MIA40_HUMAN
ID MIA40_HUMAN Reviewed; 142 AA.
AC Q8N4Q1; A8K3Z9; Q96AI2; Q96MY6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Testis;
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-53; CYS-55; CYS-64; CYS-74; CYS-87 AND CYS-97.
RX PubMed=16185709; DOI=10.1016/j.jmb.2005.08.064;
RA Hofmann S., Rothbauer U., Muehlenbein N., Baiker K., Hell K., Bauer M.F.;
RT "Functional and mutational characterization of human MIA40 acting during
RT import into the mitochondrial intermembrane space.";
RL J. Mol. Biol. 353:517-528(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH COX19 AND GFER.
RX PubMed=23676665; DOI=10.1091/mbc.e12-12-0862;
RA Fischer M., Horn S., Belkacemi A., Kojer K., Petrungaro C., Habich M.,
RA Ali M., Kuettner V., Bien M., Kauff F., Dengjel J., Herrmann J.M.,
RA Riemer J.;
RT "Protein import and oxidative folding in the mitochondrial intermembrane
RT space of intact mammalian cells.";
RL Mol. Biol. Cell 24:2160-2170(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GFER.
RX PubMed=23186364; DOI=10.1111/tra.12030;
RA Sztolsztener M.E., Brewinska A., Guiard B., Chacinska A.;
RT "Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial
RT biogenesis of human MIA40.";
RL Traffic 14:309-320(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, INTERACTION WITH MICU1, AND MUTAGENESIS OF CYS-53.
RX PubMed=26387864; DOI=10.1016/j.cmet.2015.08.019;
RA Petrungaro C., Zimmermann K.M., Kuettner V., Fischer M., Dengjel J.,
RA Bogeski I., Riemer J.;
RT "The Ca(2+)-dependent release of the Mia40-induced MICU1-MICU2 dimer from
RT MCU regulates mitochondrial Ca(2+) uptake.";
RL Cell Metab. 22:721-733(2015).
RN [11]
RP FUNCTION, INTERACTION WITH AIFM1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-4; 53-CYS--CYS-55; CYS-53; CYS-74; CYS-87 AND CYS-97.
RX PubMed=26004228; DOI=10.1016/j.molcel.2015.04.020;
RA Hangen E., Feraud O., Lachkar S., Mou H., Doti N., Fimia G.M., Lam N.V.,
RA Zhu C., Godin I., Muller K., Chatzi A., Nuebel E., Ciccosanti F.,
RA Flamant S., Benit P., Perfettini J.L., Sauvat A., Bennaceur-Griscelli A.,
RA Ser-Le Roux K., Gonin P., Tokatlidis K., Rustin P., Piacentini M., Ruvo M.,
RA Blomgren K., Kroemer G., Modjtahedi N.;
RT "Interaction between AIF and CHCHD4 Regulates Respiratory Chain
RT Biogenesis.";
RL Mol. Cell 58:1001-1014(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, INTERACTION WITH COA7, AND MUTAGENESIS OF CYS-53 AND CYS-55.
RX PubMed=30885959; DOI=10.15252/emmm.201809561;
RA Mohanraj K., Wasilewski M., Beninca C., Cysewski D., Poznanski J.,
RA Sakowska P., Bugajska Z., Deckers M., Dennerlein S., Fernandez-Vizarra E.,
RA Rehling P., Dadlez M., Zeviani M., Chacinska A.;
RT "Inhibition of proteasome rescues a pathogenic variant of respiratory chain
RT assembly factor COA7.";
RL EMBO Mol. Med. 11:0-0(2019).
RN [14]
RP STRUCTURE BY NMR, FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-53 AND CYS-55, AND
RP DISULFIDE BONDS.
RX PubMed=19182799; DOI=10.1038/nsmb.1553;
RA Banci L., Bertini I., Cefaro C., Ciofi-Baffoni S., Gallo A., Martinelli M.,
RA Sideris D.P., Katrakili N., Tokatlidis K.;
RT "MIA40 is an oxidoreductase that catalyzes oxidative protein folding in
RT mitochondria.";
RL Nat. Struct. Mol. Biol. 16:198-206(2009).
