MPCP2_ARATH
ID MPCP2_ARATH Reviewed; 363 AA.
AC Q9M2Z8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mitochondrial phosphate carrier protein 2, mitochondrial;
DE AltName: Full=Mitochondrial phosphate transporter 2;
DE Short=MPT2;
DE AltName: Full=Phosphate transporter 3;2;
DE Flags: Precursor;
GN Name=MPT2; Synonyms=AT3, PHT3;2; OrderedLocusNames=At3g48850;
GN ORFNames=T21J18_120;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 [MRNA].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. Strong expression in senescent
CC leaves. {ECO:0000269|PubMed:22937061}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:22937061}.
CC -!- MISCELLANEOUS: Plants overexpressing MPT2/PHT3;2 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL132963; CAB87913.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78463.1; -; Genomic_DNA.
DR EMBL; BT033111; ACF20466.1; -; mRNA.
DR PIR; T49281; T49281.
DR RefSeq; NP_190454.1; NM_114744.4.
DR AlphaFoldDB; Q9M2Z8; -.
DR SMR; Q9M2Z8; -.
DR BioGRID; 9364; 18.
DR STRING; 3702.AT3G48850.1; -.
DR PaxDb; Q9M2Z8; -.
DR PRIDE; Q9M2Z8; -.
DR ProteomicsDB; 238898; -.
DR EnsemblPlants; AT3G48850.1; AT3G48850.1; AT3G48850.
DR GeneID; 824046; -.
DR Gramene; AT3G48850.1; AT3G48850.1; AT3G48850.
DR KEGG; ath:AT3G48850; -.
DR Araport; AT3G48850; -.
DR TAIR; locus:2099413; AT3G48850.
DR eggNOG; KOG0767; Eukaryota.
DR HOGENOM; CLU_039456_0_1_1; -.
DR InParanoid; Q9M2Z8; -.
DR OMA; YKTGVFL; -.
DR OrthoDB; 963446at2759; -.
DR PhylomeDB; Q9M2Z8; -.
DR PRO; PR:Q9M2Z8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Z8; baseline and differential.
DR Genevisible; Q9M2Z8; AT.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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 GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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; 2.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript 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 ?..363
FT /note="Mitochondrial phosphate carrier protein 2,
FT mitochondrial"
FT /id="PRO_0000421696"
FT TOPO_DOM ?..64
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..123
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..143
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..164
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..220
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..240
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..321
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..363
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 65..149
FT /note="Solcar 1"
FT REPEAT 162..246
FT /note="Solcar 2"
FT REPEAT 263..342
FT /note="Solcar 3"
SQ SEQUENCE 363 AA; 39024 MW; 00F667B502112D02 CRC64;
MSDSSRSLIP SFLYSSDHRL FQATTMSTHL KSQPLISPTN SSVSSNGTSF AIATPNEKVE
MYSPAYFAAC TVAGMLSCGI THTAITPLDV IKCNMQIDPL KYKNITSAFK TTIKEQGLKG
FTRGWSPTLL GYSAQGAFKY GLYEYAKKYY SDIVGPEYAA KYKTLIYLAG SASAEIVADV
ALCPMEAVKV RVQTQPGFAR GLSDGLPKII KSEGFRGLHK GLVPLWGRQI PYTMMKFATF
ENTVELIYKK VMPTPKEECS KPVQLGVSFA GGYIAGIFCA IISHPADNLV SFLNNSKGAT
VADAVKRLGL WGMLTRGLPL RIFMIGTLTG AQWVIYDAVK VLAGLPTTGG ASPATALAPS
VSA
