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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:P14693
Protein Name:SAM35
Length:329
Molecular Weight:37404.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion outer membrane1
Substrate proteins

Cross database links:

DIP: DIP-1879N
RefSeq: NP_011951.1   
Entrez Gene ID: 856483   
Pfam: PF10806   
KEGG: sce:YHR083W   

Gene Ontology

GO:0001401 C:mitochondrial sorting and assembly machiner...
GO:0005515 F:protein binding
GO:0070096 P:mitochondrial outer membrane translocase co...
GO:0045040 P:protein import into mitochondrial outer mem...

References (7)

[1] “Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.”  Johnston M.et.al.   8091229
[2] “STE12, a protein involved in cell-type-specific transcription and signal transduction in yeast, is part of protein-DNA complexes.”  Errede B.et.al.   2558054
[3] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[4] “Tob38, a novel essential component in the biogenesis of beta-barrel proteins of mitochondria.”  Waizenegger T.et.al.   15205677
[5] “The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.”  Gentle I.et.al.   14699090
[6] “Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.”  Ishikawa D.et.al.   15326197
[7] “Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability.”  Milenkovic D.et.al.   15067005

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FASTA formatted sequence
1:	MVSSFSVPMP VKRIFDTFPL QTYAAQTDKD EAVALEIQRR SYTFTERGGG SSELTVEGTY 
61:	KLGVYNVFLE ANTGAALATD PWCLFVQLAL CQKNGLVLPT HSQEQTPSHT CNHEMLVLSR 
121:	LSNPDEALPI LVEGYKKRII RSTVAISEIM RSRILDDAEQ LMYYTLLDTV LYDCWITQII 
181:	FCASDAQFME LYSCQKLSGS IVTPLDVENS LLQKLSAKSL KISLTKRNKF QFRHREIVKS 
241:	MQGVYHNHHN SVNQEQVLNV LFENSKQVLL GLKDMLKSDG QPTYLHLKIA SYILCITNVK 
301:	EPIKLKTFVE NECKELVQFA QDTLKNFVQ