MDM10_EMENI
ID MDM10_EMENI Reviewed; 427 AA.
AC Q8J0L4; C8V2X8; Q5AXS9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=mdmB; Synonyms=mdm10; ORFNames=AN6901;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12740872; DOI=10.1002/cm.10117;
RA Koch K.V., Suelmann R., Fischer R.;
RT "Deletion of mdmB impairs mitochondrial distribution and morphology in
RT Aspergillus nidulans.";
RL Cell Motil. Cytoskeleton 55:114-124(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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, ECO:0000269|PubMed:12740872}.
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; AJ536057; CAD59923.1; -; Genomic_DNA.
DR EMBL; AACD01000113; EAA58300.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF71692.1; -; Genomic_DNA.
DR RefSeq; XP_664505.1; XM_659413.1.
DR AlphaFoldDB; Q8J0L4; -.
DR SMR; Q8J0L4; -.
DR STRING; 162425.CADANIAP00007703; -.
DR EnsemblFungi; CBF71692; CBF71692; ANIA_06901.
DR EnsemblFungi; EAA58300; EAA58300; AN6901.2.
DR GeneID; 2870608; -.
DR KEGG; ani:AN6901.2; -.
DR eggNOG; ENOG502QUN5; Eukaryota.
DR HOGENOM; CLU_026505_1_0_1; -.
DR InParanoid; Q8J0L4; -.
DR OMA; MLDFMDY; -.
DR OrthoDB; 1463552at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0001401; C:SAM complex; IBA:GO_Central.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IBA:GO_Central.
DR HAMAP; MF_03102; Mdm10; 1.
DR InterPro; IPR027539; Mdm10.
DR PANTHER; PTHR28035; PTHR28035; 1.
DR Pfam; PF12519; MDM10; 2.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..427
FT /note="Mitochondrial distribution and morphology protein
FT 10"
FT /id="PRO_0000384179"
FT REGION 393..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46345 MW; 8393B663F38E9739 CRC64;
MLDFMDYIQL AFAEGTQRNC DNSYSSLTAT TQNLLDFTTP ERVRIHLSSL STPNFATSYT
LGTVGLIEGS ISYLYSNISF DNTPSKSALI PLRKLAPGYR QVQAPIAPPS SKGQKATLLH
ATLHLPPPTT LNALFLRRIS PTMQLSLAVS STRGPPLSKS APQATLLTQL THDTGKYSNE
YLFSTDNSLF GWRGLWNFGP DPRFNNNAQR LSLLSAGAEA YYSPVSSLIG MSTGLRFCTL
PAATSSTPNP NTPISTFPYT LTLTLTPLTG SLSTSYSVRA SPNLSFSSRF GFNVYSWESE
MVAGFELWRQ SRKAAIVDND GLEWARNKAR IWDIPASSQV PEPITPSEEE TQESVLKVRV
DQSWNVRLLW EGRVKELLVS AGVGLGPSSF SPSSYANSQA TAGAQGSSGG PPTSYWRGVG
VSVSYSS
