MDM10_DEBHA
ID MDM10_DEBHA Reviewed; 471 AA.
AC Q6BTX9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 76.
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=DEHA2C15092g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG86420.2; -; Genomic_DNA.
DR RefSeq; XP_458340.2; XM_458340.1.
DR AlphaFoldDB; Q6BTX9; -.
DR SMR; Q6BTX9; -.
DR STRING; 4959.XP_458340.2; -.
DR EnsemblFungi; CAG86420; CAG86420; DEHA2C15092g.
DR GeneID; 2900479; -.
DR KEGG; dha:DEHA2C15092g; -.
DR VEuPathDB; FungiDB:DEHA2C15092g; -.
DR eggNOG; ENOG502QUN5; Eukaryota.
DR HOGENOM; CLU_026505_0_0_1; -.
DR InParanoid; Q6BTX9; -.
DR OMA; MLDFMDY; -.
DR OrthoDB; 1463552at2759; -.
DR Proteomes; UP000000599; 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: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: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..471
FT /note="Mitochondrial distribution and morphology protein
FT 10"
FT /id="PRO_0000384178"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 52585 MW; 930D0684AF1AC9AE CRC64;
MYTYMEYLQK CFYKTTNWNE DNIFSNITAT SSALLEFPIP NGCKVDLSSK ATEHSASSFT
LSNYHSINGS LAYLYSSIPL RNTMGTKDIS LQDAISGFKM LELNSSTTNA LQNPVYKNTH
DSLLYGRMYF PGSALEAMII KRISPQTQLL IKCINNPHLD KNGTMIVYLQ KNAPKLSREF
IYSTNEALFG FRCLYNMGSS ESNLNRSINN SNLIPKFDNS VISIGTEIWY AALSMSPGLS
TAFRYSTRST STGKPLTMTF ACNPILGHIS SAYTVKTSVA STFCSKYDFN VFSYASNLSL
GFEIYNYSSS NTSNSAATPP RIKNSDSQVL SNNSTDSKGT VHIRSPDVLD YKNHSNVIIS
PIQTFDNYYH INPTLLPSTK NEFEEVRPPP LESQVDSNNE TAMTAFENLV NESDFSSVIK
LSTSLNDKML KLLWKGRCKD FLVTTGVKMI LNPITNTPEF NRFGISFSYA C
