ID   MRS2_NEUCR              Reviewed;         547 AA.
AC   Q7SFQ9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Mitochondrial inner membrane magnesium transporter mrs2;
DE   AltName: Full=RNA-splicing protein MRS2;
DE   Flags: Precursor;
GN   Name=mrs2; ORFNames=NCU09091;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: High-conductance magnesium-selective channel that mediates
CC       the influx of magnesium into the mitochondrial matrix. Essential for
CC       the 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. {ECO:0000250|UniProtKB:Q01926}.
CC   -!- SUBUNIT: Homopentamer. Forms homooligomers. Interacts with MFM1.
CC       {ECO:0000250|UniProtKB:Q01926}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q01926}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q01926}.
CC   -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC       family. {ECO:0000305}.
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DR   EMBL; CM002236; EAA35672.1; -; Genomic_DNA.
DR   RefSeq; XP_964908.1; XM_959815.2.
DR   AlphaFoldDB; Q7SFQ9; -.
DR   SMR; Q7SFQ9; -.
DR   STRING; 5141.EFNCRP00000008702; -.
DR   PRIDE; Q7SFQ9; -.
DR   EnsemblFungi; EAA35672; EAA35672; NCU09091.
DR   GeneID; 3881059; -.
DR   KEGG; ncr:NCU09091; -.
DR   VEuPathDB; FungiDB:NCU09091; -.
DR   HOGENOM; CLU_025144_2_0_1; -.
DR   InParanoid; Q7SFQ9; -.
DR   OMA; EKTHDLY; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central.
DR   GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; ISS:UniProtKB.
DR   CDD; cd12823; Mrs2_Mfm1p-like; 1.
DR   InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR   InterPro; IPR039204; MRS2-like.
DR   PANTHER; PTHR13890; PTHR13890; 1.
DR   Pfam; PF01544; CorA; 1.
PE   3: Inferred from homology;
KW   Ion transport; Magnesium; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..75
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           76..547
FT                   /note="Mitochondrial inner membrane magnesium transporter
FT                   mrs2"
FT                   /id="PRO_0000043247"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          46..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           452..455
FT                   /note="YGMN"
FT   COMPBIAS        53..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  61554 MW;  41F0138ECFCF3E45 CRC64;
     MPPALRPAAP SRSLLRYLRA QSEGLSFAPT CRAAAERHPA LQCRHGCTAG GSTRPPRQPS
     SSTTTRSLST ATPPKRTQLR AGLVDLEAIL PKSLRKQRTT KSLLALPPPA GSLRFSSNQS
     SDCDSKRPKL REWLFGNGEK KGPPDTRLND DDIRVALEEE SGSIFQRRAL TAKAAMDPRL
     RCTEVDENGN VVMVDGELKK SELIAKYGLL PRDLRKIDSS NLPHILIRPS AILLNLLHLK
     VLIKHDCVLL FDVYGSKSSY PQSAFMYDLQ GKLQQKQSSG ANSLPYEFRA LEAVLMSVTS
     ELEADFEAVR DPVIRILSEL EDDIDREKLR VLLVLSKRVS TFEQKAKLVR DAIEELLEAD
     DDLASMYLTE KTHDLYRGED DHTEIELLLE SYNKICDEVV EEASNLVSSI RNTEEIIRAI
     LDANRNSLML LDLKFSVGTL GLAMGTFLAS WYGMNLENFI EETNWGFAMV TSVSTVASLI
     VCWYGLVKLR KVQRVKMGDL HNRNAPNHWF RDESTDVLLD PSNRERLRRI NSMKSAQQKR
     STSKKWF