LPE10_CANAL
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 03-AUG-2022, entry version 88.
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 STRING; 237561.Q59S85; -.
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; 1363588at2759; -.
DR PRO; PR:Q59S85; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015693; P:magnesium ion transport; IBA:GO_Central.
DR GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd12823; Mrs2_Mfm1p-like; 1.
DR InterPro; IPR039204; MRS2-like.
DR PANTHER; PTHR13890; PTHR13890; 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