A1CM86 · MMM1_ASPCL

Function

function

Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. 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. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all 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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentERMES complex
Molecular Functionlipid binding
Biological Processmitochondrial genome maintenance
Biological Processmitochondrion-endoplasmic reticulum membrane tethering
Biological Processphospholipid transport
Biological Processprotein insertion into mitochondrial outer membrane

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Maintenance of mitochondrial morphology protein 1

Gene names

    • Name
      mmm1
    • ORF names
      ACLA_096060

Organism names

Accessions

  • Primary accession
    A1CM86

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type I membrane protein
Note: The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-22Lumenal
Transmembrane23-43Helical
Topological domain44-494Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003842121-494Maintenance of mitochondrial morphology protein 1

Interaction

Subunit

Homodimer. Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34. 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.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region50-98Disordered
Compositional bias60-98Polar residues
Domain130-387SMP-LTD
Region274-330Disordered
Compositional bias303-330Polar residues
Region398-426Disordered
Compositional bias402-416Polar residues
Region449-494Disordered
Compositional bias450-480Polar residues

Domain

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.

Sequence similarities

Belongs to the MMM1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    53,099
  • Last updated
    2007-01-23 v1
  • Checksum
    283DF95B427E2274
MSSQPGDPATLPAQSSLSFTQGFLLGQLSVVLVLAAFIKFFIFGEAPPPPSRGLSHRSATHRRSNSIYSNSPQEAGSRSLREKPSTSNVLRPVPSSSTNTRSILRKTYYSAIPTNPAKHGRLRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYSLKDSPTSSILNSLTAALNNPEKKPAFIDKITVTDISLGEEFPIFSNCRIIAVDDPNSDGGRLQALMDVDLSDDNLSIAIETQLLLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLDTPSHSPSPPTADTATSGRSKPGDKAGGNQPRSNGSTEDPAGGNPPKTSPKSNVAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVQAWFEERVVEPRVQVVGLPDLWPRMGRTGVRTGDDAETASNGPRSTVSADIGGSARHEELAREPEALRFRGLLGARPPFDVASRTSSFNVETGDLRSRSMTRQESSGDLSDQLHIPGSLPEAVTPG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias60-98Polar residues
Compositional bias303-330Polar residues
Compositional bias402-416Polar residues
Compositional bias450-480Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027058
EMBL· GenBank· DDBJ
EAW08673.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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