NDUA8_HUMAN
ID NDUA8_HUMAN Reviewed; 172 AA.
AC P51970; B1AM93; Q9Y6N0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;
DE AltName: Full=Complex I-19kD;
DE Short=CI-19kD;
DE AltName: Full=Complex I-PGIV;
DE Short=CI-PGIV;
DE AltName: Full=NADH-ubiquinone oxidoreductase 19 kDa subunit;
GN Name=NDUFA8;
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 [MRNA].
RX PubMed=9860297; DOI=10.1007/s004390050869;
RA Triepels R., van den Heuvel L., Loeffen J., Smeets R., Trijbels F.,
RA Smeitink J.;
RT "The nuclear-encoded human NADH:ubiquinone oxidoreductase NDUFA8 subunit:
RT cDNA cloning, chromosomal localization, tissue distribution, and mutation
RT detection in complex-I-deficient patients.";
RL Hum. Genet. 103:557-563(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [6]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Kidney;
RX PubMed=9150947; DOI=10.1002/elps.1150180343;
RA Sarto C., Marocchi A., Sanchez J.-C., Giannone B., Frutiger S., Golaz O.,
RA Wilkins M.R., Doro G., Cappellano F., Hughes G.J., Hochstrasser D.F.,
RA Mocarelli P.;
RT "Renal cell carcinoma and normal kidney protein expression.";
RL Electrophoresis 18:599-604(1997).
RN [7]
RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA Ghosh S.S., Capaldi R.A.;
RT "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT one-step immunopurification.";
RL J. Biol. Chem. 278:13619-13622(2003).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION, SUBUNIT, AND PROBABLE DISULFIDE BOND.
RX PubMed=21310150; DOI=10.1016/j.febslet.2011.01.046;
RA Szklarczyk R., Wanschers B.F., Nabuurs S.B., Nouws J., Nijtmans L.G.,
RA Huynen M.A.;
RT "NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I.";
RL FEBS Lett. 585:737-743(2011).
RN [10]
RP SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
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 [11]
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 [12]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP 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, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=27626371; DOI=10.1038/nature19754;
RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA Salim A., Ryan M.T.;
RT "Accessory subunits are integral for assembly and function of human
RT mitochondrial complex I.";
RL Nature 538:123-126(2016).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-140.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP INVOLVEMENT IN MC1DN37, VARIANT MC1DN37 CYS-47, CHARACTERIZATION OF VARIANT
RP MC1DN37 CYS-47, AND FUNCTION.
RX PubMed=32385911; DOI=10.1111/cge.13773;
RA Yatsuka Y., Kishita Y., Formosa L.E., Shimura M., Nozaki F., Fujii T.,
RA Nitta K.R., Ohtake A., Murayama K., Ryan M.T., Okazaki Y.;
RT "A homozygous variant in NDUFA8 is associated with developmental delay,
RT microcephaly, and epilepsy due to mitochondrial complex I deficiency.";
RL Clin. Genet. 98:155-165(2020).
RN [16]
RP VARIANT MC1DN37 LEU-98, CHARACTERIZATION OF VARIANT MC1DN37 LEU-98, AND
RP FUNCTION.
RX PubMed=33153867; DOI=10.1016/j.ymgme.2020.10.005;
RA Tort F., Barredo E., Parthasarathy R., Ugarteburu O., Ferrer-Cortes X.,
RA Garcia-Villoria J., Gort L., Gonzalez-Quintana A., Martin M.A.,
RA Fernandez-Vizarra E., Zeviani M., Ribes A.;
RT "Biallelic mutations in NDUFA8 cause complex I deficiency in two siblings
RT with favorable clinical evolution.";
RL Mol. Genet. Metab. 131:349-357(2020).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis (PubMed:27626371, PubMed:32385911,
CC PubMed:33153867). Complex I functions in the transfer of electrons from
CC NADH to the respiratory chain (PubMed:27626371). The immediate electron
CC acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371).
CC {ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:32385911,
CC ECO:0000269|PubMed:33153867}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:21310150,
CC ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC P51970; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1237250, EBI-10976677;
CC P51970; O75489: NDUFS3; NbExp=5; IntAct=EBI-1237250, EBI-1224896;
CC P51970; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1237250, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21310150}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:21310150}. Mitochondrion
CC {ECO:0000269|PubMed:23676665}.
CC -!- DOMAIN: Contains four C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000305|PubMed:21310150}.
CC -!- PTM: May contain intrachain disulfide bonds, as evidenced by its
CC electrophoretic mobility under reducing vs non-reducing conditions.
CC {ECO:0000269|PubMed:21310150}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 37 (MC1DN37)
CC [MIM:619272]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN37 features include developmental delay,
CC cerebral atrophy, epilepsy, growth retardation, congenital myopathy
CC with disproportion of fibers, and severely decreased activity of
CC complex I. MC1DN37 transmission pattern is consistent with autosomal
CC recessive inheritance. {ECO:0000269|PubMed:32385911,
CC ECO:0000269|PubMed:33153867}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the complex I NDUFA8 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044953; AAD42056.1; -; mRNA.
DR EMBL; AK314135; BAG36825.1; -; mRNA.
DR EMBL; AL162423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87511.1; -; Genomic_DNA.
DR EMBL; BC001016; AAH01016.1; -; mRNA.
DR CCDS; CCDS6835.1; -.
DR RefSeq; NP_055037.1; NM_014222.2.
DR PDB; 5XTC; EM; 3.70 A; u=4-172.
