ID NDUV2_BOVIN Reviewed; 249 AA. AC P04394; Q3T0G9; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 3. DT 24-JAN-2024, entry version 192. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; DE EC=7.1.1.2 {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}; DE AltName: Full=NADH dehydrogenase subunit II; DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit {ECO:0000303|PubMed:18721790}; DE Flags: Precursor; GN Name=NDUFV2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2500970; DOI=10.1021/bi00434a021; RA Pilkington S.J., Walker J.E.; RT "Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of RT import precursors of the bovine and human 24-kDa subunit."; RL Biochemistry 28:3257-3264(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-249. RC TISSUE=Brain; RX PubMed=2598272; DOI=10.1007/bf00393404; RA Chomyn A., Tsai Lai S.S.-A.; RT "cDNA of the 24 kDa subunit of the bovine respiratory chain NADH RT dehydrogenase: high sequence conservation in mammals and tissue-specific RT and growth-dependent expression."; RL Curr. Genet. 16:117-125(1989). RN [4] RP PROTEIN SEQUENCE OF 33-249. RC TISSUE=Heart; RX PubMed=6861757; DOI=10.1111/j.1432-1033.1983.tb07543.x; RA von Bahr-Lindstroem H., Galante Y.M., Persson M., Joernvall H.; RT "The primary structure of subunit II of NADH dehydrogenase from bovine- RT heart mitochondria."; RL Eur. J. Biochem. 134:145-150(1983). RN [5] RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION, RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=10852722; DOI=10.1021/bi000335t; RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.; RT "Resolution of the membrane domain of bovine complex I into subcomplexes: RT implications for the structural organization of the enzyme."; RL Biochemistry 39:7229-7235(2000). RN [6] RP SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029; RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A., RA Robinson N.C.; RT "Subunit analysis of bovine heart complex I by reversed-phase high- RT performance liquid chromatography, electrospray ionization-tandem mass RT spectrometry, and matrix-assisted laser desorption/ionization-time-of- RT flight mass spectrometry."; RL Anal. Biochem. 382:116-121(2008). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=25209663; DOI=10.1038/nature13686; RA Vinothkumar K.R., Zhu J., Hirst J.; RT "Architecture of mammalian respiratory complex I."; RL Nature 515:80-84(2014). RN [8] {ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, ECO:0007744|PDB:5LDX} RP STRUCTURE BY ELECTRON MICROSCOPY (4.27 ANGSTROMS) OF 33-249, FUNCTION, RP CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=27509854; DOI=10.1038/nature19095; RA Zhu J., Vinothkumar K.R., Hirst J.; RT "Structure of mammalian respiratory complex I."; RL Nature 536:354-358(2016). 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:10852722, PubMed:18721790, PubMed:25209663, CC PubMed:27509854). Parts of the peripheral arm of the enzyme, where the CC electrons from NADH are accepted by flavin mononucleotide (FMN) and CC then passed along a chain of iron-sulfur clusters by electron CC tunnelling to the final acceptor ubiquinone (PubMed:10852722, CC PubMed:25209663, PubMed:27509854). Contains one iron-sulfur cluster CC (PubMed:25209663, PubMed:27509854). {ECO:0000269|PubMed:10852722, CC ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663, CC ECO:0000269|PubMed:27509854}. 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:10852722, ECO:0000305|PubMed:18721790, CC ECO:0000305|PubMed:25209663, ECO:0000305|PubMed:27509854}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; CC Evidence={ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790, CC ECO:0000305|PubMed:25209663, ECO:0000305|PubMed:27509854}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000269|PubMed:27509854}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:27509854}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits (PubMed:10852722, CC PubMed:18721790, PubMed:27509854). This is a component of the CC flavoprotein-sulfur (FP) fragment of the enzyme. CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, CC ECO:0000269|PubMed:27509854}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein CC {ECO:0000305|PubMed:25209663}; Matrix side CC {ECO:0000305|PubMed:25209663}. CC -!