MIA40_BOVIN
ID MIA40_BOVIN Reviewed; 137 AA.
AC Q2KHZ4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Pancreas;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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. 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; BC112827; AAI12828.1; -; mRNA.
DR RefSeq; NP_001039624.1; NM_001046159.2.
DR AlphaFoldDB; Q2KHZ4; -.
DR SMR; Q2KHZ4; -.
DR STRING; 9913.ENSBTAP00000020635; -.
DR PaxDb; Q2KHZ4; -.
DR PRIDE; Q2KHZ4; -.
DR Ensembl; ENSBTAT00000020635; ENSBTAP00000020635; ENSBTAG00000015529.
DR GeneID; 513889; -.
DR KEGG; bta:513889; -.
DR CTD; 131474; -.
DR VEuPathDB; HostDB:ENSBTAG00000015529; -.
DR VGNC; VGNC:27273; CHCHD4.
DR eggNOG; KOG4149; Eukaryota.
DR GeneTree; ENSGT00390000013132; -.
DR HOGENOM; CLU_127296_1_0_1; -.
DR InParanoid; Q2KHZ4; -.
DR OMA; MECAMRT; -.
DR OrthoDB; 1594252at2759; -.
DR TreeFam; TF314054; -.
DR Proteomes; UP000009136; Chromosome 22.
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:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; 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 InterPro; IPR009069; Cys_alpha_HP_mot_SF.
DR PANTHER; PTHR21622; PTHR21622; 1.
DR Pfam; PF06747; CHCH; 1.
DR SUPFAM; SSF47072; SSF47072; 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..137
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000235276"
FT DOMAIN 61..105
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 102..137
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 137 AA; 15173 MW; 8522163B309BD0EE CRC64;
MAYCRQEGKD RIIFVTKEDH ETPSNAELVA DDPNDPYEEH GLILPNGDIN WNCPCLGGMA
SGPCGEQFKA AFSCFHYSKE DVKGSDCVDQ FRAMQECMQK YPDLYPQEEE EEEEQPADPL
PEAASEASAT KEAAASS
