P36046 · MIA40_YEAST

Function

function

Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced MIA40 is reoxidized by FAD-linked sulfhydryl oxidase ERV1.

Miscellaneous

Present with 5040 molecules/cell in log phase SD medium.

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Cu2+ or Zn2+.

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 Componentmitochondrial inner membrane
Cellular Componentmitochondrial intermembrane space
Cellular Componentmitochondrion
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionoxidoreductase activity
Molecular Functionprotein disulfide isomerase activity
Molecular Functionprotein-disulfide reductase activity
Molecular Functionthiol oxidase activity
Biological Processprotein folding
Biological Processprotein import into mitochondrial intermembrane space
Biological Processprotein maturation by protein folding

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitochondrial intermembrane space import and assembly protein 40
  • Alternative names
    • Mitochondrial import inner membrane translocase TIM40

Gene names

    • Name
      MIA40
    • Synonyms
      TIM40
    • Ordered locus names
      YKL195W

Organism names

Accessions

  • Primary accession
    P36046
  • Secondary accessions
    • D6VX05

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain33-46Mitochondrial matrix
Transmembrane47-66Helical; Signal-anchor for type II membrane protein
Topological domain67-403Mitochondrial intermembrane

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis296Loss of function; when associated with S-298.
Mutagenesis298Loss of function; when associated with S-296.
Mutagenesis307Loss of function; when associated with S-317.
Mutagenesis317Loss of function; when associated with S-307.
Mutagenesis330Loss of function; when associated with S-340.
Mutagenesis340Loss of function; when associated with S-330.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain, disulfide bond.

TypeIDPosition(s)Description
Transit peptide1-31Mitochondrion
ChainPRO_000020313532-403Mitochondrial intermembrane space import and assembly protein 40
Disulfide bond296↔298Redox-active
Disulfide bond307↔340
Disulfide bond317↔330

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Monomer. Interacts with the FAD-linked sulfhydryl oxidase ERV1 and with the substrate proteins COX17, TIM9, and TIM13, forming transient intermolecular disulfide bridges. Interacts with FCJ1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P36046ATP23 P537225EBI-26978, EBI-8059929
BINARY P36046ERV1 P278824EBI-26978, EBI-6621

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region75-292Disordered
Compositional bias97-118Basic and acidic residues
Compositional bias140-172Basic and acidic residues
Compositional bias202-245Basic and acidic residues
Compositional bias252-284Basic and acidic residues
Domain304-348CHCH
Motif307-317Cx9C motif 1
Motif330-340Cx9C motif 2
Compositional bias351-366Basic and acidic residues
Region351-403Disordered
Compositional bias368-383Polar residues
Compositional bias384-403Basic and acidic residues

Domain

The CHCH domain contains a conserved twin Cys-X9-Cys motif which is required for import and stability of MIA40 in mitochondria.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    403
  • Mass (Da)
    44,536
  • Last updated
    2006-03-21 v2
  • Checksum
    5904E8D0213D6EFA
MLRNLVVRNACRNRPSIQVARGLCRHQTRRLMASSPQFGRNSNQEKTAGFIMGILSMAGALYFIAPNRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHYAEQLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias97-118Basic and acidic residues
Compositional bias140-172Basic and acidic residues
Compositional bias202-245Basic and acidic residues
Compositional bias252-284Basic and acidic residues
Compositional bias351-366Basic and acidic residues
Compositional bias368-383Polar residues
Compositional bias384-403Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z28195
EMBL· GenBank· DDBJ
CAA82039.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006944
EMBL· GenBank· DDBJ
DAA08971.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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