RN [15]
RP STRUCTURE BY NMR IN COMPLEX WITH COX17, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=21059946; DOI=10.1073/pnas.1010095107;
RA Banci L., Bertini I., Cefaro C., Cenacchi L., Ciofi-Baffoni S., Felli I.C.,
RA Gallo A., Gonnelli L., Luchinat E., Sideris D., Tokatlidis K.;
RT "Molecular chaperone function of Mia40 triggers consecutive induced folding
RT steps of the substrate in mitochondrial protein import.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20190-20195(2010).
RN [16]
RP INTERACTION WITH NDUFB10.
RX PubMed=28040730; DOI=10.1093/hmg/ddw431;
RA Friederich M.W., Erdogan A.J., Coughlin C.R. II, Elos M.T., Jiang H.,
RA O'Rourke C.P., Lovell M.A., Wartchow E., Gowan K., Chatfield K.C.,
RA Chick W.S., Spector E.B., Van Hove J.L.K., Riemer J.;
RT "Mutations in the accessory subunit NDUFB10 result in isolated complex I
RT deficiency and illustrate the critical role of intermembrane space import
RT for complex I holoenzyme assembly.";
RL Hum. Mol. Genet. 26:702-716(2017).
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 (PubMed:26004228). Functions
CC as chaperone and catalyzes the formation of disulfide bonds in
CC substrate proteins, such as COX17, COX19, MICU1 and COA7
CC (PubMed:16185709, PubMed:26387864, PubMed:19182799, PubMed:21059946,
CC PubMed:23186364, PubMed:23676665, PubMed:30885959). Required for the
CC import and folding of small cysteine-containing proteins (small Tim) in
CC the mitochondrial intermembrane space (IMS). Required for the import of
CC COA7 in the IMS (PubMed:30885959). Precursor proteins to be imported
CC into the IMS are translocated in their reduced form into the
CC mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient
CC intermolecular disulfide bridge with the reduced precursor protein,
CC resulting in oxidation of the precursor protein that now contains an
CC intramolecular disulfide bond and is able to undergo folding in the IMS
CC (PubMed:16185709, PubMed:19182799, PubMed:21059946, PubMed:23676665).
CC Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide
CC relay system (PubMed:23186364). Mediates formation of disulfide bond in
CC MICU1 in the IMS, promoting formation of the MICU1-MICU2 heterodimer
CC that regulates mitochondrial calcium uptake (PubMed:26387864).
CC {ECO:0000269|PubMed:16185709, ECO:0000269|PubMed:19182799,
CC ECO:0000269|PubMed:21059946, ECO:0000269|PubMed:23186364,
CC ECO:0000269|PubMed:23676665, ECO:0000269|PubMed:26004228,
CC ECO:0000269|PubMed:26387864, ECO:0000269|PubMed:30885959}.
CC -!- SUBUNIT: Monomer (PubMed:19182799). Can form homooligomers
CC (PubMed:16185709). Interacts with GFER and forms transient disulfide
CC bonds with GFER (PubMed:23186364, PubMed:23676665). Interacts with
CC MICU1 (PubMed:26387864). Interacts with COX19 forming transient
CC intermolecular disulfide bridges (PubMed:23676665). Interacts with COA7
CC through transient intermolecular disulfide bonds (PubMed:30885959).
CC Interacts with AIFM1; the interaction increases in presence of NADH
CC (PubMed:26004228). Interacts with NDUFB10; assists NDUFB10 oxidation,
CC folding and import into mitochondrion. {ECO:0000269|PubMed:16185709,
CC ECO:0000269|PubMed:19182799, ECO:0000269|PubMed:23186364,
CC ECO:0000269|PubMed:23676665, ECO:0000269|PubMed:26004228,
CC ECO:0000269|PubMed:28040730, ECO:0000269|PubMed:30885959}.
CC -!- INTERACTION:
CC Q8N4Q1; Q9BPX6: MICU1; NbExp=6; IntAct=EBI-2562213, EBI-2371996;
CC Q8N4Q1-1; Q14061: COX17; NbExp=2; IntAct=EBI-15755238, EBI-711311;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:16185709, ECO:0000269|PubMed:23186364,
CC ECO:0000269|PubMed:23676665, ECO:0000269|PubMed:26004228}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N4Q1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N4Q1-2; Sequence=VSP_018433;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, suggesting an
CC ubiquitous expression. {ECO:0000269|PubMed:16185709}.
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:0000305}.
