MPCP_RAT
ID MPCP_RAT Reviewed; 356 AA.
AC P16036;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 151.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-62.
RC TISSUE=Liver;
RX PubMed=2670944; DOI=10.1016/s0021-9258(19)84878-0;
RA Ferreira G.C., Pratt R.D., Pedersen P.L.;
RT "Energy-linked anion transport. Cloning, sequencing, and characterization
RT of a full length cDNA encoding the rat liver mitochondrial proton/phosphate
RT symporter.";
RL J. Biol. Chem. 264:15628-15633(1989).
RN [2]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=2250020; DOI=10.1016/s0021-9258(17)45346-4;
RA Ferreira G.C., Pratt R.D., Pedersen P.L.;
RT "Mitochondrial proton/phosphate transporter. An antibody directed against
RT the COOH terminus and proteolytic cleavage experiments provides new
RT insights about its membrane topology.";
RL J. Biol. Chem. 265:21202-21206(1990).
RN [3]
RP TRANSIT PEPTIDE CLEAVAGE SITE.
RX PubMed=1985946; DOI=10.1016/s0021-9258(17)35312-7;
RA Pratt R.D., Ferreira G.C., Pedersen P.L.;
RT "Mitochondrial phosphate transport. Import of the H+/Pi symporter and role
RT of the presequence.";
RL J. Biol. Chem. 266:1276-1280(1991).
RN [4]
RP FUNCTION, AND INTERACTION WITH PPIF.
RX PubMed=18667415; DOI=10.1074/jbc.m805235200;
RA Leung A.W., Varanyuwatana P., Halestrap A.P.;
RT "The mitochondrial phosphate carrier interacts with cyclophilin D and may
RT play a key role in the permeability transition.";
RL J. Biol. Chem. 283:26312-26323(2008).
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). {ECO:0000269|PubMed:18667415}.
CC -!- SUBUNIT: Interacts with PPIF; the interaction is impaired by CsA.
CC {ECO:0000269|PubMed:18667415}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:2250020}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:2250020}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; M23984; AAA41634.1; -; mRNA.
DR PIR; A34350; A34350.
DR AlphaFoldDB; P16036; -.
DR SMR; P16036; -.
DR CORUM; P16036; -.
DR IntAct; P16036; 4.
DR MINT; P16036; -.
DR STRING; 10116.ENSRNOP00000011494; -.
DR iPTMnet; P16036; -.
DR PhosphoSitePlus; P16036; -.
DR SwissPalm; P16036; -.
DR jPOST; P16036; -.
DR PaxDb; P16036; -.
DR PRIDE; P16036; -.
DR UCSC; RGD:70986; rat.
DR RGD; 70986; Slc25a3.
DR eggNOG; KOG0767; Eukaryota.
DR InParanoid; P16036; -.
DR PRO; PR:P16036; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015317; F:phosphate:proton symporter activity; NAS:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
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..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1985946,
FT ECO:0000269|PubMed:2670944"
FT CHAIN 45..356
FT /note="Phosphate carrier protein, mitochondrial"
FT /id="PRO_0000019258"
FT TOPO_DOM 45..57
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..115
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..155
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..212
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..232
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..255
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..278
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..308
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..327
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..356
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 57..141
FT /note="Solcar 1"
FT REPEAT 154..238
FT /note="Solcar 2"
FT REPEAT 255..333
FT /note="Solcar 3"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 106
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEM8"
SQ SEQUENCE 356 AA; 39445 MW; 64AF5FD9DD671DBE CRC64;
MFSSVAHLAR ANPFNAPHLQ LVHDVSGPRS PPGPPRRSRH LAAAAVEGYS CEFGSMKYYA
LCGFGGVLSC GLTHTAVVPL DLVKCRMQVD PQKYKGIFNG FSITLKEDGV RGLAKGWAPT
LIGYSMQGLC KFGFYEVFKA LYSNILGEEN TYLWRTSLYL AASASAEFFA DIALAPMEAA
KVRIQTQPGY ANTLREAVPK MYKEEGLNAF YKGVAPVWMR QIPYTMMKFA CFERTVEALY
KFVVPKPRSE CTKAEQLVVT FVAGYIAGVF CAIVSHPADS VVSVLNKEKG STASQVLQRL
GFRGVWKGLF ARIIMIGTLT ALQWFIYDSV KVYFRLPRPP PPEMPESLKK KLGLTE
