ID   MIA40_DANRE             Reviewed;         146 AA.
AC   Q6DEI8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Mitochondrial intermembrane space import and assembly protein 40;
DE   AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 4;
GN   Name=chchd4; Synonyms=mia40; ORFNames=zgc:100849;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Central component of a redox-sensitive mitochondrial
CC       intermembrane space import machinery which is required for the
CC       biogenesis of respiratory chain complexes (By similarity). Functions as
CC       chaperone and catalyzes the formation of disulfide bonds in substrate
CC       proteins, such as COX17 or MICU1. Required for the import and folding
CC       of small cysteine-containing proteins (small Tim) in the mitochondrial
CC       intermembrane space (IMS). Precursor proteins to be imported into the
CC       IMS are translocated in their reduced form into the mitochondria.
CC       {ECO:0000250|UniProtKB:Q2KHZ4, ECO:0000250|UniProtKB:Q8N4Q1}.
CC   -!- SUBUNIT: Monomer. Can form homooligomers.
CC       {ECO:0000250|UniProtKB:Q8N4Q1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:Q8N4Q1}.
CC   -!- DOMAIN: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif
CC       which is required for import and stability of chchd4/mia40 in
CC       mitochondria. {ECO:0000250}.
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DR   EMBL; BC077126; AAH77126.1; -; mRNA.
DR   RefSeq; NP_001003538.1; NM_001003538.2.
DR   AlphaFoldDB; Q6DEI8; -.
DR   SMR; Q6DEI8; -.
DR   STRING; 7955.ENSDARP00000039846; -.
DR   PaxDb; Q6DEI8; -.
DR   DNASU; 445144; -.
DR   GeneID; 445144; -.
DR   KEGG; dre:445144; -.
DR   CTD; 445144; -.
DR   ZFIN; ZDB-GENE-040801-46; chchd4a.
DR   eggNOG; KOG4149; Eukaryota.
DR   InParanoid; Q6DEI8; -.
DR   OrthoDB; 1594252at2759; -.
DR   PhylomeDB; Q6DEI8; -.
DR   PRO; PR:Q6DEI8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR   GO; GO:0051084; P:'de novo' post-translational protein folding; ISS:UniProtKB.
DR   GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0022417; P:protein maturation by protein folding; ISS:UniProtKB.
DR   InterPro; IPR010625; CHCH.
DR   InterPro; IPR039289; CHCHD4.
DR   PANTHER; PTHR21622; PTHR21622; 1.
DR   Pfam; PF06747; CHCH; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Mitochondrion; Oxidoreductase; Protein transport;
KW   Redox-active center; Reference proteome; Translocation; Transport.
FT   CHAIN           1..146
FT                   /note="Mitochondrial intermembrane space import and
FT                   assembly protein 40"
FT                   /id="PRO_0000235278"
FT   DOMAIN          61..105
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          101..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           64..74
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           87..97
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COMPBIAS        113..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        53..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4Q1"
FT   DISULFID        64..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        74..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   146 AA;  15755 MW;  1558B7863EC5A549 CRC64;
     MSYCKQEGKD CIIFVTKEDH EAPSNAELVE DDPNDPYEDH GLILPNGDIN WNCPCLGGMA
     SGPCGQQFKD AFSCFHYSKE EIKGSDCVEN FRGMQECMQK YPELYPQEDD NDSAPSGGAN
     TAPTDSLPAS STDSTAAAAT ENPATS