ID NDUV1_HUMAN Reviewed; 464 AA. AC P49821; O60924; O60940; Q16104; Q6IBR3; Q96BF8; Q96HS7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 4. DT 27-MAR-2024, entry version 223. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; DE Short=NDUFV1 {ECO:0000303|PubMed:9571201}; DE EC=7.1.1.2 {ECO:0000305|PubMed:28844695}; DE AltName: Full=Complex I-51kD; DE Short=CI-51kD; DE AltName: Full=NADH dehydrogenase flavoprotein 1; DE AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit {ECO:0000303|PubMed:9571201}; DE Flags: Precursor; GN Name=NDUFV1 {ECO:0000312|HGNC:HGNC:7716}; Synonyms=UQOR1; 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]. RX PubMed=9892733; DOI=10.1007/s003359900941; RA de Coo R.F.M., Buddiger P.A., Smeets H.J.M., van Oost B.A.; RT "The structure of the human NDUFV1 gene encoding the 51-kDa subunit of RT mitochondrial complex I."; RL Mamm. Genome 10:49-53(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=9571201; DOI=10.1006/bbrc.1998.8486; RA Schuelke M., Loeffen J., Mariman E., Smeitink J., van den Heuvel L.; RT "Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% RT antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon RT inducible protein (IP-30) precursor: is this a link between mitochondrial RT myopathy and inflammation?"; RL Biochem. Biophys. Res. Commun. 245:599-606(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Eye; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130. RX PubMed=1478657; DOI=10.1016/s0888-7543(05)80144-2; RA Spencer S.R., Taylor J.B., Cowell I.G., Xia C.L., Pemble S.E., Ketterer B.; RT "The human mitochondrial NADH: ubiquinone oxidoreductase 51-kDa subunit RT maps adjacent to the glutathione S-transferase P1-1 gene on chromosome RT 11q13."; RL Genomics 14:1116-1118(1992). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-305. RC TISSUE=Kidney; RX PubMed=8288251; DOI=10.1006/geno.1993.1493; RA Ali S.T., Duncan A.M.V., Schappert K.T., Heng H.H.Q., Tsui L.-C., Chow W., RA Robinson B.H.; RT "Chromosomal localization of the human gene encoding the 51-kDa subunit of RT mitochondrial complex I (NDUFV1) to 11q13."; RL Genomics 18:435-439(1993). RN [9] 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 [10] 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 [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 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] {ECO:0007744|PDB:5XTB, ECO:0007744|PDB:5XTD, ECO:0007744|PDB:5XTH, ECO:0007744|PDB:5XTI} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 27-457, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT. RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050; RA Guo R., Zong S., Wu M., Gu J., Yang M.; RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2."; RL Cell 170:1247-1257(2017). RN [14] 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 [15] RP INVOLVEMENT IN MC1DN4, AND VARIANTS MC1DN4 VAL-341 AND MET-423. RX PubMed=10080174; DOI=10.1038/6772; RA Schuelke M., Smeitink J., Mariman E., Loeffen J., Plecko B., Trijbels F., RA Stockler-Ipsiroglu S., van den Heuvel L.; RT "Mutant NDUFV1 subunit of mitochondrial complex I causes leukodystrophy and RT myoclonic epilepsy."; RL Nat. Genet. 21:260-261(1999). RN [16] RP INVOLVEMENT IN MC1DN4, AND VARIANT MC1DN4 LYS-214. RX PubMed=11349233; DOI=10.1086/320603; RA Benit P., Chretien D., Kadhom N., de Lonlay-Debeney P., Cormier-Daire V., RA Cabral A., Peudenier S., Rustin P., Munnich A., Roetig A.; RT "Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 RT genes in mitochondrial complex I deficiency."; RL Am. J. Hum. Genet. 68:1344-1352(2001). 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:28844695). Part of the peripheral arm of the enzyme, CC where the electrons from NADH are accepted by flavin mononucleotide CC (FMN) and then passed along a chain of iron-sulfur clusters by electron CC tunnelling to the final acceptor ubiquinone (PubMed:28844695). Contains CC FMN, which is the initial electron acceptor as well as one iron-sulfur CC cluster (PubMed:28844695). {ECO:0000269|PubMed:28844695}. 