CC -!- PTM: Forms intrachain disulfide bridges, but exists in different redox
CC states.
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DR EMBL; AK056271; BAB71132.1; -; mRNA.
DR EMBL; AK290764; BAF83453.1; -; mRNA.
DR EMBL; CH471055; EAW64180.1; -; Genomic_DNA.
DR EMBL; BC017082; AAH17082.2; -; mRNA.
DR EMBL; BC033775; AAH33775.1; -; mRNA.
DR CCDS; CCDS2617.1; -. [Q8N4Q1-2]
DR CCDS; CCDS43054.1; -. [Q8N4Q1-1]
DR RefSeq; NP_001091972.1; NM_001098502.1. [Q8N4Q1-1]
DR RefSeq; NP_653237.1; NM_144636.2. [Q8N4Q1-2]
DR PDB; 2K3J; NMR; -; A=1-142.
DR PDB; 2L0Y; NMR; -; A=1-142.
DR PDBsum; 2K3J; -.
DR PDBsum; 2L0Y; -.
DR AlphaFoldDB; Q8N4Q1; -.
DR BMRB; Q8N4Q1; -.
DR SMR; Q8N4Q1; -.
DR BioGRID; 126282; 132.
DR DIP; DIP-48483N; -.
DR IntAct; Q8N4Q1; 44.
DR MINT; Q8N4Q1; -.
DR STRING; 9606.ENSP00000295767; -.
DR GlyGen; Q8N4Q1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N4Q1; -.
DR PhosphoSitePlus; Q8N4Q1; -.
DR BioMuta; CHCHD4; -.
DR DMDM; 62510498; -.
DR EPD; Q8N4Q1; -.
DR jPOST; Q8N4Q1; -.
DR MassIVE; Q8N4Q1; -.
DR MaxQB; Q8N4Q1; -.
DR PaxDb; Q8N4Q1; -.
DR PeptideAtlas; Q8N4Q1; -.
DR PRIDE; Q8N4Q1; -.
DR ProteomicsDB; 71958; -. [Q8N4Q1-1]
DR ProteomicsDB; 71959; -. [Q8N4Q1-2]
DR TopDownProteomics; Q8N4Q1-1; -. [Q8N4Q1-1]
DR Antibodypedia; 45048; 187 antibodies from 28 providers.
DR DNASU; 131474; -.
DR Ensembl; ENST00000295767.9; ENSP00000295767.5; ENSG00000163528.13. [Q8N4Q1-2]
DR Ensembl; ENST00000396914.4; ENSP00000380122.3; ENSG00000163528.13. [Q8N4Q1-1]
DR GeneID; 131474; -.
DR KEGG; hsa:131474; -.
DR MANE-Select; ENST00000396914.4; ENSP00000380122.3; NM_001098502.2; NP_001091972.1.
DR UCSC; uc003byi.5; human. [Q8N4Q1-1]
DR CTD; 131474; -.
DR DisGeNET; 131474; -.
DR GeneCards; CHCHD4; -.
DR HGNC; HGNC:26467; CHCHD4.
DR HPA; ENSG00000163528; Low tissue specificity.
DR MIM; 611077; gene.
DR neXtProt; NX_Q8N4Q1; -.
DR OpenTargets; ENSG00000163528; -.
DR PharmGKB; PA134990707; -.
DR VEuPathDB; HostDB:ENSG00000163528; -.
DR eggNOG; KOG4149; Eukaryota.
DR GeneTree; ENSGT00390000013132; -.
DR HOGENOM; CLU_127296_1_0_1; -.
DR InParanoid; Q8N4Q1; -.
DR OMA; MECAMRT; -.
DR PhylomeDB; Q8N4Q1; -.
DR TreeFam; TF314054; -.
DR PathwayCommons; Q8N4Q1; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q8N4Q1; -.
DR BioGRID-ORCS; 131474; 648 hits in 1073 CRISPR screens.
DR ChiTaRS; CHCHD4; human.
DR EvolutionaryTrace; Q8N4Q1; -.
DR GenomeRNAi; 131474; -.
DR Pharos; Q8N4Q1; Tbio.
DR PRO; PR:Q8N4Q1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N4Q1; protein.
DR Bgee; ENSG00000163528; Expressed in left ventricle myocardium and 186 other tissues.
