MIA40_CANGA
ID MIA40_CANGA Reviewed; 404 AA.
AC Q6FW26;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Mitochondrial intermembrane space import and assembly protein 40;
DE AltName: Full=Mitochondrial import inner membrane translocase TIM40;
DE Flags: Precursor;
GN Name=MIA40; Synonyms=TIM40; OrderedLocusNames=CAGL0D03520g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Required for the import and folding of small cysteine-
CC containing proteins (small Tim) in the mitochondrial intermembrane
CC space (IMS). Forms a redox cycle with ERV1 that involves a disulfide
CC relay system. Precursor proteins to be imported into the IMS are
CC translocated in their reduced form into the mitochondria. The oxidized
CC form of MIA40 forms a transient intermolecular disulfide bridge with
CC the reduced precursor protein, resulting in oxidation of the precursor
CC protein that now contains an intramolecular disulfide bond and is able
CC to undergo folding in the IMS (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Cu(2+) or Zn(2+). {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- DOMAIN: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif
CC which is required for import and stability of MIA40 in mitochondria.
CC {ECO:0000250}.
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DR EMBL; CR380950; CAG58479.1; -; Genomic_DNA.
DR RefSeq; XP_445568.1; XM_445568.1.
DR AlphaFoldDB; Q6FW26; -.
DR SMR; Q6FW26; -.
DR STRING; 5478.XP_445568.1; -.
DR EnsemblFungi; CAG58479; CAG58479; CAGL0D03520g.
DR GeneID; 2887208; -.
DR KEGG; cgr:CAGL0D03520g; -.
DR CGD; CAL0127949; CAGL0D03520g.
DR VEuPathDB; FungiDB:CAGL0D03520g; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_681511_0_0_1; -.
DR InParanoid; Q6FW26; -.
DR OMA; RKFKPWR; -.
DR Proteomes; UP000002428; Chromosome D.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:InterPro.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR039289; CHCHD4.
DR PANTHER; PTHR21622; PTHR21622; 1.
DR Pfam; PF06747; CHCH; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Protein transport; Redox-active center; Reference proteome;
KW Signal-anchor; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..404
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000235286"
FT TOPO_DOM 35..50
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..404
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 299..343
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 84..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 302..312
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 325..335
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 116..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 291..293
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 302..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 312..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 404 AA; 44619 MW; 6E365DFD6B931A8E CRC64;
MVSAVSRQLV NRQLNRVLLR NARIAPFARA TRFYSSKYAQ ESENAKRHKM GLLIAGVAVA
GAIVFVTPPQ WKKYFRAAKK VEEVAESKED PVSEAAEEVS ESVQESTEEP QQSQEKETAD
VGNEQAQDES ASSGDSEAKK AHDEFADQNE ASEKESAPMG ESADADQTAK DETVAEKTGN
SKSESSESDQ SEQDILSSDL EETMETVSEA DKELHQISDN TVLSSEEDKT PKAEELKSTS
PSGNDEEPKK EDDSSKTIHS LNSEKDMEAV EEEVKQESAY NPDTGEINWD CPCLGGMAHG
PCGEEFKAAF SCFVYSEAEP KGIDCVEKFQ HMQDCFRRYP EHYAEQLADP ADDENVDHEK
NLSEGKDTGV DSTPPKDEAY LKTEKEKKIE ENASPDEDTA SKKD