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:0000305|PubMed:28844695}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; CC Evidence={ECO:0000305|PubMed:28844695}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:28844695}; CC Note=Binds 1 FMN. {ECO:0000269|PubMed:28844695}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:28844695}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:28844695}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits (PubMed:12611891, CC PubMed:28844695). This is a component of the flavoprotein-sulfur (FP) CC fragment of the enzyme (PubMed:12611891). Interacts with RAB5IF CC (PubMed:31536960). {ECO:0000269|PubMed:12611891, CC ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:31536960}. CC -!- INTERACTION: CC P49821; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-748312, EBI-2875816; CC P49821; Q9Y297: BTRC; NbExp=3; IntAct=EBI-748312, EBI-307461; CC P49821; P61201: COPS2; NbExp=3; IntAct=EBI-748312, EBI-1050386; CC P49821; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-748312, EBI-3867333; CC P49821; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-748312, EBI-8468186; CC P49821; Q8TCJ0-3: FBXO25; NbExp=3; IntAct=EBI-748312, EBI-6262578; CC P49821; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-748312, EBI-2506081; CC P49821; Q92993: KAT5; NbExp=3; IntAct=EBI-748312, EBI-399080; CC P49821; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-748312, EBI-11742507; CC P49821; P41218: MNDA; NbExp=3; IntAct=EBI-748312, EBI-2829677; CC P49821; P56181: NDUFV3; NbExp=2; IntAct=EBI-748312, EBI-721902; CC P49821; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-748312, EBI-9091423; CC P49821; P17252: PRKCA; NbExp=3; IntAct=EBI-748312, EBI-1383528; CC P49821; P25788-2: PSMA3; NbExp=3; IntAct=EBI-748312, EBI-348394; CC P49821; P20618: PSMB1; NbExp=3; IntAct=EBI-748312, EBI-372273; CC P49821; Q16401: PSMD5; NbExp=3; IntAct=EBI-748312, EBI-752143; CC P49821; Q7Z6E9-3: RBBP6; NbExp=3; IntAct=EBI-748312, EBI-11743772; CC P49821; Q9H871: RMND5A; NbExp=3; IntAct=EBI-748312, EBI-2797992; CC P49821; Q9NTX7-2: RNF146; NbExp=3; IntAct=EBI-748312, EBI-11750630; CC P49821; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-748312, EBI-9090795; CC P49821; Q2TAY7: SMU1; NbExp=3; IntAct=EBI-748312, EBI-298027; CC P49821; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-748312, EBI-11959123; CC P49821; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-748312, EBI-21575846; CC P49821; Q96B65: USP25; NbExp=3; IntAct=EBI-748312, EBI-25876491; CC P49821; P45880: VDAC2; NbExp=3; IntAct=EBI-748312, EBI-354022; CC P49821; P61981: YWHAG; NbExp=3; IntAct=EBI-748312, EBI-359832; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P25708}; Matrix side CC {ECO:0000250|UniProtKB:P25708}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49821-1; Sequence=Displayed; CC Name=2; CC IsoId=P49821-2; Sequence=VSP_003730; CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 4 (MC1DN4) CC [MIM:618225]: 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. MC1DN4 transmission pattern is consistent with CC autosomal recessive inheritance. {ECO:0000269|PubMed:10080174, CC ECO:0000269|PubMed:11349233}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the complex I 51 kDa 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; Y17379; CAA76757.1; -; Genomic_DNA. DR EMBL; Y17380; CAA76757.1; JOINED; Genomic_DNA. DR EMBL; Y17381; CAA76757.1; JOINED; Genomic_DNA. DR EMBL; Y17382; CAA76757.1; JOINED; Genomic_DNA. DR EMBL; Y17383; CAA76757.1; JOINED; Genomic_DNA. DR EMBL; AF053069; AAC39750.1; -; Genomic_DNA. DR EMBL; AF053070; AAC39722.1; -; mRNA. DR EMBL; AF092131; AAD40373.1; -; mRNA. DR EMBL; CR456739; CAG33020.1; -; mRNA. DR EMBL; CH471076; EAW74655.1; -; Genomic_DNA. DR EMBL; BC008146; AAH08146.1; -; mRNA. DR EMBL; BC015645; AAH15645.1; -; mRNA. DR EMBL; AH004147; AAB24883.1; -; Genomic_DNA. DR EMBL; S67973; AAB29698.2; ALT_SEQ; mRNA. DR CCDS; CCDS53669.1; -. [P49821-2] DR CCDS; CCDS8173.1; -. [P49821-1] DR PIR; JE0092; JE0092. DR RefSeq; NP_001159574.1; NM_001166102.1. [P49821-2] DR RefSeq; NP_009034.2; NM_007103.3. [P49821-1] DR PDB; 5XTB; EM; 3.40 A; A=27-457. DR PDB; 5XTD; EM; 3.70 A; A=27-457. DR PDB; 5XTH; EM; 