MRS2_YEAST
ID MRS2_YEAST Reviewed; 470 AA.
AC Q01926; D6W329;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Magnesium transporter MRS2, mitochondrial;
DE AltName: Full=RNA-splicing protein MRS2;
DE Flags: Precursor;
GN Name=MRS2; OrderedLocusNames=YOR334W;
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 [GENOMIC DNA].
RC STRAIN=ATCC 44774 / DBY747;
RX PubMed=1551905; DOI=10.1016/s0021-9258(19)50522-1;
RA Wiesenberger G., Waldherr M., Schweyen R.J.;
RT "The nuclear gene MRS2 is essential for the excision of group II introns
RT from yeast mitochondrial transcripts in vivo.";
RL J. Biol. Chem. 267:6963-6969(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8252639; DOI=10.1007/bf00336780;
RA Waldherr M., Ragnini A., Jank B., Teply R., Wiesenberger G., Schweyen R.J.;
RT "A multitude of suppressors of group II intron-splicing defects in yeast.";
RL Curr. Genet. 24:301-306(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=11544180; DOI=10.1101/gad.201301;
RA Gregan J., Kolisek M., Schweyen R.J.;
RT "Mitochondrial Mg(2+) homeostasis is critical for group II intron splicing
RT in vivo.";
RL Genes Dev. 15:2229-2237(2001).
RN [7]
RP TOPOLOGY.
RX PubMed=11932259; DOI=10.1074/jbc.m201670200;
RA Baumann F., Neupert W., Herrmann J.M.;
RT "Insertion of bitopic membrane proteins into the inner membrane of
RT mitochondria involves an export step from the matrix.";
RL J. Biol. Chem. 277:21405-21413(2002).
RN [8]
RP FUNCTION.
RX PubMed=12628916; DOI=10.1093/emboj/cdg122;
RA Kolisek M., Zsurka G., Samaj J., Weghuber J., Schweyen R.J., Schweigel M.;
RT "Mrs2p is an essential component of the major electrophoretic Mg2+ influx
RT system in mitochondria.";
RL EMBO J. 22:1235-1244(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=17827224; DOI=10.1529/biophysj.107.112318;
RA Schindl R., Weghuber J., Romanin C., Schweyen R.J.;
RT "Mrs2p forms a high conductance Mg2+ selective channel in mitochondria.";
RL Biophys. J. 93:3872-3883(2007).
RN [12]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MFM1.
RX PubMed=20653776; DOI=10.1111/j.1742-4658.2010.07761.x;
RA Sponder G., Svidova S., Schindl R., Wieser S., Schweyen R.J., Romanin C.,
RA Froschauer E.M., Weghuber J.;
RT "Lpe10p modulates the activity of the Mrs2p-based yeast mitochondrial Mg2+
RT channel.";
RL FEBS J. 277:3514-3525(2010).
RN [13] {ECO:0007744|PDB:3RKG}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 48-308, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-97; MET-309 AND VAL-315.
RX PubMed=23999289; DOI=10.1107/s0907444913011712;
RA Khan M.B., Sponder G., Sjoblom B., Svidova S., Schweyen R.J., Carugo O.,
RA Djinovic-Carugo K.;
RT "Structural and functional characterization of the N-terminal domain of the
RT yeast Mg2+ channel Mrs2.";
RL Acta Crystallogr. D 69:1653-1664(2013).
CC -!- FUNCTION: High-conductance magnesium-selective channel that mediates
CC the influx of magnesium into the mitochondrial matrix (PubMed:12628916,
CC PubMed:17827224, PubMed:20653776, PubMed:23999289). Essential for the
CC splicing of mRNA group II introns in mitochondria by affecting
CC mitochondrial magnesium concentrations, which are critical for group II
CC intron splicing. It also suppresses a variety of mitochondrial intron
CC mutations and its absence may disturb the assembly of mitochondrial
CC membrane complexes (PubMed:11544180). {ECO:0000269|PubMed:11544180,
CC ECO:0000269|PubMed:12628916, ECO:0000269|PubMed:17827224,
CC ECO:0000269|PubMed:20653776, ECO:0000269|PubMed:23999289}.
CC -!- SUBUNIT: Homopentamer (PubMed:23999289). Forms homooligomers. Interacts
CC with MFM1 (PubMed:20653776). {ECO:0000269|PubMed:20653776,
CC ECO:0000269|PubMed:23999289}.
