ID LPE10_CANAL Reviewed; 453 AA. AC Q59S85; A0A1D8PPV1; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 27-MAR-2024, entry version 94. DE RecName: Full=Mitochondrial inner membrane magnesium transporter LPE10; DE Flags: Precursor; GN Name=LPE10; OrderedLocusNames=CAALFM_C602150CA; GN ORFNames=CaO19.10959, CaO19.3455; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). 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:0000250|UniProtKB:Q02783}. CC -!- SUBUNIT: Forms homooligomers. Interacts with MRS2. CC {ECO:0000250|UniProtKB:Q02783}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:Q02783}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q02783}. 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; CP017628; AOW30150.1; -; Genomic_DNA. DR RefSeq; XP_712495.2; XM_707402.2. DR AlphaFoldDB; Q59S85; -. DR SMR; Q59S85; -. DR EnsemblFungi; C6_02150C_A-T; C6_02150C_A-T-p1; C6_02150C_A. DR GeneID; 3645888; -. DR KEGG; cal:CAALFM_C602150CA; -. DR CGD; CAL0000183380; orf19.10959. DR VEuPathDB; FungiDB:C6_02150C_A; -. DR eggNOG; KOG2662; Eukaryota. DR HOGENOM; CLU_025144_1_0_1; -. DR InParanoid; Q59S85; -. DR OrthoDB; 73031at2759; -. DR PRO; PR:Q59S85; -. DR Proteomes; UP000000559; Chromosome 6. DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; IBA:GO_Central. DR CDD; cd12823; Mrs2_Mfm1p-like; 1. DR Gene3D; 2.40.128.330; -; 1. DR Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1. DR InterPro; IPR039204; MRS2-like. DR PANTHER; PTHR13890:SF26; MAGNESIUM TRANSPORTER MRS2 HOMOLOG, MITOCHONDRIAL; 1. DR PANTHER; PTHR13890; RNA SPLICING PROTEIN MRS2, MITOCHONDRIAL; 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..19 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 20..453 FT /note="Mitochondrial inner membrane magnesium transporter FT LPE10" FT /id="PRO_0000043236" FT TRANSMEM 376..396 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 414..434 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 108..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 400..403 FT /note="YGMN" SQ SEQUENCE 453 AA; 51091 MW; D637CD86460DCEAA CRC64; MIPIRSSITR ILPNGFLSKP FLRQLNKKSK PNPHKNKNFD SFNEVFIHKT LLSSIKQHND TDYVRCSIFN ANGDMIQHGK EILKSQFIKR YNLTPRDFRK FNWQRSATGT TTTSSSSSSS AGQTSSGTSK SSSSSSSSSS PHSTISALSL SNSSLGSSTN VDIVPNITIR RNSILVQLLN IRALINHDQL IIFDNSSSFQ NSHVSSYTHS QCLKDLSQRL KSTNLDGLPF EFKALEGILI YIVSNLNMEM KVHNTVLQNI ITGLEDSIDR NKLRYLLIES KKIHQFHRKI TLIKNCLEDL LENDDELNDL YITEKFNSEG DGQPRQGTNH EEIEMLLENY YQTIDEIVQI VENLKNQIKT TEDLINVVLD SNRNQLMLLG LKFSTGLLSM GVALYVSALY GMNLENFIEE IDGGFEVVTV VSTIALIALL LFSVKQLKKV EKVTMTSLND QRK //