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9.A.58.1.1
The TULIP complex is a major mediator of lipid sensing and transport in eukaryotes (Alva and Lupas 2016). Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria include MMM1, MMM2 (MDM34), MDM10 and MDM12. This complex is involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM34 (MMM2) is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. MDM12 is required for the interaction of MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex (TC# 1.B.33). The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway (TC# 1.B.8) after the action of the MDM12-MMM1 complex (Meisinger et al. 2007).  Discrete sites of close apposition between ER and mitochondria may facilitate interorganelle calcium and phospholipid exchange (Kornmann et al. 2009).  See family description for more details and additional references.

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 lipids

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