ID   MDM10_CANGA             Reviewed;         460 AA.
AC   Q6FWV0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Mitochondrial distribution and morphology protein 10 {ECO:0000255|HAMAP-Rule:MF_03102};
DE   AltName: Full=Mitochondrial inheritance component MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
GN   Name=MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
GN   OrderedLocusNames=CAGL0C02695g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC       molecular tether to connect the endoplasmic reticulum and mitochondria.
CC       Components of this complex are involved in the control of mitochondrial
CC       shape and protein biogenesis and may function in phospholipid exchange.
CC       MDM10 is involved in the late assembly steps of the general translocase
CC       of the mitochondrial outer membrane (TOM complex). Functions in the
CC       TOM40-specific route of the assembly of outer membrane beta-barrel
CC       proteins, including the association of TOM40 with the receptor TOM22
CC       and small TOM proteins. Can associate with the SAM(core) complex as
CC       well as the MDM12-MMM1 complex, both involved in late steps of the
CC       major beta-barrel assembly pathway, that is responsible for biogenesis
CC       of all outer membrane beta-barrel proteins. May act as a switch that
CC       shuttles between both complexes and channels precursor proteins into
CC       the TOM40-specific pathway. Plays a role in mitochondrial morphology
CC       and in the inheritance of mitochondria. {ECO:0000255|HAMAP-
CC       Rule:MF_03102}.
CC   -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC       or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates
CC       with the mitochondrial outer membrane sorting assembly machinery
CC       SAM(core) complex. {ECO:0000255|HAMAP-Rule:MF_03102}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03102}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03102}. Note=The ERMES/MDM complex localizes to a few discrete
CC       foci (around 10 per single cell), that represent mitochondria-
CC       endoplasmic reticulum junctions. These foci are often found next to
CC       mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03102}.
CC   -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting that it
CC       resides in the membrane via beta-sheet conformations similar to those
CC       predicted for other outer membrane proteins and porin.
CC   -!- SIMILARITY: Belongs to the MDM10 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03102}.
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DR   EMBL; CR380949; CAG58200.1; -; Genomic_DNA.
DR   RefSeq; XP_445294.1; XM_445294.1.
DR   AlphaFoldDB; Q6FWV0; -.
DR   SMR; Q6FWV0; -.
DR   STRING; 5478.XP_445294.1; -.
DR   EnsemblFungi; CAG58200; CAG58200; CAGL0C02695g.
DR   GeneID; 2886928; -.
DR   KEGG; cgr:CAGL0C02695g; -.
DR   CGD; CAL0127332; CAGL0C02695g.
DR   VEuPathDB; FungiDB:CAGL0C02695g; -.
DR   eggNOG; ENOG502QUN5; Eukaryota.
DR   HOGENOM; CLU_026505_0_0_1; -.
DR   InParanoid; Q6FWV0; -.
DR   OMA; MLDFMDY; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0001401; C:SAM complex; IEA:EnsemblFungi.
DR   GO; GO:0051654; P:establishment of mitochondrion localization; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:UniProtKB-UniRule.
DR   GO; GO:0015914; P:phospholipid transport; IEA:EnsemblFungi.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03102; Mdm10; 1.
DR   InterPro; IPR027539; Mdm10.
DR   PANTHER; PTHR28035; PTHR28035; 1.
DR   Pfam; PF12519; MDM10; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane beta strand.
FT   CHAIN           1..460
FT                   /note="Mitochondrial distribution and morphology protein
FT                   10"
FT                   /id="PRO_0000384171"
SQ   SEQUENCE   460 AA;  52995 MW;  1C7DA8E74B2EFF1A CRC64;
     MLDYMDYVQQ CFDSAGRWKR QNSYGEVTQT PRNLIDFKIP DAVNLQVSNR STKYSYNSLQ
     LSTRQSINGS LTYLYTNLDA VEGLVKNTEE LPLHDIVQTY ELPAVTHHRK EKTNFHKCSL
     FYGKIFYPSS DVEAMMIKRF SPMNQVIVKC LSSLKENVNI FTAYFQRNSE KNFQELIVSS
     NDLLCGYRIS HHFLRTPSKL NSSLYNNSSL FFGAEFWLGM ISLNPGCSTS LKYCTHSANT
     GRPLTLTLSW NPLFGHISTT YSAMTSSSST FCAKYDFNIY SIESNLSFGI ELWRKTGALF
     KSEDSVEANR KEYEQNFYIS HDHNLLPSKY GYDHEYNISD GKLSKEHKRN KIIKDLNHAF
     STSLQKIDKE KTRIENFGNI IRNSHFTSVF KASTSLRERN LKFLWEGEYK NFLLSAGTEL
     RVLKAEESEL RRTSGQSSNS LLNEFSLQPL KFGVQIQFSS