ID NDUS8_HUMAN Reviewed; 210 AA.
AC O00217; B2RB86; Q0VDA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE EC=7.1.1.2 {ECO:0000269|PubMed:22499348};
DE AltName: Full=Complex I-23kD;
DE Short=CI-23kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE AltName: Full=TYKY subunit;
DE Flags: Precursor;
GN Name=NDUFS8;
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 / MRNA].
RX PubMed=9116042; DOI=10.1016/s0167-4781(97)00020-1;
RA Procaccio V., Depetris D., Soularue P., Mattei M.-G., Lunardi J.,
RA Issartel J.-P.;
RT "cDNA sequence and chromosomal localization of the NDUFS8 human gene coding
RT for the 23 kDa subunit of the mitochondrial complex I.";
RL Biochim. Biophys. Acta 1351:37-41(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9666055; DOI=10.1016/s0378-1119(98)00275-3;
RA de Sury R., Martinez P., Procaccio V., Lunardi J., Issartel J.-P.;
RT "Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY
RT subunit of the mitochondrial NADH:ubiquinone oxidoreductase.";
RL Gene 215:1-10(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE
RP OXIDOREDUCTASE COMPLEX, AND SUBCELLULAR LOCATION.
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 [6]
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 [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
RN [10]
RP INVOLVEMENT IN MC1DN2, AND VARIANTS MC1DN2 LEU-79 AND HIS-102.
RX PubMed=9837812; DOI=10.1086/302154;
RA Loeffen J., Smeitink J., Triepels R., Smeets R., Schuelke M., Sengers R.,
RA Trijbels F., Hamel B.C.J., Mullaart R., van den Heuvel L.;
RT "The first nuclear-encoded complex I mutation in a patient with Leigh
RT syndrome.";
RL Am. J. Hum. Genet. 63:1598-1608(1998).
RN [11]
RP VARIANTS MC1DN2 LEU-85 AND HIS-138.
RX PubMed=15159508; DOI=10.1212/01.wnl.0000125251.56131.65;
RA Procaccio V., Wallace D.C.;
RT "Late-onset Leigh syndrome in a patient with mitochondrial complex I NDUFS8
RT mutations.";
RL Neurology 62:1899-1901(2004).
RN [12]
RP VARIANT MC1DN2 CYS-18.
RX PubMed=16142472; DOI=10.1007/s00109-005-0712-y;
RA Hinttala R., Uusimaa J., Remes A.M., Rantala H., Hassinen I.E., Majamaa K.;
RT "Sequence analysis of nuclear genes encoding functionally important complex
RT I subunits in children with encephalomyopathy.";
RL J. Mol. Med. 83:786-794(2005).
RN [13]
RP VARIANTS MC1DN2 GLN-63; TRP-77 AND ASP-159, CHARACTERIZATION OF VARIANTS
RP MC1DN2 GLN-63; TRP-77 AND ASP-159, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22499348; DOI=10.1136/jmedgenet-2012-100846;
RA Haack T.B., Haberberger B., Frisch E.M., Wieland T., Iuso A., Gorza M.,
RA Strecker V., Graf E., Mayr J.A., Herberg U., Hennermann J.B., Klopstock T.,
RA Kuhn K.A., Ahting U., Sperl W., Wilichowski E., Hoffmann G.F., Tesarova M.,
RA Hansikova H., Zeman J., Plecko B., Zeviani M., Wittig I., Strom T.M.,
RA Schuelke M., Freisinger P., Meitinger T., Prokisch H.;
RT "Molecular diagnosis in mitochondrial complex I deficiency using exome
RT sequencing.";
RL J. Med. Genet. 49:277-283(2012).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor (PubMed:22499348). Essential for the catalytic activity and
CC assembly of complex I (PubMed:22499348). {ECO:0000269|PubMed:22499348}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000269|PubMed:22499348};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q56224};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q56224};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (PubMed:12611891). This
CC is a component of the iron-sulfur (IP) fragment of the enzyme (By
CC similarity). Interacts with RAB5IF (PubMed:31536960).
CC {ECO:0000250|UniProtKB:P42028, ECO:0000269|PubMed:12611891,
CC ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:9666055}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P42028}; Matrix side
CC {ECO:0000250|UniProtKB:P42028}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues with the highest level in
CC heart and skeletal muscle and the lowest level in lung.
CC {ECO:0000269|PubMed:9666055}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 2 (MC1DN2)
CC [MIM:618222]: 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. MC1DN2 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:15159508, ECO:0000269|PubMed:16142472,
CC ECO:0000269|PubMed:22499348, ECO:0000269|PubMed:9837812}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U65579; AAB51776.1; -; mRNA.
DR EMBL; AF038406; AAC34273.1; -; Genomic_DNA.
DR EMBL; AK314546; BAG37133.1; -; mRNA.
DR EMBL; BC119754; AAI19755.1; -; mRNA.
DR CCDS; CCDS8176.1; -.
DR RefSeq; NP_002487.1; NM_002496.3.
DR RefSeq; XP_005274070.1; XM_005274013.1.
DR RefSeq; XP_005274071.1; XM_005274014.2.
DR RefSeq; XP_011543355.1; XM_011545053.2.
DR PDB; 5XTB; EM; 3.40 A; B=35-210.
DR PDB; 5XTD; EM; 3.70 A; B=35-210.
DR PDB; 5XTH; EM; 3.90 A; B=35-210.
DR PDB; 5XTI; EM; 17.40 A; B/BB=35-210.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O00217; -.
DR SMR; O00217; -.
