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Protein

Mitochondrial distribution and morphology protein 10

Gene

MDM10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.UniRule annotation7 Publications

GO - Biological processi

  • establishment of mitochondrion localization Source: SGD
  • mitochondrial genome maintenance Source: UniProtKB-HAMAP
  • mitochondrial outer membrane translocase complex assembly Source: SGD
  • mitochondrion-ER tethering Source: SGD
  • mitochondrion organization Source: SGD
  • phospholipid transport Source: SGD
  • protein import into mitochondrial outer membrane Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-28823-MONOMER.

Protein family/group databases

TCDBi1.B.33.3.1. the outer membrane protein insertion porin (bam complex) (ompip) family.
1.B.8.6.1. the mitochondrial and plastid porin (mpp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial distribution and morphology protein 10UniRule annotation
Alternative name(s):
Mitochondrial inheritance component MDM10UniRule annotation
Gene namesi
Name:MDM10UniRule annotation
Ordered Locus Names:YAL010C
ORF Names:FUN37
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL010C.
SGDiS000000008. MDM10.

Subcellular locationi

GO - Cellular componenti

  • ERMES complex Source: SGD
  • integral component of mitochondrial outer membrane Source: UniProtKB-HAMAP
  • mitochondrial sorting and assembly machinery complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Mitochondrial distribution and morphology protein 10PRO_0000096327Add
BLAST

Proteomic databases

MaxQBiP18409.

Interactioni

Subunit structurei

Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates with the mitochondrial outer membrane sorting assembly machinery SAM(core) complex, which consists of SAM35, SAM37 and SAM50, to form a SAM(holo) complex.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM12Q923284EBI-10580,EBI-10584
SAM35P146935EBI-10580,EBI-24602
SAM50P539694EBI-10580,EBI-28646

Protein-protein interaction databases

BioGridi31756. 190 interactions.
DIPiDIP-6697N.
IntActiP18409. 14 interactions.
MINTiMINT-626988.

Family & Domainsi

Domaini

Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.

Sequence similaritiesi

Belongs to the MDM10 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane beta strand

Phylogenomic databases

HOGENOMiHOG000177242.
InParanoidiP18409.
KOiK17774.
OMAiNTMGTKD.
OrthoDBiEOG7B05QC.

Family and domain databases

HAMAPiMF_03102. Mdm10.
InterProiIPR027539. Mdm10.
[Graphical view]
PfamiPF12519. MDM10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPYMDQVLR AFYQSTHWST QNSYEDITAT SRTLLDFRIP SAIHLQISNK
60 70 80 90 100
STPNTFNSLD FSTRSRINGS LSYLYSDAQQ LEKFMRNSTD IPLQDATETY
110 120 130 140 150
RQLQPNLNFS VSSANTLSSD NTTVDNDKKL LHDSKFVKKS LYYGRMYYPS
160 170 180 190 200
SDLEAMIIKR LSPQTQFMLK GVSSFKESLN VLTCYFQRDS HRNLQEWIFS
210 220 230 240 250
TSDLLCGYRV LHNFLTTPSK FNTSLYNNSS LSLGAEFWLG LVSLSPGCST
260 270 280 290 300
TLRYYTHSTN TGRPLTLTLS WNPLFGHISS TYSAKTGTNS TFCAKYDFNL
310 320 330 340 350
YSIESNLSFG CEFWQKKHHL LETNKNNNDK LEPISDELVD INPNSRATKL
360 370 380 390 400
LHENVPDLNS AVNDIPSTLD IPVHKQKLLN DLTYAFSSSL RKIDEERSTI
410 420 430 440 450
EKFDNKINSS IFTSVWKLST SLRDKTLKLL WEGKWRGFLI SAGTELVFTR
460 470 480 490
GFQESLSDDE KNDNAISISA TDTENGNIPV FPAKFGIQFQ YST
Length:493
Mass (Da):56,237
Last modified:July 27, 2011 - v5
Checksum:i5AE98366B5EF25E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2721N → Q no nucleotide entry (PubMed:7941740).Curated
Sequence conflicti272 – 2721N → Q in AAC04948 (PubMed:7731988).Curated
Sequence conflicti272 – 2721N → Q in AAC04947 (PubMed:8458570).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80874 Genomic DNA. Translation: CAA56842.1.
L22015 Genomic DNA. Translation: AAC04948.1.
M36073 Genomic DNA. Translation: AAA35072.2.
L05146 Genomic DNA. Translation: AAC04947.1.
BK006935 Genomic DNA. Translation: DAA06978.2.
PIRiPS0157.
RefSeqiNP_009392.2. NM_001178155.2.

