LPE10_YEAST
ID LPE10_YEAST Reviewed; 413 AA.
AC Q02783; D6W3V4; Q6B1B1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mitochondrial inner membrane magnesium transporter MFM1;
DE AltName: Full=MRS2 function modulating factor 1;
DE Flags: Precursor;
GN Name=MFM1; Synonyms=LPE10; OrderedLocusNames=YPL060W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11254124; DOI=10.1007/s004380000366;
RA Gregan J., Bui D.M., Pillich R., Fink M., Zsurka G., Schweyen R.J.;
RT "The mitochondrial inner membrane protein Lpe10p, a homologue of Mrs2p, is
RT essential for magnesium homeostasis and group II intron splicing in
RT yeast.";
RL Mol. Gen. Genet. 264:773-781(2001).
RN [5]
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 [6]
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 [7]
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [9]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MRS2.
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).
CC -!- FUNCTION: Mitochondrial inner membrane magnesium transporter required
CC for mitochondrial magnesium homeostasis. Modulates the conductance of
CC the MRS2 channel. Involved in the splicing of mRNA group II introns in
CC mitochondria by affecting mitochondrial magnesium concentrations, which
CC are critical for group II intron splicing.
CC {ECO:0000269|PubMed:11254124, ECO:0000269|PubMed:17827224,
CC ECO:0000269|PubMed:20653776}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with MRS2.
CC {ECO:0000269|PubMed:20653776}.
CC -!- INTERACTION:
CC Q02783; Q01926: MRS2; NbExp=2; IntAct=EBI-33672, EBI-11283;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11254124, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19756047}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11254124, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19756047}.
CC -!- PTM: N-glycosylated. Glycosylation is important for correct
CC localization of the protein. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 396 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}.
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DR EMBL; U39205; AAB68305.1; -; Genomic_DNA.
DR EMBL; AY693169; AAT93188.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11370.1; -; Genomic_DNA.
DR PIR; S60930; S60930.
DR RefSeq; NP_015265.1; NM_001183874.1.
DR AlphaFoldDB; Q02783; -.
DR SMR; Q02783; -.
DR BioGRID; 36118; 138.
DR DIP; DIP-4653N; -.
DR IntAct; Q02783; 1.
DR MINT; Q02783; -.
DR STRING; 4932.YPL060W; -.
DR TCDB; 1.A.35.5.5; the cora metal ion transporter (mit) family.
DR MaxQB; Q02783; -.
DR PaxDb; Q02783; -.
DR PRIDE; Q02783; -.
DR EnsemblFungi; YPL060W_mRNA; YPL060W; YPL060W.
DR GeneID; 856045; -.
DR KEGG; sce:YPL060W; -.
DR SGD; S000005981; MFM1.
DR VEuPathDB; FungiDB:YPL060W; -.
DR eggNOG; KOG2662; Eukaryota.
DR GeneTree; ENSGT00390000009988; -.
DR HOGENOM; CLU_025144_1_0_1; -.
DR InParanoid; Q02783; -.
DR OMA; TRNNCII; -.
DR BioCyc; YEAST:G3O-33971-MON; -.
DR BRENDA; 7.2.2.14; 984.
DR Reactome; R-SCE-5223345; Miscellaneous transport and binding events.
DR PRO; PR:Q02783; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02783; 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:0015095; F:magnesium ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central.
DR GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; IMP: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 Glycoprotein; Ion transport; Magnesium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..413
FT /note="Mitochondrial inner membrane magnesium transporter
FT MFM1"
FT /id="PRO_0000042816"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 353..356
FT /note="YGMN"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 267
FT /note="M -> V (in Ref. 3; AAT93188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47083 MW; BC34284D00A465CA CRC64;
MRAFPRVLPF RHQRSYNNIL LRTVRLFGSS LSSFDFSRQM PKVDPDNTAA MLLQKNLIQR
NNMLYGYGSG TIRCTLLDST GRAKSPLVEI KREDLVSKHG LLPRDLRKIE KSRKNDLVPS
LLVRENSILI SLLTVKALIK PDMVIIFDSA GSGITLNSEA HKDFINDMKL RLKNQETSEL
NSDPLPYEFR ALETIFISAL SNLTSEMKVL LTICKGVLQD LEFSITRDKL RFLLGQNKKL
SSFNKKAVLV KDMLDDLLEQ DDMLCDMYLT DKKAGKIRVQ DDHTEIEMLL ETYHNYVDEI
VQKSESAISD VKTTEEIINI ILDSNRNELM LLGIRYAIGM LSLGGALFLG SIYGMNLESF
IEESNYAYLT VTILGLISTV WLYAKGIRHL HKLQRMTLLS KIKTDSVHEL LKK
