ID   MME1_YEAST              Reviewed;         368 AA.
AC   Q03829; D6VZY8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-NOV-2023, entry version 165.
DE   RecName: Full=Mitochondrial magnesium exporter 1 {ECO:0000303|PubMed:25585246};
GN   Name=MME1 {ECO:0000303|PubMed:25585246}; OrderedLocusNames=YMR166C;
GN   ORFNames=YM8520.15C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   IDENTIFICATION AS A MITOCHONDRIAL TRANSPORTER.
RX   PubMed=10930523; DOI=10.1016/s0005-2736(00)00222-4;
RA   Belenkiy R., Haefele A., Eisen M.B., Wohlrab H.;
RT   "The yeast mitochondrial transport proteins: new sequences and consensus
RT   residues, lack of direct relation between consensus residues and
RT   transmembrane helices, expression patterns of the transport protein genes,
RT   and protein-protein interactions with other proteins.";
RL   Biochim. Biophys. Acta 1467:207-218(2000).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=25585246; DOI=10.1016/j.bbamcr.2014.12.029;
RA   Cui Y., Zhao S., Wang J., Wang X., Gao B., Fan Q., Sun F., Zhou B.;
RT   "A novel mitochondrial carrier protein Mme1 acts as a yeast mitochondrial
RT   magnesium exporter.";
RL   Biochim. Biophys. Acta 1853:724-732(2015).
CC   -!- FUNCTION: Transporter of the mitochondrial inner membrane that exports
CC       magnesium and thus, plays a key role in mitochondrial Mg(2+)
CC       homeostasis. {ECO:0000269|PubMed:25585246,
CC       ECO:0000305|PubMed:10930523}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:25585246}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Significantly increases steady-state
CC       mitochondrial magnesium concentration (PubMed:25585246). Rescues the
CC       group II RNA splicing defect in the MRS2 and LPE10 deletion mutants
CC       (PubMed:25585246). {ECO:0000269|PubMed:25585246}.
CC   -!- MISCELLANEOUS: Present with 2060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; Z49705; CAA89802.1; -; Genomic_DNA.
DR   EMBL; AY558121; AAS56447.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10062.1; -; Genomic_DNA.
DR   PIR; S54524; S54524.
DR   RefSeq; NP_013889.1; NM_001182670.1.
DR   AlphaFoldDB; Q03829; -.
DR   SMR; Q03829; -.
DR   BioGRID; 35344; 147.
DR   STRING; 4932.YMR166C; -.
DR   TCDB; 2.A.29.18.6; the mitochondrial carrier (mc) family.
DR   iPTMnet; Q03829; -.
DR   PaxDb; 4932-YMR166C; -.
DR   PeptideAtlas; Q03829; -.
DR   EnsemblFungi; YMR166C_mRNA; YMR166C; YMR166C.
DR   GeneID; 855202; -.
DR   KEGG; sce:YMR166C; -.
DR   AGR; SGD:S000004776; -.
DR   SGD; S000004776; MME1.
DR   VEuPathDB; FungiDB:YMR166C; -.
DR   eggNOG; KOG0770; Eukaryota.
DR   HOGENOM; CLU_015166_3_2_1; -.
DR   InParanoid; Q03829; -.
DR   OMA; FFGVYEF; -.
DR   OrthoDB; 103750at2759; -.
DR   BioCyc; YEAST:G3O-32856-MONOMER; -.
DR   BioGRID-ORCS; 855202; 4 hits in 10 CRISPR screens.
DR   PRO; PR:Q03829; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03829; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:SGD.
DR   GO; GO:1990616; P:magnesium ion export from mitochondrion; IMP:SGD.
DR   GO; GO:0015693; P:magnesium ion transport; IDA:SGD.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45667:SF7; MITOCHONDRIAL MAGNESIUM EXPORTER 1; 1.
DR   PANTHER; PTHR45667; S-ADENOSYLMETHIONINE MITOCHONDRIAL CARRIER PROTEIN; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..368
FT                   /note="Mitochondrial magnesium exporter 1"
FT                   /id="PRO_0000090699"
FT   TRANSMEM        56..77
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..165
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..353
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          51..138
FT                   /note="Solcar 1"
FT   REPEAT          146..240
FT                   /note="Solcar 2"
FT   REPEAT          254..360
FT                   /note="Solcar 3"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  40992 MW;  B583100018DF045D CRC64;
     MNSWNLSSSI PIIHTPHDHP PTSEGTPDQP NNNRKDDKLH KKRGDSDEDL SPIWHCVVSG
     GIGGKIGDSA MHSLDTVKTR QQGAPNVKKY RNMISAYRTI WLEEGVRRGL YGGYMAAMLG
     SFPSAAIFFG TYEYTKRTMI EDWQINDTIT HLSAGFLGDF ISSFVYVPSE VLKTRLQLQG
     RFNNPFFQSG YNYSNLRNAI KTVIKEEGFR SLFFGYKATL ARDLPFSALQ FAFYEKFRQL
     AFKIEQKDGR DGELSIPNEI LTGACAGGLA GIITTPMDVV KTRVQTQQPP SQSNKSYSVT
     HPHVTNGRPA ALSNSISLSL RTVYQSEGVL GFFSGVGPRF VWTSVQSSIM LLLYQMTLRG
     LSNAFPTD
//