ID   S25A3_MOUSE             Reviewed;         357 AA.
AC   Q8VEM8; Q542V7;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Solute carrier family 25 member 3 {ECO:0000303|PubMed:29237729};
DE   AltName: Full=Phosphate carrier protein, mitochondrial {ECO:0000250|UniProtKB:Q00325};
DE   AltName: Full=Phosphate transport protein;
DE            Short=PTP;
DE   Flags: Precursor;
GN   Name=Slc25a3 {ECO:0000303|PubMed:29237729,
GN   ECO:0000312|MGI:MGI:1353498};
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,
RC   Pancreas, 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).
RN   [7]
RP   FUNCTION.
RX   PubMed=29237729; DOI=10.1074/jbc.ra117.000265;
RA   Boulet A., Vest K.E., Maynard M.K., Gammon M.G., Russell A.C.,
RA   Mathews A.T., Cole S.E., Zhu X., Phillips C.B., Kwong J.Q., Dodani S.C.,
RA   Leary S.C., Cobine P.A.;
RT   "The mammalian phosphate carrier SLC25A3 is a mitochondrial copper
RT   transporter required for cytochrome c oxidase biogenesis.";
RL   J. Biol. Chem. 293:1887-1896(2018).
CC   -!- FUNCTION: Inorganic ion transporter that transports phosphate or copper
CC       ions across the mitochondrial inner membrane into the matrix
CC       compartment (By similarity). Mediates proton-coupled symport of
CC       phosphate ions necessary for mitochondrial oxidative phosphorylation of
CC       ADP to ATP (By similarity). Transports copper ions probably in the form
CC       of anionic copper(I) complexes to maintain mitochondrial matrix copper
CC       pool and to supply copper for cytochrome C oxidase complex assembly
CC       (PubMed:29237729). May also play a role in regulation of the
CC       mitochondrial permeability transition pore (mPTP) (By similarity).
CC       {ECO:0000250|UniProtKB:P12234, ECO:0000250|UniProtKB:P16036,
CC       ECO:0000250|UniProtKB:Q00325, ECO:0000269|PubMed:29237729}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out);
CC         Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000250|UniProtKB:P12234};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29941;
CC         Evidence={ECO:0000250|UniProtKB:P12234};
CC   -!- SUBUNIT: Interacts with PPIF; the interaction is impaired by CsA.
CC       {ECO:0000250|UniProtKB:P16036}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P12234}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P12234}.
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; 33.
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   GlyGen; Q8VEM8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8VEM8; -.
DR   PhosphoSitePlus; Q8VEM8; -.
DR   SwissPalm; Q8VEM8; -.
DR   EPD; Q8VEM8; -.
DR   jPOST; Q8VEM8; -.
DR   MaxQB; Q8VEM8; -.
DR   PaxDb; 10090-ENSMUSP00000075987; -.
DR   PeptideAtlas; Q8VEM8; -.
DR   ProteomicsDB; 291435; -.
DR   Pumba; Q8VEM8; -.
DR   TopDownProteomics; Q8VEM8; -.
DR   Antibodypedia; 30219; 87 antibodies from 17 providers.
DR   DNASU; 18674; -.
DR   Ensembl; ENSMUST00000076694.13; ENSMUSP00000075987.7; ENSMUSG00000061904.13.
DR   Ensembl; ENSMUST00000164505.2; ENSMUSP00000132480.2; ENSMUSG00000061904.13.
DR   GeneID; 18674; -.
DR   KEGG; mmu:18674; -.
DR   UCSC; uc007gtn.1; mouse.
DR   AGR; MGI:1353498; -.
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   OrthoDB; 5472853at2759; -.
DR   PhylomeDB; Q8VEM8; -.
DR   TreeFam; TF314119; -.
DR   BioGRID-ORCS; 18674; 23 hits in 60 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 222 other cell types or tissues.
DR   ExpressionAtlas; Q8VEM8; baseline and differential.
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:0015317; F:phosphate:proton symporter activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; Mitochondrial carrier domain; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR044677; SLC25A3/Pic2/Mir1-like.
DR   PANTHER; PTHR45671:SF10; PHOSPHATE CARRIER PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45671; SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER PHOSPHATE CARRIER), MEMBER 3, LIKE-RELATED-RELATED; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   Genevisible; Q8VEM8; MM.
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="Solute carrier family 25 member 3"
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
//