MIA40_USTMA
ID MIA40_USTMA Reviewed; 247 AA.
AC Q4P8D2; A0A0D1E1T3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
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; ORFNames=UMAG_03631;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003148; KIS68545.1; -; Genomic_DNA.
DR RefSeq; XP_011390053.1; XM_011391751.1.
DR AlphaFoldDB; Q4P8D2; -.
DR SMR; Q4P8D2; -.
DR STRING; 5270.UM03631P0; -.
DR EnsemblFungi; KIS68545; KIS68545; UMAG_03631.
DR GeneID; 23564040; -.
DR KEGG; uma:UMAG_03631; -.
DR VEuPathDB; FungiDB:UMAG_03631; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_054990_1_3_1; -.
DR InParanoid; Q4P8D2; -.
DR OMA; SSAIQCE; -.
DR OrthoDB; 1416113at2759; -.
DR Proteomes; UP000000561; Chromosome 9.
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:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IBA:GO_Central.
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..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..247
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000235293"
FT TOPO_DOM 29..45
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..247
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 157..201
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 81..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..170
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 183..193
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 149..151
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 160..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 170..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 247 AA; 26545 MW; CABFAF16B884EC3C CRC64;
MLSSKLVACS AGRSVQRISR TFLPAMRGVA TKAAAGPSRQ SALSSYSIAA VTAIGVGASF
YALQSRSSAI QCEPRQAWHD RLKPKEAKGD ATLHKDAHTR HAPAEVQDER VEPVEETPVA
IEVAVEESEE QTGQQSAYDP ETGEINWDCP CLGGMAHGPC GEQFKLAFSC FVYSEAEPKG
IDCVDKFKAM QDCFREHPDV YKDEIEDDEA ANAQFEKEEA NAKSNGLNDA AQEAVEESSG
GKEGASA