3.90 A; A=27-457. DR PDB; 5XTI; EM; 17.40 A; A/BA=27-457. DR PDBsum; 5XTB; -. DR PDBsum; 5XTD; -. DR PDBsum; 5XTH; -. DR PDBsum; 5XTI; -. DR AlphaFoldDB; P49821; -. DR SMR; P49821; -. DR BioGRID; 110802; 302. DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I. DR CORUM; P49821; -. DR IntAct; P49821; 92. DR MINT; P49821; -. DR STRING; 9606.ENSP00000497587; -. DR BindingDB; P49821; -. DR ChEMBL; CHEMBL2363065; -. DR DrugBank; DB00157; NADH. DR DrugCentral; P49821; -. DR CarbonylDB; P49821; -. DR GlyGen; P49821; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P49821; -. DR PhosphoSitePlus; P49821; -. DR SwissPalm; P49821; -. DR BioMuta; NDUFV1; -. DR DMDM; 20455501; -. DR REPRODUCTION-2DPAGE; IPI00028520; -. DR REPRODUCTION-2DPAGE; IPI00221298; -. DR EPD; P49821; -. DR jPOST; P49821; -. DR MassIVE; P49821; -. DR MaxQB; P49821; -. DR PaxDb; 9606-ENSP00000322450; -. DR PeptideAtlas; P49821; -. DR ProteomicsDB; 56148; -. [P49821-1] DR ProteomicsDB; 56149; -. [P49821-2] DR Pumba; P49821; -. DR Antibodypedia; 30465; 295 antibodies from 30 providers. DR DNASU; 4723; -. DR Ensembl; ENST00000322776.11; ENSP00000322450.6; ENSG00000167792.13. [P49821-1] DR Ensembl; ENST00000529927.5; ENSP00000436766.1; ENSG00000167792.13. [P49821-2] DR Ensembl; ENST00000647561.1; ENSP00000497587.1; ENSG00000167792.13. [P49821-1] DR GeneID; 4723; -. DR KEGG; hsa:4723; -. DR MANE-Select; ENST00000322776.11; ENSP00000322450.6; NM_007103.4; NP_009034.2. DR UCSC; uc001omj.3; human. [P49821-1] DR AGR; HGNC:7716; -. DR CTD; 4723; -. DR DisGeNET; 4723; -. DR GeneCards; NDUFV1; -. DR GeneReviews; NDUFV1; -. DR HGNC; HGNC:7716; NDUFV1. DR HPA; ENSG00000167792; Low tissue specificity. DR MalaCards; NDUFV1; -. DR MIM; 161015; gene. DR MIM; 618225; phenotype. DR neXtProt; NX_P49821; -. DR OpenTargets; ENSG00000167792; -. DR Orphanet; 2609; Isolated complex I deficiency. DR PharmGKB; PA31526; -. DR VEuPathDB; HostDB:ENSG00000167792; -. DR eggNOG; KOG2658; Eukaryota. DR GeneTree; ENSGT00390000010641; -. DR HOGENOM; CLU_014881_0_1_1; -. DR InParanoid; P49821; -. DR OMA; KWQFIPQ; -. DR OrthoDB; 5483539at2759; -. DR PhylomeDB; P49821; -. DR TreeFam; TF300381; -. DR BioCyc; MetaCyc:HS09641-MONOMER; -. DR PathwayCommons; P49821; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR Reactome; R-HSA-6799198; Complex I biogenesis. DR SignaLink; P49821; -. DR SIGNOR; P49821; -. DR BioGRID-ORCS; 4723; 188 hits in 1175 CRISPR screens. DR ChiTaRS; NDUFV1; human. DR GeneWiki; NDUFV1; -. DR GenomeRNAi; 4723; -. DR Pharos; P49821; Tclin. DR PRO; PR:P49821; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P49821; Protein. DR Bgee; ENSG00000167792; Expressed in apex of heart and 201 other cell types or tissues. DR ExpressionAtlas; P49821; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:UniProtKB. DR GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal. DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:CAFA. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:UniProtKB. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. DR Gene3D; 3.10.20.600; -; 1. DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1. DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR037225; Nuo51_FMN-bd_sf. DR InterPro; IPR019575; Nuop51_4Fe4S-bd. DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf. DR NCBIfam; TIGR01959; nuoF_fam; 1. DR PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1. DR PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1. DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1. DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1. DR PROSITE; PS00644; COMPLEX1_51K_1; 1. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. DR Genevisible; P49821; HS. