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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:Q92328
Protein Name:Mitochondrial distribution and morphology protein 12
Length:271
Molecular Weight:30729.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Location1 / Topology2 / Orientation3: Mitochondrion outer membrane1 / Peripheral membrane protein2 / Cytoplasmic side3
Substrate lipids

Cross database links:

Structure:
5GYD   5GYK   5YK7     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSFDINWSTL ESDNRLNDLI RKHLNSYLQN TQLPSYVSNL RVLDFDLGKV GPAITLKEIT 
61:	DPLDEFYDSI REEADQETEE NNDNKEDSEH ICPDRTIANH EGPKDDFEAP VVMPSPNDIQ 
121:	FLLEVEYKGD LLVTIGADLV LNYPVEKFMT LPVKLSISDI GLHSLCIVAC LSKQLFLSFL 
181:	CDVSDPALDD NQTVLDPKGP ILAATKPLER ISIVRSMKIE TEIGEQYQGQ GSVLRSVGEL 
241:	EQFLFTIFKD FLRKELAWPS WINLDFNDGD E