- SIMILARITY: Belongs to the complex I 24 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; X14724; CAA32848.1; -; mRNA. DR EMBL; BC102401; AAI02402.1; -; mRNA. DR EMBL; M22539; AAA87358.1; -; mRNA. DR PIR; B30113; B30113. DR RefSeq; NP_776990.1; NM_174565.3. DR PDB; 5LC5; EM; 4.35 A; E=1-249. DR PDB; 5LDW; EM; 4.27 A; E=33-249. DR PDB; 5LDX; EM; 5.60 A; E=33-249. DR PDB; 5O31; EM; 4.13 A; E=33-249. DR PDB; 7DGQ; EM; 5.00 A; 9=33-249. DR PDB; 7DGR; EM; 4.60 A; 9=33-249. DR PDB; 7DGS; EM; 7.80 A; 9=33-249. DR PDB; 7DGZ; EM; 3.80 A; 9=33-249. DR PDB; 7DH0; EM; 4.20 A; 9=33-249. DR PDB; 7DKF; EM; 8.30 A; 92=33-249. DR PDB; 7QSD; EM; 3.10 A; E=1-249. DR PDB; 7QSK; EM; 2.84 A; E=1-249. DR PDB; 7QSL; EM; 2.76 A; E=1-249. DR PDB; 7QSM; EM; 2.30 A; E=1-249. DR PDB; 7QSN; EM; 2.81 A; E=1-249. DR PDB; 7QSO; EM; 3.02 A; E=1-249. DR PDB; 7R41; EM; 2.30 A; E=1-249. DR PDB; 7R42; EM; 2.30 A; E=1-249. DR PDB; 7R43; EM; 2.40 A; E=1-249. DR PDB; 7R44; EM; 2.40 A; E=1-249. DR PDB; 7R45; EM; 2.40 A; E=1-249. DR PDB; 7R46; EM; 2.40 A; E=1-249. DR PDB; 7R47; EM; 2.30 A; E=1-249. DR PDB; 7R48; EM; 2.30 A; E=1-249. DR PDB; 7R4C; EM; 2.30 A; E=1-249. DR PDB; 7R4D; EM; 2.30 A; E=1-249. DR PDB; 7R4F; EM; 2.40 A; E=1-249. DR PDB; 7R4G; EM; 2.50 A; E=1-249. DR PDBsum; 5LC5; -. DR PDBsum; 5LDW; -. DR PDBsum; 5LDX; -. DR PDBsum; 5O31; -. DR PDBsum; 7DGQ; -. DR PDBsum; 7DGR; -. DR PDBsum; 7DGS; -. DR PDBsum; 7DGZ; -. DR PDBsum; 7DH0; -. DR PDBsum; 7DKF; -. DR PDBsum; 7QSD; -. DR PDBsum; 7QSK; -. DR PDBsum; 7QSL; -. DR PDBsum; 7QSM; -. DR PDBsum; 7QSN; -. DR PDBsum; 7QSO; -. DR PDBsum; 7R41; -. DR PDBsum; 7R42; -. DR PDBsum; 7R43; -. DR PDBsum; 7R44; -. DR PDBsum; 7R45; -. DR PDBsum; 7R46; -. DR PDBsum; 7R47; -. DR PDBsum; 7R48; -. DR PDBsum; 7R4C; -. DR PDBsum; 7R4D; -. DR PDBsum; 7R4F; -. DR PDBsum; 7R4G; -. DR AlphaFoldDB; P04394; -. DR EMDB; EMD-14127; -. DR EMDB; EMD-14132; -. DR EMDB; EMD-14133; -. DR EMDB; EMD-14134; -. DR EMDB; EMD-14139; -. DR EMDB; EMD-14140; -. DR EMDB; EMD-14251; -. DR EMDB; EMD-14256; -. DR EMDB; EMD-14261; -. DR EMDB; EMD-14266; -. DR EMDB; EMD-14272; -. DR EMDB; EMD-14277; -. DR EMDB; EMD-14282; -. DR EMDB; EMD-14287; -. DR EMDB; EMD-14292; -. DR EMDB; EMD-14297; -. DR EMDB; EMD-14302; -. DR EMDB; EMD-14307; -. DR EMDB; EMD-30673; -. DR EMDB; EMD-30674; -. DR EMDB; EMD-30675; -. DR EMDB; EMD-30676; -. DR EMDB; EMD-30677; -. DR EMDB; EMD-30706; -. DR EMDB; EMD-3731; -. DR EMDB; EMD-4032; -. DR EMDB; EMD-4040; -. DR EMDB; EMD-4041; -. DR SMR; P04394; -. DR CORUM; P04394; -. DR DIP; DIP-38821N; -. DR IntAct; P04394; 3. DR STRING; 9913.ENSBTAP00000052906; -. DR TCDB; 3.D.1.6.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR PaxDb; 9913-ENSBTAP00000052906; -. DR PeptideAtlas; P04394; -. DR Ensembl; ENSBTAT00000006405.5; ENSBTAP00000052906.2; ENSBTAG00000004871.5. DR GeneID; 282290; -. DR KEGG; bta:282290; -. DR CTD; 4729; -. DR VEuPathDB; HostDB:ENSBTAG00000004871; -. DR VGNC; VGNC:31975; NDUFV2. DR eggNOG; KOG3196; Eukaryota. DR GeneTree; ENSGT00390000017580; -. DR HOGENOM; CLU_054362_1_0_1; -. DR InParanoid; P04394; -. DR OMA; IMSIYPE; -. DR OrthoDB; 177389at2759; -. DR TreeFam; TF300004; -. DR Reactome; R-BTA-611105; Respiratory electron transport. DR Reactome; R-BTA-6799198; Complex I biogenesis. DR Proteomes; UP000009136; Chromosome 24. DR Bgee; ENSBTAG00000004871; Expressed in spermatocyte and 105 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:AgBase. DR GO; GO:0051537; F:2 iron, 2 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; IDA:UniProtKB. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:UniProtKB. DR CDD; cd03064; TRX_Fd_NuoE; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR042128; NuoE_dom. DR InterPro; IPR041921; NuoE_N. DR InterPro; IPR036249; Thioredoxin-like_sf. DR NCBIfam; TIGR01958; nuoE_fam; 1. DR PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1. DR Pfam; PF01257; 2Fe-2S_thioredx; 1. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Acetylation; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide; KW Translocase; Transport; Ubiquinone. FT TRANSIT 1..32 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:6861757" FT CHAIN 33..249 FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 2, FT mitochondrial" FT /id="PRO_0000020002" FT REGION 213..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 135 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 140 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 176 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 180 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT MOD_RES 61 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D6J6" FT MOD_RES 193 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P19404" FT CONFLICT 89..97 FT /note="QNGWLPISA -> SSGTSYPDVLKBZZZPPGGAAIILW (in Ref. 4; FT AA sequence)" FT /evidence="ECO:0000305" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:7QSK" FT HELIX 57..67 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 79..90 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 95..105 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 145..156 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 167..175 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 191..195 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:7QSN" FT TURN 241..244 FT /evidence="ECO:0007829|PDB:7QSM" SQ SEQUENCE 249 AA; 27308 MW; 8F7E8259F08EBF65 CRC64; MFLSAALRAR AAGLAAHWGK HIRNLHKTAV QNGAGGALFV HRDTPENNPE TPFDFTPENY KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEILQVPPM RVYEVATFYT MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC VNAPMVQIND NYYEDLTPKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG PGFGVQAGL //