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Mitochondrial intermembrane space import and assembly protein 40 (Mitochondrial import inner membrane translocase TIM40)

 MIA40_YEAST             Reviewed;         403 AA.
P36046; D6VX05;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=Mitochondrial intermembrane space import and assembly protein 40;
AltName: Full=Mitochondrial import inner membrane translocase TIM40;
Flags: Precursor;
Name=MIA40; Synonyms=TIM40; OrderedLocusNames=YKL195W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
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., 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.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 32-36, FUNCTION, SUBCELLULAR LOCATION, INTERACTION
WITH TIM13, MUTAGENESIS OF CYS-296; CYS-298 AND CYS-307, AND
METAL-BINDING.
PubMed=15620710; DOI=10.1016/j.febslet.2004.11.072;
Terziyska N., Lutz T., Kozany C., Mokranjac D., Mesecke N.,
Neupert W., Herrmann J.M., Hell K.;
"Mia40, a novel factor for protein import into the intermembrane space
of mitochondria is able to bind metal ions.";
FEBS Lett. 579:179-184(2005).
[4]
IDENTIFICATION OF PROBABLE INITIATION SITE.
PubMed=12748633; DOI=10.1038/nature01644;
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and
regulatory elements.";
Nature 423:241-254(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
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.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIM9.
PubMed=15359280; DOI=10.1038/sj.emboj.7600389;
Chacinska A., Pfannschmidt S., Wiedemann N., Kozjak V.,
Sanjuan Szklarz L.K., Schulze-Specking A., Truscott K.N., Guiard B.,
Meisinger C., Pfanner N.;
"Essential role of Mia40 in import and assembly of mitochondrial
intermembrane space proteins.";
EMBO J. 23:3735-3746(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-296; CYS-298;
CYS-307; CYS-317; CYS-330 AND CYS-340.
PubMed=15364952; DOI=10.1074/jbc.M410272200;
Naoe M., Ohwa Y., Ishikawa D., Ohshima C., Nishikawa S., Yamamoto H.,
Endo T.;
"Identification of Tim40 that mediates protein sorting to the
mitochondrial intermembrane space.";
J. Biol. Chem. 279:47815-47821(2004).
[10]
FUNCTION, AND INTERACTION WITH COX17; ERV1 AND TIM13.
PubMed=15989955; DOI=10.1016/j.cell.2005.04.011;
Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K.,
Herrmann J.M.;
"A disulfide relay system in the intermembrane space of mitochondria
that mediates protein import.";
Cell 121:1059-1069(2005).
[11]
FUNCTION, AND INTERACTION WITH ERV1.
PubMed=16181637; DOI=10.1016/j.jmb.2005.08.051;
Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B.,
Pfanner N., Chacinska A.;
"The essential mitochondrial protein Erv1 cooperates with Mia40 in
biogenesis of intermembrane space proteins.";
J. Mol. Biol. 353:485-492(2005).
[12]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16407407; DOI=10.1091/mbc.E05-08-0740;
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals
accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
[13]
INTERACTION WITH FCJ1.
PubMed=21944719; DOI=10.1016/j.devcel.2011.08.026;
von der Malsburg K., Muller J.M., Bohnert M., Oeljeklaus S.,
Kwiatkowska P., Becker T., Loniewska-Lwowska A., Wiese S., Rao S.,
Milenkovic D., Hutu D.P., Zerbes R.M., Schulze-Specking A.,
Meyer H.E., Martinou J.C., Rospert S., Rehling P., Meisinger C.,
Veenhuis M., Warscheid B., van der Klei I.J., Pfanner N.,
Chacinska A., van der Laan M.;
"Dual role of mitofilin in mitochondrial membrane organization and
protein biogenesis.";
Dev. Cell 21:694-707(2011).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 284-353, FUNCTION, AND
DISULFIDE BONDS.
PubMed=19667201; DOI=10.1073/pnas.0901793106;
Kawano S., Yamano K., Naoe M., Momose T., Terao K., Nishikawa S.,
Watanabe N., Endo T.;
"Structural basis of yeast Tim40/Mia40 as an oxidative translocator in
the mitochondrial intermembrane space.";
Proc. Natl. Acad. Sci. U.S.A. 106:14403-14407(2009).
-!- 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. {ECO:0000269|PubMed:15359280,
ECO:0000269|PubMed:15364952, ECO:0000269|PubMed:15620710,
ECO:0000269|PubMed:15989955, ECO:0000269|PubMed:16181637,
ECO:0000269|PubMed:19667201}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Cu(2+) or Zn(2+).;
-!- 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. {ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15620710,
ECO:0000269|PubMed:15989955, ECO:0000269|PubMed:16181637,
ECO:0000269|PubMed:21944719}.
-!- INTERACTION:
P53722:ATP23; NbExp=5; IntAct=EBI-26978, EBI-8059929;
P27882:ERV1; NbExp=2; IntAct=EBI-26978, EBI-6621;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15364952,
ECO:0000269|PubMed:15620710, ECO:0000269|PubMed:16407407}; Single-
pass type II membrane protein {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15359280,
ECO:0000269|PubMed:15364952, ECO:0000269|PubMed:15620710,
ECO:0000269|PubMed:16407407}; Intermembrane side
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:15359280, ECO:0000269|PubMed:15364952,
ECO:0000269|PubMed:15620710, ECO:0000269|PubMed:16407407}.
-!- DOMAIN: The CHCH domain contains a conserved twin Cys-X(9)-Cys
motif which is required for import and stability of MIA40 in
mitochondria. {ECO:0000305}.
