUSE Reviewed; 357 AA.
AC Q8VEM8; Q542V7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphate carrier protein, mitochondrial;
DE AltName: Full=Phosphate transport protein;
DE Short=PTP;
DE AltName: Full=Solute carrier family 25 member 3;
DE Flags: Precursor;
GN Name=Slc25a3;
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;
RC TISSUE=Amnion, Bone marrow, Ovary, Thymus, and Uterus;
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 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 [3]
RP PROTEIN SEQUENCE OF 88-94; 97-107; 117-156; 185-196; 202-242; 291-300 AND
RP 337-350, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, 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: Transport of phosphate groups from the cytosol to
CC mitochondrial matrix. Phosphate is cotransported with H(+). May play a
CC role regulation of the mitochondrial permeability transition pore
CC (mPTP) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPIF; the interaction is impaired by CsA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK077274; BAC36723.1; -; mRNA.
DR EMBL; AK077723; BAC36982.1; -; mRNA.
DR EMBL; AK088013; BAC40095.1; -; mRNA.
DR EMBL; AK150641; BAE29729.1; -; mRNA.
DR EMBL; AK150729; BAE29806.1; -; mRNA.
DR EMBL; AK150870; BAE29921.1; -; mRNA.
DR EMBL; AK151518; BAE30467.1; -; mRNA.
DR EMBL; AK152006; BAE30870.1; -; mRNA.
DR EMBL; AK152292; BAE31101.1; -; mRNA.
DR EMBL; AK152341; BAE31137.1; -; mRNA.
DR EMBL; AK167197; BAE39327.1; -; mRNA.
DR EMBL; AK168580; BAE40449.1; -; mRNA.
DR EMBL; BC018161; AAH18161.1; -; mRNA.
DR CCDS; CCDS24121.1; -.
DR RefSeq; NP_598429.1; NM_133668.3.
DR AlphaFoldDB; Q8VEM8; -.
DR SMR; Q8VEM8; -.
DR BioGRID; 202142; 31.
DR DIP; DIP-32038N; -.
DR IntAct; Q8VEM8; 13.
DR MINT; Q8VEM8; -.
DR STRING; 10090.ENSMUSP00000075987; -.
DR TCDB; 2.A.29.4.5; the mitochondrial carrier (mc) family.
DR iPTMnet; Q8VEM8; -.
DR PhosphoSitePlus; Q8VEM8; -.
DR SwissPalm; Q8VEM8; -.
DR EPD; Q8VEM8; -.
DR jPOST; Q8VEM8; -.
DR MaxQB; Q8VEM8; -.
DR PaxDb; Q8VEM8; -.
DR PeptideAtlas; Q8VEM8; -.
DR PRIDE; Q8VEM8; -.
DR ProteomicsDB; 291435; -.
DR TopDownProteomics; Q8VEM8; -.
DR Antibodypedia; 30219; 57 antibodies from 17 providers.
DR DNASU; 18674; -.
DR Ensembl; ENSMUST00000076694; ENSMUSP00000075987; ENSMUSG00000061904.
DR Ensembl; ENSMUST00000164505; ENSMUSP00000132480; ENSMUSG00000061904.
DR GeneID; 18674; -.
DR KEGG; mmu:18674; -.
DR UCSC; uc007gtn.1; mouse.
DR CTD; 5250; -.
DR MGI; MGI:1353498; Slc25a3.
DR VEuPathDB; HostDB:ENSMUSG00000061904; -.
DR eggNOG; KOG0767; Eukaryota.
DR GeneTree; ENSGT00390000008708; -.
DR HOGENOM; CLU_039456_3_1_1; -.
DR InParanoid; Q8VEM8; -.
DR OMA; KFFFFEY; -.
DR PhylomeDB; Q8VEM8; -.
DR TreeFam; TF314119; -.
DR BioGRID-ORCS; 18674; 23 hits in 57 CRISPR screens.
DR ChiTaRS; Slc25a3; mouse.
DR PRO; PR:Q8VEM8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VEM8; protein.
DR Bgee; ENSMUSG00000061904; Expressed in hindlimb stylopod muscle and 219 other tissues.
DR ExpressionAtlas; Q8VEM8; baseline and differential.
DR Genevisible; Q8VEM8; 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:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR044677; Pic2/Mir1-like.
DR PANTHER; PTHR45671; PTHR45671; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Methylation;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; Symport; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 46..357
FT /note="Phosphate carrier protein, mitochondrial"
FT /id="PRO_0000019257"
FT TOPO_DOM 46..58
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..116
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..136
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..156
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..178
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..213
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..233
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..256
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..279
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..309
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..357
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 58..142
FT /note="Solcar 1"
FT REPEAT 155..239
FT /note="Solcar 2"
FT REPEAT 256..334
FT /note="Solcar 3"
FT MOD_RES 94
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 107
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 191
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
SQ SEQUENCE 357 AA; 39632 MW; 2887B9ADF034339E CRC64;
MFSSVAHLAR ANPFNAPHLQ LVHDGLSGPR SPPAPPRRSR HLAAAAVEEY SCEFGSMKYY
ALCGFGGVLS CGLTHTAVVP LDLVKCRMQV DPQKYKGIFN GFSITLKEDG VRGLAKGWAP
TLIGYSMQGL CKFGFYEVFK ALYSNILGEE NTYLWRTSLY LASSASAEFF ADIALAPMEA
AKVRIQTQPG YANTLREAVP KMYKEEGLNA FYKGVAPLWM RQIPYTMMKF ACFERTVEAL
YKFVVPKPRS ECTKAEQLVV TFVAGYIAGV FCAIVSHPAD SVVSVLNKEK GSTASQVLQR
LGFRGVWKGL FARIIMIGTL TALQWFIYDS VKVYFRLPRP PPPEMPESLK KKLGLTE
