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1.B.33.3.1
The mitochondrial Sorting and Assembly Machinery (SAM) includes SAM50, Tom37 (Mas37; Sam37), Tom13 (Mim1), Mim2, and porin; see 3.A.8 (Paschen et al., 2005). The MIM complex can assemble N- and C-terminal α-helical anchor proteins. SAM and TOM insert β-barrel proteins in the outer mitochondrial membrane (Stojanovski et al., 2007). Mim1 (Tom13) is required for the biogenesis of the beta-barrel protein Tom40 and also for membrane insertion and assembly of signal- and C-terminally-anchored Tom receptors (Becker et al., 2008; 2011). It has cation-selective ion transport activity (Checchetto and Szabo 2018; Krüger et al. 2017). Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40 (Yamano et al., 2010). Homologous Omp85 proteins are essential for membrane insertion of β-barrel precursors. Precursors are apparently threaded through the Omp85-channel interior and exit laterally. Höhr et al. 2018  mapped the interaction of a precursor in transit with the mitochondrial Omp85-channel Sam50 in the native membrane environment. The precursor is translocated into the channel interior, interacts with an internal loop, and inserts into the lateral gate by β-signal exchange. Transport through the Omp85-channel interior followed by release through the lateral gate into the lipid phase represents a basic mechanism for membrane insertion of β-barrel proteins (Höhr et al. 2018). The TOM and SAM complexes cooperate in the import of beta-barrel proteins, whereas the mitochondrial import  (MIM) complex (Mim1/Mim2/porin) inserts precursors of multi-spanning alpha-helical proteins. Single-spanning proteins constitute more than half of the integral outer membrane proteins. Doan et al. 2020 reported that the yeast MIM complex promotes the insertion of proteins with N-terminal (signal-anchored) or C-terminal (tail-anchored) membrane anchors. The MIM complex exists in three dynamic populations. MIM interacts with TOM to accept precursor proteins from the receptor Tom70. Free MIM complexes insert single-spanning proteins that are imported in a Tom70-independent manner. Finally, coupling of MIM and SAM promotes early assembly steps of TOM subunits. Thus, the MIM complex is a major and versatile protein translocase of the mitochondrial outer membrane (Doan et al. 2020).

Accession Number:P18409
Protein Name:Mdm10
Length:493
Molecular Weight:56237.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion outer membrane1 / Multi-pass membrane protein2
Substrate proteins

Cross database links:

DIP: DIP-6697N
RefSeq: NP_009392.1   
Entrez Gene ID: 851223   
Pfam: PF12519   
KEGG: sce:YAL010C   

Gene Ontology

GO:0032865 C:ERMES complex
GO:0016021 C:integral to membrane
GO:0001401 C:mitochondrial sorting and assembly machiner...
GO:0000002 P:mitochondrial genome maintenance
GO:0000001 P:mitochondrion inheritance
GO:0015914 P:phospholipid transport
GO:0006461 P:protein complex assembly
GO:0045040 P:protein import into mitochondrial outer mem...

References (16)

[1] “Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane.”  Sogo L.F.et.al.   8089171
[2] “Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region.”  Clark M.W.et.al.   7941740
[3] “The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.”  Bussey H.et.al.   7731988
[4] “Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: isolation, characterization and regulation of the SPO7 sporulation gene.”  Whyte W.et.al.   2253888
[5] “Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes.”  Ouellette B.F.F.et.al.   8458570
[6] “Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p.”  Boldogh I.R.et.al.   9628893
[7] “Maintenance of mitochondrial morphology is linked to maintenance of the mitochondrial genome in Saccharomyces cerevisiae.”  Hanekamp T.et.al.   12454062
[8] “A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery.”  Boldogh I.R.et.al.   13679517
[9] “Machinery for protein sorting and assembly in the mitochondrial outer membrane.”  Wiedemann N.et.al.   12891361
[10] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[11] “Evolutionary conservation of biogenesis of beta-barrel membrane proteins.”  Paschen S.A.et.al.   14685243
[12] “The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane.”  Meisinger C.et.al.   15239954
[13] “Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10.”  Meisinger C.et.al.   16760475
[14] “Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.”  Zahedi R.P.et.al.   16407407
[15] “The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.”  Meisinger C.et.al.   17410204
[16] “An ER-mitochondria tethering complex revealed by a synthetic biology screen.”  Kornmann B.et.al.   19556461

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FASTA formatted sequence
1:	MLPYMDQVLR AFYQSTHWST QNSYEDITAT SRTLLDFRIP SAIHLQISNK STPNTFNSLD 
61:	FSTRSRINGS LSYLYSDAQQ LEKFMRNSTD IPLQDATETY RQLQPNLNFS VSSANTLSSD 
121:	NTTVDNDKKL LHDSKFVKKS LYYGRMYYPS SDLEAMIIKR LSPQTQFMLK GVSSFKESLN 
181:	VLTCYFQRDS HRNLQEWIFS TSDLLCGYRV LHNFLTTPSK FNTSLYNNSS LSLGAEFWLG 
241:	LVSLSPGCST TLRYYTHSTN TGRPLTLTLS WNPLFGHISS TYSAKTGTNS TFCAKYDFNL 
301:	YSIESNLSFG CEFWQKKHHL LETNKNNNDK LEPISDELVD INPNSRATKL LHENVPDLNS 
361:	AVNDIPSTLD IPVHKQKLLN DLTYAFSSSL RKIDEERSTI EKFDNKINSS IFTSVWKLST 
421:	SLRDKTLKLL WEGKWRGFLI SAGTELVFTR GFQESLSDDE KNDNAISISA TDTENGNIPV 
481:	FPAKFGIQFQ YST