MPCP_BOVIN
ID MPCP_BOVIN Reviewed; 362 AA.
AC P12234; A6QQU5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=8144629; DOI=10.1016/s0021-9258(17)34081-4;
RA Dolce V., Iacobazzi V., Palmieri F., Walker J.E.;
RT "The sequences of human and bovine genes of the phosphate carrier from
RT mitochondria contain evidence of alternatively spliced forms.";
RL J. Biol. Chem. 269:10451-10460(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=3038521; DOI=10.1002/j.1460-2075.1987.tb02377.x;
RA Runswick M.J., Powell S.J., Nyren P., Walker J.E.;
RT "Sequence of the bovine mitochondrial phosphate carrier protein: structural
RT relationship to ADP/ATP translocase and the brown fat mitochondria
RT uncoupling protein.";
RL EMBO J. 6:1367-1373(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 50-96.
RX PubMed=4066697; DOI=10.1016/s0021-9258(17)36343-3;
RA Kolbe H.V.J., Wohlrab H.;
RT "Sequence of the N-terminal formic acid fragment and location of the N-
RT ethylmaleimide-binding site of the phosphate transport protein from beef
RT heart mitochondria.";
RL J. Biol. Chem. 260:15899-15906(1985).
RN [5]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=2036364; DOI=10.1021/bi00234a018;
RA Capobianco L., Brandolin G., Palmieri F.;
RT "Transmembrane topography of the mitochondrial phosphate carrier explored
RT by peptide-specific antibodies and enzymatic digestion.";
RL Biochemistry 30:4963-4969(1991).
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).
CC -!- SUBUNIT: Interacts with PPIF; the interaction is impaired by CsA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:2036364}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:2036364}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P12234-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P12234-2; Sequence=VSP_003268;
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X77338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X05340; CAA28951.1; -; mRNA.
DR EMBL; BC149996; AAI49997.1; -; mRNA.
DR PIR; C53737; C53737.
DR PIR; D53737; D53737.
DR RefSeq; NP_777082.1; NM_174657.2. [P12234-1]
DR RefSeq; XP_005206570.1; XM_005206513.3. [P12234-2]
DR AlphaFoldDB; P12234; -.
DR SMR; P12234; -.
DR BioGRID; 159730; 1.
DR STRING; 9913.ENSBTAP00000017131; -.
DR TCDB; 2.A.29.4.1; the mitochondrial carrier (mc) family.
DR PaxDb; P12234; -.
DR PeptideAtlas; P12234; -.
DR PRIDE; P12234; -.
DR Ensembl; ENSBTAT00000017131; ENSBTAP00000017131; ENSBTAG00000012890. [P12234-1]
DR Ensembl; ENSBTAT00000053663; ENSBTAP00000048807; ENSBTAG00000012890. [P12234-2]
DR GeneID; 282477; -.
DR KEGG; bta:282477; -.
DR CTD; 5250; -.
DR VEuPathDB; HostDB:ENSBTAG00000012890; -.
DR eggNOG; KOG0767; Eukaryota.
DR GeneTree; ENSGT00390000008708; -.
DR HOGENOM; CLU_039456_3_1_1; -.
DR InParanoid; P12234; -.
DR OMA; KFFFFEY; -.
DR OrthoDB; 963446at2759; -.
DR TreeFam; TF314119; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012890; Expressed in cardiac ventricle and 105 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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; Alternative splicing; Direct protein sequencing; Membrane;
KW Methylation; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; Symport; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:4066697"
FT CHAIN 50..362
FT /note="Phosphate carrier protein, mitochondrial"
FT /id="PRO_0000019255"
FT TOPO_DOM 50..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..121
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..141
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..161
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..183
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..218
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..238
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..284
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..314
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..333
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..362
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 63..147
FT /note="Solcar 1"
FT REPEAT 160..244
FT /note="Solcar 2"
FT REPEAT 261..339
FT /note="Solcar 3"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 112
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00325"
FT MOD_RES 209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEM8"
FT VAR_SEQ 54..83
FT /note="QYSCDYGSGRFFILCGLGGIISCGTTHTAL -> YSCEYGSAKFYALCGFGG
FT VLSCGLTHTAV (in isoform B)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_003268"
SQ SEQUENCE 362 AA; 40140 MW; 500DD66867B95A10 CRC64;
MYSSVVHLAR ANPFNAPHLQ LVHDGLAGPR SDPAGPPGPP RRSRNLAAAA VEEQYSCDYG
SGRFFILCGL GGIISCGTTH TALVPLDLVK CRMQVDPQKY KSIFNGFSVT LKEDGFRGLA
KGWAPTFIGY SLQGLCKFGF YEVFKVLYSN MLGEENAYLW RTSLYLAASA SAEFFADIAL
APMEAAKVRI QTQPGYANTL RDAAPKMYKE EGLKAFYKGV APLWMRQIPY TMMKFACFER
TVEALYKFVV PKPRSECSKP EQLVVTFVAG YIAGVFCAIV SHPADSVVSV LNKEKGSSAS
EVLKRLGFRG VWKGLFARII MIGTLTALQW FIYDSVKVYF RLPRPPPPEM PESLKKKLGY
TQ