CC -!- INTERACTION:
CC Q01926; Q02783: MFM1; NbExp=2; IntAct=EBI-11283, EBI-33672;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000305|PubMed:23999289}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:1551905 and PubMed:8252639) identified
CC in genetic screens for bona fide RNA splicing factors, but it has later
CC been shown that not the MRS2 protein per se but certain magnesium
CC concentrations are essential for group II intron splicing.
CC {ECO:0000305|PubMed:11544180}.
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DR EMBL; M82916; AAA34795.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89979.1; -; Genomic_DNA.
DR EMBL; Z75241; CAA99656.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11095.1; -; Genomic_DNA.
DR PIR; S62064; S62064.
DR RefSeq; NP_014979.1; NM_001183754.1.
DR PDB; 3RKG; X-ray; 1.28 A; A=48-308.
DR PDBsum; 3RKG; -.
DR AlphaFoldDB; Q01926; -.
DR SMR; Q01926; -.
DR BioGRID; 34717; 175.
DR DIP; DIP-5325N; -.
DR IntAct; Q01926; 1.
DR MINT; Q01926; -.
DR STRING; 4932.YOR334W; -.
DR TCDB; 1.A.35.5.1; the cora metal ion transporter (mit) family.
DR MaxQB; Q01926; -.
DR PaxDb; Q01926; -.
DR PRIDE; Q01926; -.
DR EnsemblFungi; YOR334W_mRNA; YOR334W; YOR334W.
DR GeneID; 854511; -.
DR KEGG; sce:YOR334W; -.
DR SGD; S000005861; MRS2.
DR VEuPathDB; FungiDB:YOR334W; -.
DR eggNOG; KOG2662; Eukaryota.
DR GeneTree; ENSGT00390000009988; -.
DR HOGENOM; CLU_025144_1_0_1; -.
DR InParanoid; Q01926; -.
DR OMA; TQHDVEG; -.
DR BioCyc; YEAST:G3O-33809-MON; -.
DR PRO; PR:Q01926; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q01926; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central.
DR GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; IDA:SGD.
DR CDD; cd12823; Mrs2_Mfm1p-like; 1.
DR InterPro; IPR039204; MRS2-like.
DR PANTHER; PTHR13890; PTHR13890; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Magnesium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..470
FT /note="Magnesium transporter MRS2, mitochondrial"
FT /id="PRO_0000021753"
FT TOPO_DOM 33..314
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..344
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..470
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT MOTIF 332..335
FT /note="YGMN"
FT /evidence="ECO:0000305"
FT MUTAGEN 97
FT /note="D->A,F,W: No effect on Mg(2+) import."
FT /evidence="ECO:0000269|PubMed:23999289"
FT MUTAGEN 309
FT /note="M->E,G: Increases Mg(2+) import into mitochondria."
FT /evidence="ECO:0000269|PubMed:23999289"
FT MUTAGEN 309
FT /note="M->F: Decreases Mg(2+) import into mitochondria."
FT /evidence="ECO:0000269|PubMed:23999289"
FT MUTAGEN 315
FT /note="V->E,F,G: No effect on Mg(2+) import."
FT /evidence="ECO:0000269|PubMed:23999289"
FT CONFLICT 371
FT /note="S -> F (in Ref. 1; AAA34795 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="E -> D (in Ref. 1; AAA34795 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3RKG"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 143..161
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 170..206
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 210..241
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3RKG"
FT HELIX 263..303
FT /evidence="ECO:0007829|PDB:3RKG"
SQ SEQUENCE 470 AA; 54203 MW; EFEBA11765AB8B31 CRC64;
MNRRLLVRSI SCFQPLSRIT FGRPNTPFLR KYADTSTAAN TNSTILRKQL LSLKPISASD
SLFISCTVFN SKGNIISMSE KFPKWSFLTE HSLFPRDLRK IDNSSIDIIP TIMCKPNCIV
INLLHIKALI ERDKVYVFDT TNPSAAAKLS VLMYDLESKL SSTKNNSQFY EHRALESIFI
NVMSALETDF KLHSQICIQI LNDLENEVNR LKLRHLLIKS KDLTLFYQKT LLIRDLLDEL
LENDDDLANM YLTVKKSPKD NFSDLEMLIE TYYTQCDEYV QQSESLIQDI KSTEEIVNII
LDANRNSLML LELKVTIYTL GFTVASVLPA FYGMNLKNFI EESEWGFTSV AVFSIVSALY
ITKKNFNSLR SVTKMTMYPN SPANSSVYPK TSASIALTNK LKRRRKWWKS TKQRLGVLLY
GSSYTNKANL SNNKINKGFS KVKKFNMEND IKNKQNRDMI WKWLIEDKKN
