CHC10_HUMAN
ID CHC10_HUMAN Reviewed; 142 AA.
AC Q8WYQ3; A8K0J5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial;
DE AltName: Full=Protein N27C7-4;
DE Flags: Precursor;
GN Name=CHCHD10; Synonyms=C22orf16;
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 [GENOMIC DNA].
RA Shimizu N., Minosima S., Kawasaki K., Sasaki T., Hosono K.;
RT "Molecular cloning of N27C7-4 gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN FTDALS2,
RP VARIANT FTDALS2 LEU-59, AND CHARACTERIZATION OF VARIANT FTDALS2 LEU-59.
RX PubMed=24934289; DOI=10.1093/brain/awu138;
RA Bannwarth S., Ait-El-Mkadem S., Chaussenot A., Genin E.C.,
RA Lacas-Gervais S., Fragaki K., Berg-Alonso L., Kageyama Y., Serre V.,
RA Moore D.G., Verschueren A., Rouzier C., Le Ber I., Auge G., Cochaud C.,
RA Lespinasse F., N'Guyen K., de Septenville A., Brice A., Yu-Wai-Man P.,
RA Sesaki H., Pouget J., Paquis-Flucklinger V.;
RT "A mitochondrial origin for frontotemporal dementia and amyotrophic lateral
RT sclerosis through CHCHD10 involvement.";
RL Brain 137:2329-2345(2014).
RN [6]
RP INVOLVEMENT IN SMAJ, AND VARIANT SMAJ VAL-66.
RX PubMed=25428574; DOI=10.1002/ana.24319;
RA Penttilae S., Jokela M., Bouquin H., Saukkonen A.M., Toivanen J., Udd B.;
RT "Late onset spinal motor neuronopathy is caused by mutation in CHCHD10.";
RL Ann. Neurol. 77:163-172(2015).
RN [7]
RP INVOLVEMENT IN IMMD, VARIANTS IMMD SER-15 AND ARG-58, AND CHARACTERIZATION
RP OF VARIANTS IMMD SER-15 AND ARG-58.
RX PubMed=25193783; DOI=10.1007/s10048-014-0421-1;
RA Ajroud-Driss S., Fecto F., Ajroud K., Lalani I., Calvo S.E., Mootha V.K.,
RA Deng H.X., Siddique N., Tahmoush A.J., Heiman-Patterson T.D., Siddique T.;
RT "Mutation in the novel nuclear-encoded mitochondrial protein CHCHD10 in a
RT family with autosomal dominant mitochondrial myopathy.";
RL Neurogenetics 16:1-9(2015).
RN [8]
RP VARIANT FTDALS2 SER-34.
RX PubMed=25155093; DOI=10.1016/j.neurobiolaging.2014.07.022;
RG The French research network on FTD and FTD-ALS;
RA Chaussenot A., Le Ber I., Ait-El-Mkadem S., Camuzat A., de Septenville A.,
RA Bannwarth S., Genin E.C., Serre V., Auge G., Brice A., Pouget J.,
RA Paquis-Flucklinger V.;
RT "Screening of CHCHD10 in a French cohort confirms the involvement of this
RT gene in frontotemporal dementia with amyotrophic lateral sclerosis
RT patients.";
RL Neurobiol. Aging 0:0-0(2014).
CC -!- FUNCTION: May be involved in the maintenance of mitochondrial
CC organization and mitochondrial cristae structure.
CC {ECO:0000269|PubMed:24934289}.
CC -!- INTERACTION:
CC Q8WYQ3; Q9Y6H1: CHCHD2; NbExp=15; IntAct=EBI-16721660, EBI-2321769;
CC Q8WYQ3; Q16891: IMMT; NbExp=4; IntAct=EBI-16721660, EBI-473801;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:24934289}. Note=Enriched at the cristae junctions.
CC {ECO:0000269|PubMed:24934289}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Higher expression is
CC observed in heart and liver. {ECO:0000269|PubMed:24934289}.
CC -!- DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 2
CC (FTDALS2) [MIM:615911]: A neurodegenerative disorder characterized by
CC frontotemporal dementia and/or amyotrophic lateral sclerosis in
CC affected individuals. There is high intrafamilial variation.
