ID   MPCP3_ARATH             Reviewed;         375 AA.
AC   Q9FMU6; O80415; Q56WI0;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Mitochondrial phosphate carrier protein 3, mitochondrial;
DE   AltName: Full=Mitochondrial phosphate transporter 3;
DE            Short=MPT3;
DE   AltName: Full=Phosphate transporter 3;1;
DE   Flags: Precursor;
GN   Name=MPT3; Synonyms=AT5, PHT3;1; OrderedLocusNames=At5g14040;
GN   ORFNames=MUA22_4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 88-375.
RC   STRAIN=cv. Columbia;
RX   PubMed=10437831; DOI=10.1023/a:1006285009435;
RA   Takabatake R., Hata S., Taniguchi M., Kouchi H., Sugiyama T., Izui K.;
RT   "Isolation and characterization of cDNAs encoding mitochondrial phosphate
RT   transporters in soybean, maize, rice, and Arabidopis.";
RL   Plant Mol. Biol. 40:479-486(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-375.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=14756774; DOI=10.1046/j.1365-2958.2003.03810.x;
RA   Hamel P., Saint-Georges Y., de Pinto B., Lachacinski N., Altamura N.,
RA   Dujardin G.;
RT   "Redundancy in the function of mitochondrial phosphate transport in
RT   Saccharomyces cerevisiae and Arabidopsis thaliana.";
RL   Mol. Microbiol. 51:307-317(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA   Picault N., Hodges M., Palmieri L., Palmieri F.;
RT   "The growing family of mitochondrial carriers in Arabidopsis.";
RL   Trends Plant Sci. 9:138-146(2004).
RN   [9]
RP   GENE FAMILY, TISSUE SPECIFICITY, INDUCTION BY SALT, AND FUNCTION.
RX   PubMed=22937061; DOI=10.1371/journal.pone.0043530;
RA   Zhu W., Miao Q., Sun D., Yang G., Wu C., Huang J., Zheng C.;
RT   "The mitochondrial phosphate transporters modulate plant responses to salt
RT   stress via affecting ATP and gibberellin metabolism in Arabidopsis
RT   thaliana.";
RL   PLoS ONE 7:E43530-E43530(2012).
CC   -!- FUNCTION: Transport of phosphate groups from the cytosol to the
CC       mitochondrial matrix. Mediates salt stress tolerance through an ATP-
CC       dependent pathway and via modulation of the gibberellin metabolism.
CC       {ECO:0000269|PubMed:14756774, ECO:0000269|PubMed:22937061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14671022}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14671022}.
CC   -!- TISSUE SPECIFICITY: Expressed in stems, leaves and flowers. Strong
CC       expression in vascular tissues. {ECO:0000269|PubMed:22937061}.
CC   -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:22937061}.
CC   -!- MISCELLANEOUS: Plants overexpressing MPT3/PHT3;1 display increased
CC       sensitivity to salt stress. {ECO:0000305|PubMed:22937061}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD94852.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB007650; BAB08283.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91980.1; -; Genomic_DNA.
DR   EMBL; AY058848; AAL24236.1; -; mRNA.
DR   EMBL; AY143869; AAN28808.1; -; mRNA.
DR   EMBL; AB016066; BAA31585.1; -; mRNA.
DR   EMBL; AK222060; BAD94852.1; ALT_INIT; mRNA.
DR   PIR; T51595; T51595.
DR   RefSeq; NP_196908.1; NM_121407.3.
DR   AlphaFoldDB; Q9FMU6; -.
DR   SMR; Q9FMU6; -.
DR   BioGRID; 16530; 24.
DR   IntAct; Q9FMU6; 1.
DR   MINT; Q9FMU6; -.
DR   STRING; 3702.Q9FMU6; -.
DR   TCDB; 2.A.29.4.6; the mitochondrial carrier (mc) family.
DR   PaxDb; 3702-AT5G14040-1; -.
DR   ProteomicsDB; 239065; -.
DR   EnsemblPlants; AT5G14040.1; AT5G14040.1; AT5G14040.
DR   GeneID; 831252; -.
DR   Gramene; AT5G14040.1; AT5G14040.1; AT5G14040.
DR   KEGG; ath:AT5G14040; -.
DR   Araport; AT5G14040; -.
DR   TAIR; AT5G14040; PHT3.
DR   eggNOG; KOG0767; Eukaryota.
DR   HOGENOM; CLU_039456_0_1_1; -.
DR   InParanoid; Q9FMU6; -.
DR   OMA; VNTMSAN; -.
DR   OrthoDB; 5472853at2759; -.
DR   PhylomeDB; Q9FMU6; -.
DR   BRENDA; 7.3.2.1; 399.
DR   PRO; PR:Q9FMU6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMU6; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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; 2.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   Genevisible; Q9FMU6; AT.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..375
FT                   /note="Mitochondrial phosphate carrier protein 3,
FT                   mitochondrial"
FT                   /id="PRO_0000421697"
FT   TOPO_DOM        ?..75
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..134
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..154
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..175
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..231
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..251
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..272
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..332
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..375
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REPEAT          76..160
FT                   /note="Solcar 1"
FT   REPEAT          173..257
FT                   /note="Solcar 2"
FT   REPEAT          274..353
FT                   /note="Solcar 3"
SQ   SEQUENCE   375 AA;  40090 MW;  C58B3057954C9CF6 CRC64;
     MESPKNSLIP SFLYSSSSSP RSFLLDQVLN SNSNAAFEKS PSPAPRSSPT SMISRKNFLI
     ASPTEPGKGI EMYSPAFYAA CTFGGILSCG LTHMTVTPLD LVKCNMQIDP AKYKSISSGF
     GILLKEQGVK GFFRGWVPTL LGYSAQGACK FGFYEYFKKT YSDLAGPEYT AKYKTLIYLA
     GSASAEIIAD IALCPFEAVK VRVQTQPGFA RGMSDGFPKF IKSEGYGGLY KGLAPLWGRQ
     IPYTMMKFAS FETIVEMIYK YAIPNPKSEC SKGLQLGVSF AGGYVAGVFC AIVSHPADNL
     VSFLNNAKGA TVGDAVKKIG MVGLFTRGLP LRIVMIGTLT GAQWGLYDAF KVFVGLPTTG
     GVAPAPAIAA TEAKA
//