-!- MISCELLANEOUS: Present with 5040 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Z28195; CAA82039.1; -; Genomic_DNA.
EMBL; BK006944; DAA08971.1; -; Genomic_DNA.
PIR; S38032; S38032.
RefSeq; NP_012726.2; NM_001179761.1.
PDB; 2ZXT; X-ray; 3.00 A; A=282-365.
PDB; 3A3C; X-ray; 2.50 A; A=282-353.
PDBsum; 2ZXT; -.
PDBsum; 3A3C; -.
ProteinModelPortal; P36046; -.
SMR; P36046; -.
BioGrid; 33926; 208.
DIP; DIP-5432N; -.
IntAct; P36046; 11.
MINT; MINT-574280; -.
STRING; 4932.YKL195W; -.
TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
iPTMnet; P36046; -.
MaxQB; P36046; -.
PRIDE; P36046; -.
EnsemblFungi; YKL195W; YKL195W; YKL195W.
GeneID; 853639; -.
KEGG; sce:YKL195W; -.
EuPathDB; FungiDB:YKL195W; -.
SGD; S000001678; MIA40.
GeneTree; ENSGT00390000013132; -.
InParanoid; P36046; -.
KO; K17782; -.
OrthoDB; EOG092C567C; -.
BioCyc; YEAST:G3O-31957-MONOMER; -.
EvolutionaryTrace; P36046; -.
PRO; PR:P36046; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:SGD.
GO; GO:0016491; F:oxidoreductase activity; IMP:SGD.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; TAS:Reactome.
GO; GO:0016972; F:thiol oxidase activity; IDA:SGD.
GO; GO:0006457; P:protein folding; IDA:SGD.
GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:SGD.
GO; GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome.
InterPro; IPR010625; CHCH.
Pfam; PF06747; CHCH; 1.
PROSITE; PS51808; CHCH; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
Oxidoreductase; Protein transport; Redox-active center;
Reference proteome; Signal-anchor; Transit peptide; Translocation;
Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 31 Mitochondrion.
{ECO:0000269|PubMed:15620710}.
CHAIN 32 403 Mitochondrial intermembrane space import
and assembly protein 40.
/FTId=PRO_0000203135.
TOPO_DOM 33 46 Mitochondrial matrix. {ECO:0000255}.
TRANSMEM 47 66 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 67 403 Mitochondrial intermembrane.
{ECO:0000255}.
DOMAIN 304 348 CHCH. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
MOTIF 307 317 Cx9C motif 1. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
MOTIF 330 340 Cx9C motif 2. {ECO:0000255|PROSITE-
ProRule:PRU01150}.
DISULFID 296 298 Redox-active.
{ECO:0000269|PubMed:19667201}.
DISULFID 307 340 {ECO:0000255|PROSITE-ProRule:PRU01150,
ECO:0000269|PubMed:19667201}.
DISULFID 317 330 {ECO:0000255|PROSITE-ProRule:PRU01150,
ECO:0000269|PubMed:19667201}.
MUTAGEN 296 296 C->S: Loss of function; when associated
with S-298. {ECO:0000269|PubMed:15364952,
ECO:0000269|PubMed:15620710}.
MUTAGEN 298 298 C->S: Loss of function; when associated
with S-296. {ECO:0000269|PubMed:15364952,
ECO:0000269|PubMed:15620710}.
MUTAGEN 307 307 C->S: Loss of function; when associated
with S-317. {ECO:0000269|PubMed:15364952,
ECO:0000269|PubMed:15620710}.
MUTAGEN 317 317 C->S: Loss of function; when associated
with S-307.
{ECO:0000269|PubMed:15364952}.
MUTAGEN 330 330 C->S: Loss of function; when associated
with S-340.
{ECO:0000269|PubMed:15364952}.
MUTAGEN 340 340 C->S: Loss of function; when associated
with S-330.
{ECO:0000269|PubMed:15364952}.
HELIX 282 284 {ECO:0000244|PDB:3A3C}.
TURN 287 290 {ECO:0000244|PDB:3A3C}.
HELIX 297 299 {ECO:0000244|PDB:3A3C}.
TURN 300 303 {ECO:0000244|PDB:3A3C}.
HELIX 308 319 {ECO:0000244|PDB:3A3C}.
STRAND 323 325 {ECO:0000244|PDB:3A3C}.
TURN 326 329 {ECO:0000244|PDB:3A3C}.
HELIX 331 341 {ECO:0000244|PDB:3A3C}.
TURN 345 347 {ECO:0000244|PDB:3A3C}.
SEQUENCE 403 AA; 44536 MW; 5904E8D0213D6EFA CRC64;
MLRNLVVRNA CRNRPSIQVA RGLCRHQTRR LMASSPQFGR NSNQEKTAGF IMGILSMAGA
LYFIAPNRKP LFASRKVESD KTAEEELSSG GEQSPENEDD NNSKSDENGD DNDSKNDETE
AGPQLGGDKI GASKVAEDGE LVVLAEEDNK SSEDKDTDES KVSTKDDEQS NEDNATANNQ
KDENISSENS EENTSDKTLD NNAGSSEKKD PEHSDDEKSQ QGQSDDKTTT EDNNGEEESS
KKTVSDSENS AKQSESSDEE KEELRKQEEK QMGPTEEEVQ HEGAYNPDTG EINWDCPCLG
GMAHGPCGEE FKSAFSCFVY SEAEPKGIDC VEKFQHMQDC FRKYPEHYAE QLKETSDDEE
PQDKVKVNTI ESAPNVSSAK ENAAKKAEQS DVKKEPLNEE SKP


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