MDM10_PODAN
ID MDM10_PODAN Reviewed; 448 AA.
AC O13498; A0A090CUH5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
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}; Synonyms=RGS27;
GN OrderedLocusNames=Pa_7_11600; ORFNames=PODANS_7_11600;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LEU-420.
RX PubMed=9343397; DOI=10.1128/mcb.17.11.6359;
RA Jamet-Vierny C., Contamine V., Boulay J., Zickler D., Picard M.;
RT "Mutations in genes encoding the mitochondrial outer membrane proteins
RT Tom70 and Mdm10 of Podospora anserina modify the spectrum of mitochondrial
RT DNA rearrangements associated with cellular death.";
RL Mol. Cell. Biol. 17:6359-6366(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; Y14749; CAA75046.1; -; Genomic_DNA.
DR EMBL; CU633900; CAP69204.1; -; Genomic_DNA.
DR EMBL; FO904942; CDP32685.1; -; Genomic_DNA.
DR RefSeq; XP_001908531.1; XM_001908496.1.
DR AlphaFoldDB; O13498; -.
DR SMR; O13498; -.
DR STRING; 5145.XP_001908531.1; -.
DR EnsemblFungi; CAP69204; CAP69204; PODANS_7_11600.
DR GeneID; 6192148; -.
DR KEGG; pan:PODANSg5566; -.
DR VEuPathDB; FungiDB:PODANS_7_11600; -.
DR eggNOG; ENOG502QUN5; Eukaryota.
DR HOGENOM; CLU_026505_1_0_1; -.
DR OrthoDB; 1463552at2759; -.
DR Proteomes; UP000001197; Chromosome 7.
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 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..448
FT /note="Mitochondrial distribution and morphology protein
FT 10"
FT /id="PRO_0000384195"
FT MUTAGEN 420
FT /note="L->P: In MDM10-1; produces giant mitochondria and
FT results in the accumulation of specific deleted
FT mitochondrial genomes during the senescence process of the
FT fungus."
FT /evidence="ECO:0000269|PubMed:9343397"
SQ SEQUENCE 448 AA; 48963 MW; CC4E629277136A2F CRC64;
MREFMQYVRN AFYGATGWSE DNSYKDLNVT ARELIDFPLP RGIRLSLSSL ATPHFATSYQ
LCNVGVVDGS ISYLHSSVPL AAVPAQSNKI PLGALMRSYR GLHQLGSRGG TPWSWETGPQ
IGTIPQVPAV ADMGQIPNKD KSSLLYGRLY LPQSLLEAMV IKRFSPALQV QISAVSEQSL
RNGGTMLSVV QYDRGKYGVE GLYSTDGGLL GLRGLYNFGG DASVAVMSSQ NGTGSPESTE
KERIYGRFSA GGEMYYGTLN KSGGMSLGAR FATLPTHKGT PLTATLTINP LMGNINTTYA
VLAKDFLAMA TRMEFNAYSY ESDWAVGLEL WSNRRPAGFL LGAEPSLDLE SDQPELPSKK
ERSFQAKMEW RLDDPEPEPE PVKIAEKPTE GKEEYLGVFK ARLSSNLDLG LVWEGRAKSL
IFSLGTGVDL QRLGEPFRSL GLEVQYSS