DR ExpressionAtlas; Q8N4Q1; baseline and differential.
DR Genevisible; Q8N4Q1; HS.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; IMP:UniProtKB.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:UniProtKB.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; IMP:UniProtKB.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:UniProtKB.
DR GO; GO:0022417; P:protein maturation by protein folding; IMP:UniProtKB.
DR DisProt; DP00912; -.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR039289; CHCHD4.
DR PANTHER; PTHR21622; PTHR21622; 1.
DR Pfam; PF06747; CHCH; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Mitochondrion;
KW Oxidoreductase; Protein transport; Redox-active center; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..142
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000129165"
FT DOMAIN 61..105
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..27
FT /note="Sufficient for interaction with AIFM1"
FT /evidence="ECO:0000269|PubMed:26004228"
FT REGION 101..142
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:0000269|PubMed:19182799,
FT ECO:0000305|PubMed:26387864"
FT DISULFID 64..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:19182799, ECO:0000305|PubMed:21059946,
FT ECO:0007744|PDB:2K3J, ECO:0007744|PDB:2L0Y"
FT DISULFID 74..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:19182799, ECO:0000305|PubMed:21059946,
FT ECO:0007744|PDB:2K3J, ECO:0007744|PDB:2L0Y"
FT VAR_SEQ 1..6
FT /note="MSYCRQ -> MPVSYSSVTTRYYHRAGAE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018433"
FT MUTAGEN 4
FT /note="C->S: No effect on interaction with AIFM1."
FT /evidence="ECO:0000269|PubMed:26004228"
FT MUTAGEN 53..55
FT /note="CPC->SPS: No effect on interaction with AIFM1."
FT /evidence="ECO:0000269|PubMed:26004228"
FT MUTAGEN 53
FT /note="C->S: Does not strongly affect import and stability
FT of CHCHD4 in mitochondria; when associated with S-55. No
FT effect on disulfide exchange with substrate proteins. Does
FT not affect interaction with COA7. No effect on interaction
FT with AIFM1."
FT /evidence="ECO:0000269|PubMed:16185709,
FT ECO:0000269|PubMed:19182799, ECO:0000269|PubMed:26004228,
FT ECO:0000269|PubMed:26387864, ECO:0000269|PubMed:30885959"
FT MUTAGEN 55
FT /note="C->S: Does not strongly affect import and stability
FT of CHCHD4 in mitochondria; when associated with S-53.
FT Nearly abolishes disulfide exchange with substrate
FT proteins. Abolishes interaction with COA7."
FT /evidence="ECO:0000269|PubMed:16185709,
FT ECO:0000269|PubMed:19182799, ECO:0000269|PubMed:30885959"
FT MUTAGEN 64
FT /note="C->S: Affects import and stability of CHCHD4 in
FT mitochondria; when associated with S-74."
FT /evidence="ECO:0000269|PubMed:16185709"
FT MUTAGEN 74
FT /note="C->S: Affects import and stability of CHCHD4 in
FT mitochondria; when associated with S-64. No effect on
FT interaction with AIFM1."
FT /evidence="ECO:0000269|PubMed:16185709,
FT ECO:0000269|PubMed:26004228"
FT MUTAGEN 87
FT /note="C->S: Strongly affects import and stability of
FT CHCHD4 in mitochondria; when associated with S-97. No
FT effect on interaction with AIFM1."
FT /evidence="ECO:0000269|PubMed:16185709,
FT ECO:0000269|PubMed:26004228"
FT MUTAGEN 97
FT /note="C->S: Strongly affects import and stability of
FT CHCHD4 in mitochondria; when associated with S-87. No
FT effect on interaction with AIFM1."
FT /evidence="ECO:0000269|PubMed:16185709,
FT ECO:0000269|PubMed:26004228"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2K3J"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2K3J"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2K3J"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:2K3J"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2L0Y"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:2K3J"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2K3J"
SQ SEQUENCE 142 AA; 15996 MW; 87563CADF249800C CRC64;
MSYCRQEGKD RIIFVTKEDH ETPSSAELVA DDPNDPYEEH GLILPNGNIN WNCPCLGGMA
SGPCGEQFKS AFSCFHYSTE EIKGSDCVDQ FRAMQECMQK YPDLYPQEDE DEEEEREKKP
AEQAEETAPI EATATKEEEG SS