CC Frontotemporal dementia is characterized by frontal and temporal lobe
CC atrophy associated with neuronal loss, gliosis, and dementia. Patients
CC exhibit progressive changes in social, behavioral, and/or language
CC function. Amyotrophic lateral sclerosis is characterized by the death
CC of motor neurons in the brain, brainstem, and spinal cord, resulting in
CC fatal paralysis. {ECO:0000269|PubMed:24934289,
CC ECO:0000269|PubMed:25155093}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. The pathological events
CC leading to disease involve fragmentation of the mitochondrial network,
CC mitochondrial ultrastructural abnormalities including loss,
CC disorganization and dilatation of cristae, and mitochondrial
CC dysfunction associated with respiratory chain deficiency
CC (PubMed:24934289). {ECO:0000269|PubMed:24934289}.
CC -!- DISEASE: Spinal muscular atrophy, Jokela type (SMAJ) [MIM:615048]: An
CC autosomal dominant, slowly progressive, lower motor neuron disease.
CC SMAJ is characterized by adult-onset of muscle cramps and
CC fasciculations affecting the proximal and distal muscles of the upper
CC and lower limbs. The disorder results in weakness and mild muscle
CC atrophy later in life. {ECO:0000269|PubMed:25428574}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Myopathy, isolated mitochondrial, autosomal dominant (IMMD)
CC [MIM:616209]: A mitochondrial myopathy presenting with severe exercise
CC intolerance, progressive proximal weakness, and lactic acidemia. The
CC disorder is slowly progressive, with later involvement of facial
CC muscles, muscles of the upper limbs, and distal muscles.
CC {ECO:0000269|PubMed:25193783}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AB050774; BAB83036.1; -; Genomic_DNA.
DR EMBL; AK289560; BAF82249.1; -; mRNA.
DR EMBL; CH471095; EAW59602.1; -; Genomic_DNA.
DR EMBL; BC065232; AAH65232.1; -; mRNA.
DR CCDS; CCDS13815.1; -.
DR RefSeq; NP_001288268.1; NM_001301339.1.
DR RefSeq; NP_998885.1; NM_213720.2.
DR AlphaFoldDB; Q8WYQ3; -.
DR SMR; Q8WYQ3; -.
DR BioGRID; 134810; 84.
DR IntAct; Q8WYQ3; 97.
DR STRING; 9606.ENSP00000418428; -.
DR iPTMnet; Q8WYQ3; -.
DR PhosphoSitePlus; Q8WYQ3; -.
DR BioMuta; CHCHD10; -.
DR DMDM; 74731006; -.
DR EPD; Q8WYQ3; -.
DR jPOST; Q8WYQ3; -.
DR MassIVE; Q8WYQ3; -.
DR MaxQB; Q8WYQ3; -.
DR PaxDb; Q8WYQ3; -.
DR PeptideAtlas; Q8WYQ3; -.
DR PRIDE; Q8WYQ3; -.
DR ProteomicsDB; 75185; -.
DR Antibodypedia; 48878; 117 antibodies from 20 providers.
DR DNASU; 400916; -.
DR Ensembl; ENST00000484558.3; ENSP00000418428.3; ENSG00000250479.9.
DR Ensembl; ENST00000629095.1; ENSP00000487006.1; ENSG00000273607.3.
DR GeneID; 400916; -.
DR KEGG; hsa:400916; -.
DR MANE-Select; ENST00000484558.3; ENSP00000418428.3; NM_213720.3; NP_998885.1.
DR UCSC; uc002zxw.4; human.
DR CTD; 400916; -.
DR DisGeNET; 400916; -.
DR GeneCards; CHCHD10; -.
DR GeneReviews; CHCHD10; -.
DR HGNC; HGNC:15559; CHCHD10.
DR HPA; ENSG00000250479; Tissue enhanced (heart muscle, skeletal muscle).
DR MalaCards; CHCHD10; -.
DR MIM; 615048; phenotype.
DR MIM; 615903; gene.
DR MIM; 615911; phenotype.
DR MIM; 616209; phenotype.
