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Reviewed, UniProtKB/Swiss-Prot P36046 (MIA40_YEAST)

Last modified November 24, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mitochondrial intermembrane space import and assembly protein 40
Alternative name(s):
    Mitochondrial import inner membrane translocase TIM40
Gene names
Name: MIA40
Synonyms: TIM40
Ordered Locus Names: YKL195W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10

Cofactor

Copper or zinc.

Subunit structure

Monomer. Interacts with the FAD-linked sulfhydryl oxidase ERV1 and with the substrate proteins COX17, TIM9, and TIM13, forming transient intermolecular disulfide bridges. Ref.2 Ref.7 Ref.9 Ref.10

Subcellular location

Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side.

Domain

The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria Probable.

Miscellaneous

Present with 5040 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Contains 1 CHCH domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion Ref.2
Chain32 – 403372Mitochondrial intermembrane space import and assembly protein 40
PRO_0000203135

Regions

Topological domain33 – 4614Mitochondrial matrix Potential
Transmembrane47 – 6620Signal-anchor for type II membrane protein Potential
Topological domain67 – 403337Mitochondrial intermembrane Potential
Domain300 – 34344CHCH

Amino acid modifications

Modified residue3721Phosphoserine Ref.12

Experimental info

Mutagenesis2961C → S: Loss of function; when associated with S-298. Ref.2 Ref.8
Mutagenesis2981C → S: Loss of function; when associated with S-296. Ref.2 Ref.8
Mutagenesis3071C → S: Loss of function; when associated with S-317. Ref.2 Ref.8
Mutagenesis3171C → S: Loss of function; when associated with S-307. Ref.8
Mutagenesis3301C → S: Loss of function; when associated with S-340. Ref.8
Mutagenesis3401C → S: Loss of function; when associated with S-330. Ref.8

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Sequences

Sequence LengthMass (Da)Tools
P36046-1 [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: 5904E8D0213D6EFA

FASTA40344,536
        10         20         30         40         50         60 
MLRNLVVRNA CRNRPSIQVA RGLCRHQTRR LMASSPQFGR NSNQEKTAGF IMGILSMAGA 

        70         80         90        100        110        120 
LYFIAPNRKP LFASRKVESD KTAEEELSSG GEQSPENEDD NNSKSDENGD DNDSKNDETE 

       130        140        150        160        170        180 
AGPQLGGDKI GASKVAEDGE LVVLAEEDNK SSEDKDTDES KVSTKDDEQS NEDNATANNQ 

       190        200        210        220        230        240 
KDENISSENS EENTSDKTLD NNAGSSEKKD PEHSDDEKSQ QGQSDDKTTT EDNNGEEESS 

       250        260        270        280        290        300 
KKTVSDSENS AKQSESSDEE KEELRKQEEK QMGPTEEEVQ HEGAYNPDTG EINWDCPCLG 

       310        320        330        340        350        360 
GMAHGPCGEE FKSAFSCFVY SEAEPKGIDC VEKFQHMQDC FRKYPEHYAE QLKETSDDEE 

       370        380        390        400 
PQDKVKVNTI ESAPNVSSAK ENAAKKAEQS DVKKEPLNEE SKP

« Hide

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References

« Hide 'large scale' references
[1]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions."
Terziyska N., Lutz T., Kozany C., Mokranjac D., Mesecke N., Neupert W., Herrmann J.M., Hell K.
FEBS Lett. 579:179-184(2005) [PubMed: 15620710] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-36, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIM13, MUTAGENESIS OF CYS-296; CYS-298 AND CYS-307, METAL-BINDING.
[3]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed: 12748633] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins."
Chacinska A., Pfannschmidt S., Wiedemann N., Kozjak V., Sanjuan Szklarz L.K., Schulze-Specking A., Truscott K.N., Guiard B., Meisinger C., Pfanner N.
EMBO J. 23:3735-3746(2004) [PubMed: 15359280] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIM9.
[8]"Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space."
Naoe M., Ohwa Y., Ishikawa D., Ohshima C., Nishikawa S., Yamamoto H., Endo T.
J. Biol. Chem. 279:47815-47821(2004) [PubMed: 15364952] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-296; CYS-298; CYS-307; CYS-317; CYS-330 AND CYS-340.
[9]"A disulfide relay system in the intermembrane space of mitochondria that mediates protein import."
Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., Herrmann J.M.
Cell 121:1059-1069(2005) [PubMed: 15989955] [Abstract]
Cited for: FUNCTION, INTERACTION WITH COX17; ERV1 AND TIM13.
[10]"The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins."
Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., Chacinska A.
J. Mol. Biol. 353:485-492(2005) [PubMed: 16181637] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERV1.
[11]"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: 16407407] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Z28195 Genomic DNA. Translation: CAA82039.1.
PIRS38032.
RefSeqNP_012726.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ZXTX-ray3.00A284-365[»]
3A3CX-ray2.50A284-353[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5432N.
IntActP36046. 61 interactions.
STRINGP36046.

Protein family/group databases

TCDB3.A.8.1.1. mitochondrial protein translocase (MPT) family.

Proteomic databases

PeptideAtlasP36046.
PRIDEP36046.

Genome annotation databases

EnsemblYKL195W; YKL195W; YKL195W; Saccharomyces cerevisiae. [Genome view]
GeneID853639.
KEGGsce:YKL195W.
NMPDRfig|4932.3.peg.3703.

Organism-specific databases

CYGDYKL195w.
SGDS000001678. MIA40.

Phylogenomic databases

HOGENOMP36046.
OrthoDBEOG96Q88T

Gene expression databases

ArrayExpressP36046.
GenevestigatorP36046.
GermOnlineYKL195W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR010625. CHCH.
[Graphical view]
PfamPF06747. CHCH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio974528.

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Entry information

Entry nameMIA40_YEAST
AccessionPrimary (citable) accession number: P36046
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 21, 2006
Last modified: November 24, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents