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MDM10_ASPOR
ID   MDM10_ASPOR             Reviewed;         431 AA.
AC   Q2U5V7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=AO090120000494;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007166; BAE63058.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2U5V7; -.
DR   SMR; Q2U5V7; -.
DR   STRING; 510516.Q2U5V7; -.
DR   EnsemblFungi; BAE63058; BAE63058; AO090120000494.
DR   VEuPathDB; FungiDB:AO090120000494; -.
DR   HOGENOM; CLU_026505_1_0_1; -.
DR   OMA; MLDFMDY; -.
DR   Proteomes; UP000006564; Chromosome 5.
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..431
FT                   /note="Mitochondrial distribution and morphology protein
FT                   10"
FT                   /id="PRO_0000384166"
FT   REGION          358..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  47248 MW;  76769FF7C3161E9D CRC64;
     MLDFMDYIQL AFAEGTNWNR DNSYSSLTAT AQSLLDFSTP ERLRVHLSSL STPNFATSYT
     LGTVGLIDGS VSYLYSTVPF TNTPSRSALI PLRKLSPGYR QVAPPSAPIE DWNLDSILDN
     PQNVQPSFAS KPTLLHATLH LPPPTTLNAL FLRRISPTMH LTLAVCSTRG PPLSKSAPQA
     SLLMQLSHDT GKYSNEYLFS TDNALFGWRG LWNFGPDPRS STDTAAPRLS LLSAGAEAYY
     SPVSSLIGMS TGLRFSTLPA ATDVPASTAT GFATANQSTP ISTFPYTLTL TLTPLTGSLS
     TTYSLRASPN LAFSSRFGFN VYSWESEMVA GCELWRKSRK QDDGLEWARR KMRASEPLSL
     PSLPAESKER QEEEEATDSV LKIRVDQSWN VRVLWEGRVK ELLVSAGVGL GPSDTAFAWM
     YIFSVRAGLN R
 
 
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