MIA40_RAT
ID MIA40_RAT Reviewed; 139 AA.
AC Q5BJN5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Functions as chaperone and
CC catalyzes the formation of disulfide bonds in substrate proteins, such
CC as COX17, COX19, MICU1 and COA7. Required for the import and folding of
CC small cysteine-containing proteins (small Tim) in the mitochondrial
CC intermembrane space (IMS). Required for the import of COA7 in the IMS.
CC Precursor proteins to be imported into the IMS are translocated in
CC their reduced form into the mitochondria. The oxidized form of
CC CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the
CC 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. Reduced CHCHD4/MIA40 is then reoxidized
CC by GFER/ERV1 via a disulfide relay system. Mediates formation of
CC disulfide bond in MICU1 in the IMS, promoting formation of the MICU1-
CC MICU2 heterodimer that regulates mitochondrial calcium uptake.
CC {ECO:0000250|UniProtKB:Q8N4Q1}.
CC -!- SUBUNIT: Monomer. Can form homooligomers. Interacts with GFER and forms
CC transient disulfide bonds with GFER. Interacts with MICU1. Interacts
CC with COX19 forming transient intermolecular disulfide bridges.
CC Interacts with COA7 through transient intermolecular disulfide bonds.
CC Interacts with AIFM1; the interaction increases in presence of NADH.
CC Interacts with NDUFB10. {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}.
CC -!- PTM: Forms intrachain disulfide bridges, but exists in different redox
CC states. {ECO:0000250}.
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DR EMBL; BC091407; AAH91407.1; -; mRNA.
DR RefSeq; NP_001013449.1; NM_001013431.1.
DR RefSeq; XP_003749131.1; XM_003749083.3.
DR RefSeq; XP_003753440.1; XM_003753392.3.
DR AlphaFoldDB; Q5BJN5; -.
DR SMR; Q5BJN5; -.
DR STRING; 10116.ENSRNOP00000038359; -.
DR iPTMnet; Q5BJN5; -.
DR PhosphoSitePlus; Q5BJN5; -.
DR PaxDb; Q5BJN5; -.
DR PRIDE; Q5BJN5; -.
DR Ensembl; ENSRNOT00000038096; ENSRNOP00000038359; ENSRNOG00000022466.
DR Ensembl; ENSRNOT00000116242; ENSRNOP00000094363; ENSRNOG00000069157.
DR GeneID; 100361898; -.
DR GeneID; 312559; -.
DR KEGG; rno:100361898; -.
DR KEGG; rno:312559; -.
DR UCSC; RGD:1310746; rat.
DR CTD; 131474; -.
DR RGD; 1310746; Chchd4.
DR eggNOG; KOG4149; Eukaryota.
DR GeneTree; ENSGT00390000013132; -.
DR HOGENOM; CLU_127296_1_0_1; -.
DR InParanoid; Q5BJN5; -.
DR OMA; MECAMRT; -.
DR OrthoDB; 1594252at2759; -.
DR PhylomeDB; Q5BJN5; -.
DR TreeFam; TF314054; -.
DR PRO; PR:Q5BJN5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000022466; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5BJN5; RN.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; 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:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO:RGD.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; ISS:UniProtKB.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:RGD.
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 GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
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_0000235277"
FT DOMAIN 61..105
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 104..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 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; 15467 MW; 624DC5FD13A102FF CRC64;
MSYCRQEGKD RIIFVTKEDH ETPSSAELVA DDPNDPYEEH GLILPNGDIN WNCPCLGGMA
SGPCGEQFKS AFSCFHYSTE DIKGSDCIDQ FRAMQECMQK YPDLYPQDEE EEEEAKPVEP
VEETADTKAS AAKEQGASS
