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Protein

Mitochondrial distribution and morphology protein 12

Gene

MDM12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria (PubMed:19556461). Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria (PubMed:19556461, PubMed:27469264). MDM12 is required for the interaction of the ER-resident membrane protein 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. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids (By similarity) (PubMed:17410204).UniRule annotation3 Publications

Miscellaneous

Present with 1070 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • phosphatidylcholine binding Source: SGD
  • phosphatidylethanolamine binding Source: SGD
  • phosphatidylglycerol binding Source: SGD

GO - Biological processi

  • aminophospholipid transport Source: SGD
  • mitochondrial outer membrane translocase complex assembly Source: SGD
  • mitochondrion-endoplasmic reticulum membrane tethering Source: SGD
  • mitochondrion inheritance Source: SGD
  • phospholipid transport Source: SGD
  • protein import into mitochondrial outer membrane Source: InterPro

Keywordsi

Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33426-MONOMER

Protein family/group databases

TCDBi9.A.58.1.1 the maintenance of mitochondrial morphology (mmm) family

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial distribution and morphology protein 12UniRule annotation
Alternative name(s):
Mitochondrial inheritance component MDM12UniRule annotation
Gene namesi
Name:MDM12UniRule annotation
Ordered Locus Names:YOL009C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL009C
SGDiS000005369 MDM12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000963291 – 271Mitochondrial distribution and morphology protein 12Add BLAST271

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ92328
PaxDbiQ92328
PRIDEiQ92328

PTM databases

iPTMnetiQ92328

Interactioni

Subunit structurei

Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34 (PubMed:13679517, PubMed:17410204, PubMed:19556461). A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking (PubMed:28479252, PubMed:29078410). Interacts with PUF3 (By similarity) (PubMed:17210948).UniRule annotation6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi34395, 400 interactors
DIPiDIP-4188N
IntActiQ92328, 4 interactors
MINTiQ92328
STRINGi4932.YOL009C

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 6Combined sources6
Helixi8 – 11Combined sources4
Helixi16 – 29Combined sources14
Beta strandi37 – 46Combined sources10
Beta strandi49 – 60Combined sources12
Helixi64 – 72Combined sources9
Beta strandi119 – 128Combined sources10
Beta strandi132 – 141Combined sources10
Beta strandi143 – 147Combined sources5
Beta strandi149 – 171Combined sources23
Beta strandi174 – 182Combined sources9
Helixi186 – 188Combined sources3
Helixi200 – 203Combined sources4
Helixi207 – 209Combined sources3
Beta strandi213 – 222Combined sources10
Helixi225 – 227Combined sources3
Helixi231 – 256Combined sources26
Beta strandi262 – 264Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GYDX-ray3.11A/B/C/D1-271[»]
5GYKX-ray3.60A/B/C/D/E/F1-73[»]
A/B/C/D/E/F115-271[»]
5VKZX-ray4.10A/B1-271[»]
5YK7X-ray3.80B/D1-73[»]
B/D115-182[»]
B/D212-271[»]
ProteinModelPortaliQ92328
SMRiQ92328
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 267SMP-LTDUniRule annotationAdd BLAST267

Domaini

The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the MDM12 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000000775
InParanoidiQ92328
KOiK17765
OMAiMSLKIYW
OrthoDBiEOG092C2W17

Family and domain databases

HAMAPiMF_03104 Mdm12, 1 hit
InterProiView protein in InterPro
IPR027532 Mdm12
IPR031468 SMP_LBD
PANTHERiPTHR28204 PTHR28204, 2 hits
PROSITEiView protein in PROSITE
PS51847 SMP, 1 hit

Sequencei

Sequence statusi: Complete.

Q92328-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDINWSTL ESDNRLNDLI RKHLNSYLQN TQLPSYVSNL RVLDFDLGKV
60 70 80 90 100
GPAITLKEIT DPLDEFYDSI REEADQETEE NNDNKEDSEH ICPDRTIANH
110 120 130 140 150
EGPKDDFEAP VVMPSPNDIQ FLLEVEYKGD LLVTIGADLV LNYPVEKFMT
160 170 180 190 200
LPVKLSISDI GLHSLCIVAC LSKQLFLSFL CDVSDPALDD NQTVLDPKGP
210 220 230 240 250
ILAATKPLER ISIVRSMKIE TEIGEQYQGQ GSVLRSVGEL EQFLFTIFKD
260 270
FLRKELAWPS WINLDFNDGD E
Length:271
Mass (Da):30,729
Last modified:September 27, 2004 - v2
Checksum:iD4A89786CE59CAB4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91I → V in AAB17867 (PubMed:9024686).Curated1
Sequence conflicti269G → D in AAB17867 (PubMed:9024686).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62252 Genomic DNA Translation: AAB17867.1
Z74751 Genomic DNA Translation: CAA99008.1
AY558013 Genomic DNA Translation: AAS56339.1
BK006948 Genomic DNA Translation: DAA10774.1
PIRiS66691
RefSeqiNP_014634.1, NM_001183263.1

Genome annotation databases

EnsemblFungiiYOL009C; YOL009C; YOL009C
GeneIDi854153
KEGGisce:YOL009C

Similar proteinsi

Entry informationi

Entry nameiMDM12_YEAST
AccessioniPrimary (citable) accession number: Q92328
Secondary accession number(s): D6W258, Q08064
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2004
Last modified: May 23, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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