ID   MPCP_PONAB              Reviewed;         361 AA.
AC   Q5R7W2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
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; Synonyms=PHC;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transport of phosphate groups from the cytosol to the
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 {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; CR859997; CAH92148.1; -; mRNA.
DR   RefSeq; NP_001126257.1; NM_001132785.1.
DR   AlphaFoldDB; Q5R7W2; -.
DR   SMR; Q5R7W2; -.
DR   STRING; 9601.ENSPPYP00000005541; -.
DR   GeneID; 100173229; -.
DR   KEGG; pon:100173229; -.
DR   CTD; 5250; -.
DR   eggNOG; KOG0767; Eukaryota.
DR   InParanoid; Q5R7W2; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Membrane; Methylation; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Symport; Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..49
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           50..361
FT                   /note="Phosphate carrier protein, mitochondrial"
FT                   /id="PRO_0000294072"
FT   TOPO_DOM        50..62
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..85
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..120
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..140
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..160
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..182
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..217
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..237
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..260
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..283
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..313
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..332
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..361
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REPEAT          62..146
FT                   /note="Solcar 1"
FT   REPEAT          159..243
FT                   /note="Solcar 2"
FT   REPEAT          260..338
FT                   /note="Solcar 3"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00325"
FT   MOD_RES         111
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00325"
FT   MOD_RES         195
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00325"
FT   MOD_RES         208
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VEM8"
SQ   SEQUENCE   361 AA;  40072 MW;  E94ECF3032688460 CRC64;
     MFSSVAHLAR ANPFNTPHLQ LVHDGLGDFR SRPPGPTGQP RRPRNLAAAA VEEYSCEFGS
     AKYYALCGFG GVLSCGLTHT AVVPLDLVKC RMQVDPQKYK GIFNGFSVTL KEDGVRGLAK
     GWAPTFLGYS MQGLCKFGFY EVFKVLYSNM LGEENTYLWR TSLYLAASAS AEFFADIALA
     PMEAAKVRIQ TQPGYANTLR DAAPKMYKEE GLKAFYKGVA PLWMRQIPYT MMKFACFERT
     VEALYKFVVP KPRSECSKPE QLVVTFVAGY IAGVFCAIVS HPADSVVSVL NKEKGSSASL
     VLKRLGFKGV WKGLFARIIM IGTLTALQWF IYDSVKVYFR LPRPPPPEMP ESLKKKLGLT
     Q