DR PDB; 5XTD; EM; 3.70 A; u=4-172.
DR PDB; 5XTH; EM; 3.90 A; u=4-172.
DR PDB; 5XTI; EM; 17.40 A; Bu/u=4-172.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P51970; -.
DR SMR; P51970; -.
DR BioGRID; 110782; 173.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; P51970; -.
DR IntAct; P51970; 79.
DR MINT; P51970; -.
DR STRING; 9606.ENSP00000362873; -.
DR BindingDB; P51970; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P51970; -.
DR GlyGen; P51970; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51970; -.
DR PhosphoSitePlus; P51970; -.
DR SwissPalm; P51970; -.
DR BioMuta; NDUFA8; -.
DR DMDM; 8039804; -.
DR SWISS-2DPAGE; P51970; -.
DR UCD-2DPAGE; P51970; -.
DR EPD; P51970; -.
DR jPOST; P51970; -.
DR MassIVE; P51970; -.
DR MaxQB; P51970; -.
DR PaxDb; P51970; -.
DR PeptideAtlas; P51970; -.
DR PRIDE; P51970; -.
DR ProteomicsDB; 56464; -.
DR TopDownProteomics; P51970; -.
DR Antibodypedia; 30251; 227 antibodies from 30 providers.
DR DNASU; 4702; -.
DR Ensembl; ENST00000373768.4; ENSP00000362873.3; ENSG00000119421.7.
DR GeneID; 4702; -.
DR KEGG; hsa:4702; -.
DR MANE-Select; ENST00000373768.4; ENSP00000362873.3; NM_014222.3; NP_055037.1.
DR UCSC; uc004blv.4; human.
DR CTD; 4702; -.
DR DisGeNET; 4702; -.
DR GeneCards; NDUFA8; -.
DR HGNC; HGNC:7692; NDUFA8.
DR HPA; ENSG00000119421; Tissue enhanced (heart muscle, tongue).
DR MIM; 603359; gene.
DR MIM; 619272; phenotype.
DR neXtProt; NX_P51970; -.
DR OpenTargets; ENSG00000119421; -.
DR PharmGKB; PA31498; -.
DR VEuPathDB; HostDB:ENSG00000119421; -.
DR eggNOG; KOG3458; Eukaryota.
DR GeneTree; ENSGT00390000008938; -.
DR HOGENOM; CLU_081931_2_1_1; -.
DR InParanoid; P51970; -.
DR OMA; DRPNKEF; -.
DR OrthoDB; 1526152at2759; -.
DR PhylomeDB; P51970; -.
DR TreeFam; TF105633; -.
DR BioCyc; MetaCyc:HS04297-MON; -.
DR PathwayCommons; P51970; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; P51970; -.
DR SIGNOR; P51970; -.
DR BioGRID-ORCS; 4702; 295 hits in 1089 CRISPR screens.
DR ChiTaRS; NDUFA8; human.
DR GeneWiki; NDUFA8; -.
DR GenomeRNAi; 4702; -.
DR Pharos; P51970; Tclin.
DR PRO; PR:P51970; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P51970; protein.
DR Bgee; ENSG00000119421; Expressed in apex of heart and 197 other tissues.
DR Genevisible; P51970; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR016680; NDUFA8.
DR PANTHER; PTHR13344; PTHR13344; 1.
DR Pfam; PF06747; CHCH; 1.
DR PIRSF; PIRSF017016; NDUA8; 1.
DR PROSITE; PS51808; CHCH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Repeat;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9150947,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..172
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 8"
FT /id="PRO_0000118734"
FT DOMAIN 33..74
FT /note="CHCH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DOMAIN 75..118
FT /note="CHCH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 133..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..46
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 56..66
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 78..88
FT /note="Cx9C motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 100..110
FT /note="Cx9C motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 133..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 36..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT DISULFID 46..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT DISULFID 78..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT DISULFID 88..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150,
FT ECO:0000305|PubMed:23676665"
FT VARIANT 47
FT /note="R -> C (in MC1DN37; reduced enzymatic activity of
FT the respiratory chain complex I; reduced NDUFA8 protein
FT levels; decrease in respiratory supercomplexes comprising
FT complex I (CI/CIII 2/CIV and CI/CIII 2) as well as an
FT increase in unintegrated complex III dimers;
FT dbSNP:rs767864225)"
FT /evidence="ECO:0000269|PubMed:32385911"
FT /id="VAR_085554"
FT VARIANT 98
FT /note="R -> L (in MC1DN37; defect in the assembly of
FT respiratory chain complex I; reduced enzymatic activity of
FT the respiratory chain complex I; altered fibroblast
FT mitochondria morphology and reduced mitochondrial network
FT branching; no significant differences in mitochondrial
FT respiratory capacity)"
FT /evidence="ECO:0000269|PubMed:33153867"
FT /id="VAR_085555"
FT VARIANT 140
FT /note="N -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036176"
SQ SEQUENCE 172 AA; 20105 MW; E1647472B69E1149 CRC64;
MPGIVELPTL EELKVDEVKI SSAVLKAAAH HYGAQCDKPN KEFMLCRWEE KDPRRCLEEG
KLVNKCALDF FRQIKRHCAE PFTEYWTCID YTGQQLFRHC RKQQAKFDEC VLDKLGWVRP
DLGELSKVTK VKTDRPLPEN PYHSRPRPDP SPEIEGDLQP ATHGSRFYFW TK