DR neXtProt; NX_Q8WYQ3; -.
DR OpenTargets; ENSG00000250479; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 457050; Autosomal dominant mitochondrial myopathy with exercise intolerance.
DR Orphanet; 275872; Frontotemporal dementia with motor neuron disease.
DR Orphanet; 276435; Lower motor neuron syndrome with late-adult onset.
DR PharmGKB; PA162382225; -.
DR VEuPathDB; HostDB:ENSG00000250479; -.
DR eggNOG; KOG4090; Eukaryota.
DR GeneTree; ENSGT00940000161345; -.
DR HOGENOM; CLU_093520_2_2_1; -.
DR InParanoid; Q8WYQ3; -.
DR OMA; CKYSHGV; -.
DR OrthoDB; 1611117at2759; -.
DR PhylomeDB; Q8WYQ3; -.
DR TreeFam; TF318060; -.
DR PathwayCommons; Q8WYQ3; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q8WYQ3; -.
DR BioGRID-ORCS; 400916; 27 hits in 1075 CRISPR screens.
DR ChiTaRS; CHCHD10; human.
DR GenomeRNAi; 400916; -.
DR Pharos; Q8WYQ3; Tbio.
DR PRO; PR:Q8WYQ3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8WYQ3; protein.
DR Bgee; ENSG00000250479; Expressed in apex of heart and 97 other tissues.
DR ExpressionAtlas; Q8WYQ3; baseline and differential.
DR Genevisible; Q8WYQ3; HS.
DR GO; GO:0061617; C:MICOS complex; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR GO; GO:0099558; P:maintenance of synapse structure; ISS:UniProtKB.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:0090144; P:mitochondrial nucleoid organization; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0006119; P:oxidative phosphorylation; IMP:BHF-UCL.
DR GO; GO:1903852; P:positive regulation of cristae formation; IMP:UniProtKB.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1903109; P:positive regulation of mitochondrial transcription; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; ISS:UniProtKB.
DR InterPro; IPR010625; CHCH.
DR Pfam; PF06747; CHCH; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Amyotrophic lateral sclerosis; Disease variant; Disulfide bond;
KW Mitochondrion; Neurodegeneration; Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..142
FT /note="Coiled-coil-helix-coiled-coil-helix domain-
FT containing protein 10, mitochondrial"
FT /id="PRO_0000254038"
FT DOMAIN 99..140
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 102..112
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 122..132
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 17..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 102..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 112..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT VARIANT 15
FT /note="R -> S (in IMMD; associated in cis with R-58 in a
FT IMMD family; unknown pathological significance; does not
FT affect mitochondrial structure and organization;
FT dbSNP:rs730880032)"
FT /evidence="ECO:0000269|PubMed:25193783"
FT /id="VAR_073283"
FT VARIANT 34
FT /note="P -> S (in FTDALS2; dbSNP:rs551521196)"
FT /evidence="ECO:0000269|PubMed:25155093"
FT /id="VAR_071805"
FT VARIANT 58
FT /note="G -> R (in IMMD; associated in cis with S-15 in a
FT IMMD family; causes mitochondrial fragmentation;
FT dbSNP:rs730880033)"
FT /evidence="ECO:0000269|PubMed:25193783"
FT /id="VAR_073284"
FT VARIANT 59
FT /note="S -> L (in FTDALS2; results in disorganization of
FT mitochondrial cristae; dbSNP:rs587777574)"
FT /evidence="ECO:0000269|PubMed:24934289"
FT /id="VAR_071806"
FT VARIANT 66
FT /note="G -> V (in SMAJ; dbSNP:rs730880031)"
FT /evidence="ECO:0000269|PubMed:25428574"
FT /id="VAR_073285"
SQ SEQUENCE 142 AA; 14149 MW; A3AA3894CBEC0137 CRC64;
MPRGSRSAAS RPASRPAAPS AHPPAHPPPS AAAPAPAPSG QPGLMAQMAT TAAGVAVGSA
VGHVMGSALT GAFSGGSSEP SQPAVQQAPT PAAPQPLQMG PCAYEIRQFL DCSTTQSDLS
LCEGFSEALK QCKYYHGLSS LP
