NDUV1_HUMAN
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 03-AUG-2022, entry version 214.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE EC=7.1.1.2;
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;
DE Flags: Precursor;
GN Name=NDUFV1; 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]
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 [14]
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 [15]
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. {ECO:0000250|UniProtKB:P25708}.
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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 flavoprotein-sulfur (FP) fragment of the enzyme
CC (PubMed:12611891). Interacts with RAB5IF (PubMed:31536960).
CC {ECO:0000269|PubMed:12611891, 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}.
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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; 285.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; P49821; -.
DR IntAct; P49821; 87.
DR MINT; P49821; -.
DR STRING; 9606.ENSP00000322450; -.
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; P49821; -.
DR PeptideAtlas; P49821; -.
DR PRIDE; P49821; -.
DR ProteomicsDB; 56148; -. [P49821-1]
DR ProteomicsDB; 56149; -. [P49821-2]
DR Antibodypedia; 30465; 265 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 CTD; 4723; -.
DR DisGeNET; 4723; -.
DR GeneCards; NDUFV1; -.
DR GeneReviews; NDUFV1; -.
DR HGNC; HGNC:7716; NDUFV1.
DR HPA; ENSG00000167792; Tissue enhanced (skeletal).
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 Orphanet; 255241; Leigh syndrome with leukodystrophy.
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; CDDVIMD; -.
DR PhylomeDB; P49821; -.
DR TreeFam; TF300381; -.
DR BioCyc; MetaCyc:HS09641-MON; -.
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; 177 hits in 1085 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 199 other tissues.
DR ExpressionAtlas; P49821; baseline and differential.
DR Genevisible; P49821; HS.
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; NAS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC: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; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 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 Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
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:0000255"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
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