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Acetylation; Alternative splicing; Disease variant; KW Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Leigh syndrome; KW Membrane; Metal-binding; Methylation; Mitochondrion; KW Mitochondrion inner membrane; NAD; Oxidoreductase; KW Primary mitochondrial disease; Reference proteome; Respiratory chain; KW Transit peptide; Translocase; Transport; Ubiquinone. FT TRANSIT 1..20 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 21..464 FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 1, FT mitochondrial" FT /id="PRO_0000019976" FT BINDING 87..96 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250" FT BINDING 199..247 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:28844695, FT ECO:0007744|PDB:5XTB, ECO:0007744|PDB:5XTD, FT ECO:0007744|PDB:5XTH, ECO:0007744|PDB:5XTI" FT BINDING 382 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:28844695, FT ECO:0007744|PDB:5XTB, ECO:0007744|PDB:5XTD, FT ECO:0007744|PDB:5XTH, ECO:0007744|PDB:5XTI" FT BINDING 385 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:28844695, FT ECO:0007744|PDB:5XTB, ECO:0007744|PDB:5XTD, FT ECO:0007744|PDB:5XTH, ECO:0007744|PDB:5XTI" FT BINDING 425 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:28844695, FT ECO:0007744|PDB:5XTB, ECO:0007744|PDB:5XTD, FT ECO:0007744|PDB:5XTH, ECO:0007744|PDB:5XTI" FT MOD_RES 81 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91YT0" FT MOD_RES 81 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91YT0" FT MOD_RES 104 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91YT0" FT MOD_RES 257 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q91YT0" FT MOD_RES 375 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91YT0" FT VAR_SEQ 16..24 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_003730" FT VARIANT 76 FT /note="I -> V (in dbSNP:rs1800670)" FT /id="VAR_014480" FT VARIANT 214 FT /note="E -> K (in MC1DN4; dbSNP:rs121913661)" FT /evidence="ECO:0000269|PubMed:11349233" FT /id="VAR_019534" FT VARIANT 277 FT /note="N -> Y (in dbSNP:rs1043770)" FT /id="VAR_014481" FT VARIANT 341 FT /note="A -> V (in MC1DN4; dbSNP:rs121913660)" FT /evidence="ECO:0000269|PubMed:10080174" FT /id="VAR_008846" FT VARIANT 423 FT /note="T -> M (in MC1DN4; dbSNP:rs121913659)" FT /evidence="ECO:0000269|PubMed:10080174" FT /id="VAR_008847" FT CONFLICT 80 FT /note="I -> V (in Ref. 7; AAB24883)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="G -> A (in Ref. 8; AAB29698)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="G -> F (in Ref. 1; CAA76757)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="N -> Y (in Ref. 1; CAA76757)" FT /evidence="ECO:0000305" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 53..58 FT /evidence="ECO:0007829|PDB:5XTB" FT TURN 59..68 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 75..81 FT /evidence="ECO:0007829|PDB:5XTB" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 95..100 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 126..133 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 135..149 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 164..178 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 204..207 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 209..216 FT /evidence="ECO:0007829|PDB:5XTB" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 245..256 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 272..284 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 296..301 FT /evidence="ECO:0007829|PDB:5XTB" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 314..322 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 329..332 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 339..344 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 353..358 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 364..376 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 383..401 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 408..419 FT /evidence="ECO:0007829|PDB:5XTB" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:5XTB" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:5XTB" FT HELIX 427..454 FT /evidence="ECO:0007829|PDB:5XTB" SQ SEQUENCE 464 AA; 50817 MW; 8C261EA3B0267256 CRC64; MLATRRLLGW SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGSLSRG DWYKTKEILL KGPDWILGEI KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG EPGTCKDREI LRHDPHKLLE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG LIGKNACGSG YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV RGDARPAEID SLWEISKQIE GHTICALGDG AAWPVQGLIR HFRPELEERM QRFAQQHQAR QAAS //