P36046 · MIA40_YEAST
- ProteinMitochondrial intermembrane space import and assembly protein 40
- GeneMIA40
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids403 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Cu2+ or Zn2+.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrion | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | protein disulfide isomerase activity | |
Molecular Function | protein-disulfide reductase activity | |
Molecular Function | thiol oxidase activity | |
Biological Process | protein folding | |
Biological Process | protein import into mitochondrial intermembrane space | |
Biological Process | protein maturation by protein folding |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial intermembrane space import and assembly protein 40
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP36046
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 33-46 | Mitochondrial matrix | ||||
Sequence: ASSPQFGRNSNQEK | ||||||
Transmembrane | 47-66 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TAGFIMGILSMAGALYFIAP | ||||||
Topological domain | 67-403 | Mitochondrial intermembrane | ||||
Sequence: NRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHYAEQLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 296 | Loss of function; when associated with S-298. | ||||
Sequence: C → S | ||||||
Mutagenesis | 298 | Loss of function; when associated with S-296. | ||||
Sequence: C → S | ||||||
Mutagenesis | 307 | Loss of function; when associated with S-317. | ||||
Sequence: C → S | ||||||
Mutagenesis | 317 | Loss of function; when associated with S-307. | ||||
Sequence: C → S | ||||||
Mutagenesis | 330 | Loss of function; when associated with S-340. | ||||
Sequence: C → S | ||||||
Mutagenesis | 340 | Loss of function; when associated with S-330. | ||||
Sequence: C → S |
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.
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-31 | Mitochondrion | ||||
Sequence: MLRNLVVRNACRNRPSIQVARGLCRHQTRRL | ||||||
Chain | PRO_0000203135 | 32-403 | Mitochondrial intermembrane space import and assembly protein 40 | |||
Sequence: MASSPQFGRNSNQEKTAGFIMGILSMAGALYFIAPNRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHYAEQLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP | ||||||
Disulfide bond | 296↔298 | Redox-active | ||||
Sequence: CPC | ||||||
Disulfide bond | 307↔340 | |||||
Sequence: CGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDC | ||||||
Disulfide bond | 317↔330 | |||||
Sequence: CFVYSEAEPKGIDC |
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P36046 | ATP23 P53722 | 5 | EBI-26978, EBI-8059929 | |
BINARY | P36046 | ERV1 P27882 | 4 | EBI-26978, EBI-6621 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 75-292 | Disordered | ||||
Sequence: RKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEI | ||||||
Compositional bias | 97-118 | Basic and acidic residues | ||||
Sequence: NEDDNNSKSDENGDDNDSKNDE | ||||||
Compositional bias | 140-172 | Basic and acidic residues | ||||
Sequence: ELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNE | ||||||
Compositional bias | 202-245 | Basic and acidic residues | ||||
Sequence: NAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVS | ||||||
Compositional bias | 252-284 | Basic and acidic residues | ||||
Sequence: KQSESSDEEKEELRKQEEKQMGPTEEEVQHEGA | ||||||
Domain | 304-348 | CHCH | ||||
Sequence: HGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHY | ||||||
Motif | 307-317 | Cx9C motif 1 | ||||
Sequence: CGEEFKSAFSC | ||||||
Motif | 330-340 | Cx9C motif 2 | ||||
Sequence: CVEKFQHMQDC | ||||||
Compositional bias | 351-366 | Basic and acidic residues | ||||
Sequence: QLKETSDDEEPQDKVK | ||||||
Region | 351-403 | Disordered | ||||
Sequence: QLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP | ||||||
Compositional bias | 368-383 | Polar residues | ||||
Sequence: NTIESAPNVSSAKENA | ||||||
Compositional bias | 384-403 | Basic and acidic residues | ||||
Sequence: AKKAEQSDVKKEPLNEESKP |
Domain
The CHCH domain contains a conserved twin Cys-X9-Cys motif which is required for import and stability of MIA40 in mitochondria.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length403
- Mass (Da)44,536
- Last updated2006-03-21 v2
- Checksum5904E8D0213D6EFA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 97-118 | Basic and acidic residues | ||||
Sequence: NEDDNNSKSDENGDDNDSKNDE | ||||||
Compositional bias | 140-172 | Basic and acidic residues | ||||
Sequence: ELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNE | ||||||
Compositional bias | 202-245 | Basic and acidic residues | ||||
Sequence: NAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVS | ||||||
Compositional bias | 252-284 | Basic and acidic residues | ||||
Sequence: KQSESSDEEKEELRKQEEKQMGPTEEEVQHEGA | ||||||
Compositional bias | 351-366 | Basic and acidic residues | ||||
Sequence: QLKETSDDEEPQDKVK | ||||||
Compositional bias | 368-383 | Polar residues | ||||
Sequence: NTIESAPNVSSAKENA | ||||||
Compositional bias | 384-403 | Basic and acidic residues | ||||
Sequence: AKKAEQSDVKKEPLNEESKP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z28195 EMBL· GenBank· DDBJ | CAA82039.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA08971.1 EMBL· GenBank· DDBJ | Genomic DNA |