MIA40_XENTR
ID MIA40_XENTR Reviewed; 139 AA.
AC Q6PBC3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=TGas084k15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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 MIA40 in mitochondria.
CC {ECO:0000250}.
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DR EMBL; CR855780; CAJ83613.1; -; mRNA.
DR EMBL; BC059772; AAH59772.1; -; mRNA.
DR RefSeq; NP_988878.1; NM_203547.1.
DR AlphaFoldDB; Q6PBC3; -.
DR SMR; Q6PBC3; -.
DR PaxDb; Q6PBC3; -.
DR DNASU; 394473; -.
DR Ensembl; ENSXETT00000054090; ENSXETP00000054090; ENSXETG00000025311.
DR GeneID; 394473; -.
DR KEGG; xtr:394473; -.
DR CTD; 131474; -.
DR Xenbase; XB-GENE-968362; chchd4.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_127296_1_0_1; -.
DR InParanoid; Q6PBC3; -.
DR OMA; KDGNINW; -.
DR OrthoDB; 1594252at2759; -.
DR PhylomeDB; Q6PBC3; -.
DR TreeFam; TF314054; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025311; Expressed in egg cell and 14 other tissues.
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..139
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000235281"
FT DOMAIN 61..105
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 102..139
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 114..139
FT /note="Basic and acidic 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 139 AA; 15712 MW; 12D0498954D66953 CRC64;
MSYCRQEGKD KIIFVTKEDH ETPSSAELIA DDPNDPYEDH GLILPNGDIN WNCPCLGGMA
SGPCGEQFKS AFSCFHYSQE EIKGSDCLDQ FRAMQECMQK YPDIYPQEDD EDEAEKEKQN
KEAEAFSTET SDTKEESSS