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 09-APR-2025, entry version 203. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_014222.3. 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; 200. DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I. DR CORUM; P51970; -. DR IntAct; P51970; 84. 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 jPOST; P51970; -. DR MassIVE; P51970; -. DR PaxDb; 9606-ENSP00000362873; -. DR PeptideAtlas; P51970; -. DR ProteomicsDB; 56464; -. DR Pumba; P51970; -. DR TopDownProteomics; P51970; -. DR Antibodypedia; 30251; 273 antibodies from 31 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 AGR; HGNC:7692; -. DR CTD; 4702; -. DR DisGeNET; 4702; -. DR GeneCards; NDUFA8; -. DR HGNC; HGNC:7692; NDUFA8. DR HPA; ENSG00000119421; Tissue enhanced (heart). DR MalaCards; NDUFA8; -. 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; FRTHWQC; -. DR OrthoDB; 276296at2759; -. DR PhylomeDB; P51970; -. DR TreeFam; TF105633; -. DR BioCyc; MetaCyc:HS04297-MONOMER; -. 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; 299 hits in 1169 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 199 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0045271; C:respiratory chain complex I; 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; NAS:ComplexPortal. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. DR InterPro; IPR010625; CHCH. DR InterPro; IPR016680; NDUFA8. DR PANTHER; PTHR13344:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 8; 1. DR PANTHER; PTHR13344; NADH-UBIQUINONE OXIDOREDUCTASE; 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; Proteomics identification; KW Reference proteome; Repeat; 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 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; dbSNP:rs1319414797)" 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 //