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 29-SEP-2021, entry version 92. 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}. 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; CM002236; EAA35672.1; -; Genomic_DNA. DR RefSeq; XP_964908.1; XM_959815.2. DR SMR; Q7SFQ9; -. 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 Proteomes; UP000001805; Unassembled WGS sequence. 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 //