DR BioGRID; 110806; 257.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O00217; -.
DR IntAct; O00217; 58.
DR MINT; O00217; -.
DR STRING; 9606.ENSP00000315774; -.
DR BindingDB; O00217; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O00217; -.
DR CarbonylDB; O00217; -.
DR GlyGen; O00217; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00217; -.
DR PhosphoSitePlus; O00217; -.
DR SwissPalm; O00217; -.
DR BioMuta; NDUFS8; -.
DR OGP; O00217; -.
DR EPD; O00217; -.
DR jPOST; O00217; -.
DR MassIVE; O00217; -.
DR MaxQB; O00217; -.
DR PaxDb; 9606-ENSP00000315774; -.
DR PeptideAtlas; O00217; -.
DR ProteomicsDB; 47787; -.
DR Pumba; O00217; -.
DR TopDownProteomics; O00217; -.
DR Antibodypedia; 1263; 293 antibodies from 34 providers.
DR DNASU; 4728; -.
DR Ensembl; ENST00000313468.10; ENSP00000315774.5; ENSG00000110717.13.
DR GeneID; 4728; -.
DR KEGG; hsa:4728; -.
DR MANE-Select; ENST00000313468.10; ENSP00000315774.5; NM_002496.4; NP_002487.1.
DR UCSC; uc001onc.4; human.
DR AGR; HGNC:7715; -.
DR CTD; 4728; -.
DR DisGeNET; 4728; -.
DR GeneCards; NDUFS8; -.
DR GeneReviews; NDUFS8; -.
DR HGNC; HGNC:7715; NDUFS8.
DR HPA; ENSG00000110717; Low tissue specificity.
DR MalaCards; NDUFS8; -.
DR MIM; 602141; gene.
DR MIM; 618222; phenotype.
DR neXtProt; NX_O00217; -.
DR OpenTargets; ENSG00000110717; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA31525; -.
DR VEuPathDB; HostDB:ENSG00000110717; -.
DR eggNOG; KOG3256; Eukaryota.
DR GeneTree; ENSGT00390000003049; -.
DR HOGENOM; CLU_067218_5_1_1; -.
DR InParanoid; O00217; -.
DR OMA; QFFRAPY; -.
DR OrthoDB; 176717at2759; -.
DR PhylomeDB; O00217; -.
DR TreeFam; TF105610; -.
DR BioCyc; MetaCyc:HS03332-MONOMER; -.
DR PathwayCommons; O00217; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O00217; -.
DR SIGNOR; O00217; -.
DR BioGRID-ORCS; 4728; 296 hits in 1173 CRISPR screens.
DR ChiTaRS; NDUFS8; human.
DR GeneWiki; NDUFS8; -.
DR GenomeRNAi; 4728; -.
DR Pharos; O00217; Tclin.
DR PRO; PR:O00217; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O00217; Protein.
DR Bgee; ENSG00000110717; Expressed in apex of heart and 208 other cell types or tissues.
DR ExpressionAtlas; O00217; baseline and differential.
DR Genevisible; O00217; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP: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; NAS:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR Gene3D; 3.30.70.3270; -; 1.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR NCBIfam; TIGR01971; NuoI; 1.
DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Disease variant; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Primary mitochondrial disease; Reference proteome; Repeat;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P42028"
FT CHAIN 35..210
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 8, mitochondrial"
FT /id="PRO_0000020012"
FT DOMAIN 102..131
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 141..170
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT VARIANT 18
FT /note="R -> C (in MC1DN2; uncertain significance;
FT dbSNP:rs750062334)"
FT /evidence="ECO:0000269|PubMed:16142472"
FT /id="VAR_083603"
FT VARIANT 63
FT /note="E -> Q (in MC1DN2; decrease in enzyme activity;
FT impaired assembly of complex I; dbSNP:rs397514618)"
FT /evidence="ECO:0000269|PubMed:22499348"
FT /id="VAR_081440"
FT VARIANT 77
FT /note="R -> W (in MC1DN2; uncertain significance; decrease
FT in enzyme activity; impaired assembly of complex I;
FT dbSNP:rs146766138)"
FT /evidence="ECO:0000269|PubMed:22499348"
FT /id="VAR_081441"
FT VARIANT 79
FT /note="P -> L (in MC1DN2; dbSNP:rs28939679)"
FT /evidence="ECO:0000269|PubMed:9837812"
FT /id="VAR_019538"
FT VARIANT 85
FT /note="P -> L (in MC1DN2; uncertain significance;
FT dbSNP:rs121912639)"
FT /evidence="ECO:0000269|PubMed:15159508"
FT /id="VAR_081442"
FT VARIANT 102
FT /note="R -> H (in MC1DN2; dbSNP:rs121912638)"
FT /evidence="ECO:0000269|PubMed:9837812"
FT /id="VAR_019539"
FT VARIANT 138
FT /note="R -> H (in MC1DN2; uncertain significance;
FT dbSNP:rs111033588)"
FT /evidence="ECO:0000269|PubMed:15159508"
FT /id="VAR_081443"
FT VARIANT 159
FT /note="A -> D (in MC1DN2; uncertain significance; decrease
FT in enzyme activity; impaired assembly of complex I;
FT dbSNP:rs397514617)"
FT /evidence="ECO:0000269|PubMed:22499348"
FT /id="VAR_081444"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 210 AA; 23705 MW; 8C3EBD205BFA0112 CRC64;
MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL
WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI
CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE
LLYNKEKLLN NGDKWEAEIA ANIQADYLYR
//