Genome annotation databases

EnsemblFungiiYAL010C; YAL010C; YAL010C.
GeneIDi851223.
KEGGisce:YAL010C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80874 Genomic DNA. Translation: CAA56842.1.
L22015 Genomic DNA. Translation: AAC04948.1.
M36073 Genomic DNA. Translation: AAA35072.2.
L05146 Genomic DNA. Translation: AAC04947.1.
BK006935 Genomic DNA. Translation: DAA06978.2.
PIRiPS0157.
RefSeqiNP_009392.2. NM_001178155.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31756. 190 interactions.
DIPiDIP-6697N.
IntActiP18409. 14 interactions.
MINTiMINT-626988.

Protein family/group databases

TCDBi1.B.33.3.1. the outer membrane protein insertion porin (bam complex) (ompip) family.
1.B.8.6.1. the mitochondrial and plastid porin (mpp) family.

Proteomic databases

MaxQBiP18409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL010C; YAL010C; YAL010C.
GeneIDi851223.
KEGGisce:YAL010C.

Organism-specific databases

EuPathDBiFungiDB:YAL010C.
SGDiS000000008. MDM10.

Phylogenomic databases

HOGENOMiHOG000177242.
InParanoidiP18409.
KOiK17774.
OMAiNTMGTKD.
OrthoDBiEOG7B05QC.

Enzyme and pathway databases

BioCyciYEAST:G3O-28823-MONOMER.

Miscellaneous databases

NextBioi968124.
PROiP18409.

Family and domain databases

HAMAPiMF_03102. Mdm10.
InterProiIPR027539. Mdm10.
[Graphical view]
PfamiPF12519. MDM10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane."
    Sogo L.F., Yaffe M.P.
    J. Cell Biol. 126:1361-1373(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: MYY290.
  2. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
    Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
    Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 272.
    Strain: ATCC 204508 / S288c.
  5. "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: isolation, characterization and regulation of the SPO7 sporulation gene."
    Whyte W., Koepp L.H., Lamb J., Crowley J.C., Kaback D.B.
    Gene 95:65-72(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
  6. "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
    Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
    Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-493.
    Strain: ATCC 204511 / S288c / AB972.
  7. "Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p."
    Boldogh I.R., Vojtov N., Karmon S., Pon L.A.
    J. Cell Biol. 141:1371-1381(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Maintenance of mitochondrial morphology is linked to maintenance of the mitochondrial genome in Saccharomyces cerevisiae."
    Hanekamp T., Thorsness M.K., Rebbapragada I., Fisher E.M., Seebart C., Darland M.R., Coxbill J.A., Updike D.L., Thorsness P.E.
    Genetics 162:1147-1156(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery."
    Boldogh I.R., Nowakowski D.W., Yang H.-C., Chung H., Karmon S., Royes P., Pon L.A.
    Mol. Biol. Cell 14:4618-4627(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MDM10/MDM12/MMM1 COMPLEX, SUBCELLULAR LOCATION.
  10. "Machinery for protein sorting and assembly in the mitochondrial outer membrane."
    Wiedemann N., Kozjak V., Chacinska A., Schoenfisch B., Rospert S., Ryan M.T., Pfanner N., Meisinger C.
    Nature 424:565-571(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE BETA-BARREL TOPOLOGY.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Evolutionary conservation of biogenesis of beta-barrel membrane proteins."
    Paschen S.A., Waizenegger T., Stan T., Preuss M., Cyrklaff M., Hell K., Rapaport D., Neupert W.
    Nature 426:862-866(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE TOPOLOGY BETA-BARREL.
  14. "The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane."
    Meisinger C., Rissler M., Chacinska A., Szklarz L.K., Milenkovic D., Kozjak V., Schonfisch B., Lohaus C., Meyer H.E., Yaffe M.P., Guiard B., Wiedemann N., Pfanner N.
    Dev. Cell 7:61-71(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN SAM COMPLEX.
  15. "Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10."
    Meisinger C., Wiedemann N., Rissler M., Strub A., Milenkovic D., Schoenfisch B., Mueller H., Kozjak V., Pfanner N.
    J. Biol. Chem. 281:22819-22826(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
    Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
    Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria."
    Meisinger C., Pfannschmidt S., Rissler M., Milenkovic D., Becker T., Stojanovski D., Youngman M.J., Jensen R.E., Chacinska A., Guiard B., Pfanner N., Wiedemann N.
    EMBO J. 26:2229-2239(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN MDM10/MDM12/MMM1 AND SAM COMPLEXES.
  18. "An ER-mitochondria tethering complex revealed by a synthetic biology screen."
    Kornmann B., Currie E., Collins S.R., Schuldiner M., Nunnari J., Weissman J.S., Walter P.
    Science 325:477-481(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN ERMES/MDM COMPLEX, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMDM10_YEAST
AccessioniPrimary (citable) accession number: P18409
Secondary accession number(s): D6VPK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 27, 2011
Last modified: November 11, 2015
This is version 124 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.