ID NDUS7_BOVIN Reviewed; 216 AA. AC P42026; Q2TBS6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial; DE EC=7.1.1.2 {ECO:0000250|UniProtKB:O75251}; DE AltName: Full=Complex I-20kD; DE Short=CI-20kD; DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit; DE AltName: Full=PSST subunit; DE Flags: Precursor; GN Name=NDUFS7; 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], PARTIAL PROTEIN SEQUENCE, AND PROTEIN SEQUENCE RP OF N-TERMINUS. RC TISSUE=Heart; RX PubMed=1577158; DOI=10.1016/0014-5793(92)80248-f; RA Arizmendi J.M., Runswick M.J., Skehel J.M., Walker J.E.; RT "NADH: ubiquinone oxidoreductase from bovine heart mitochondria. A fourth RT nuclear encoded subunit with a homologue encoded in chloroplast genomes."; RL FEBS Lett. 301:237-242(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 107-120, AND HYDROXYLATION AT ARG-114. RX PubMed=23836892; DOI=10.1074/jbc.m113.488106; RA Carroll J., Ding S., Fearnley I.M., Walker J.E.; RT "Post-translational modifications near the quinone binding site of RT mammalian complex I."; RL J. Biol. Chem. 288:24799-24808(2013). RN [4] RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR RP LOCATION, AND FUNCTION. 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 [5] RP SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR LOCATION, AND FUNCTION. 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 [6] RP 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). 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). Essential for the CC catalytic activity of complex I (By similarity). CC {ECO:0000250|UniProtKB:O75251, ECO:0000269|PubMed:10852722, CC ECO:0000269|PubMed:18721790}. 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:0000250|UniProtKB:O75251}; 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:10852722, CC PubMed:18721790, PubMed:25209663). This is a component of the iron- CC sulfur (IP) fragment of the enzyme (PubMed:25209663). CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, CC ECO:0000269|PubMed:25209663}. 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 -!- PTM: Hydroxylated ar Arg-114 by NDUFAF5 early in the pathway of CC assembly of complex I, before the formation of the juncture between CC peripheral and membrane arms. {ECO:0000250|UniProtKB:O75251}. CC -!- SIMILARITY: Belongs to the complex I 20 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; X65020; CAA46154.1; -; mRNA. DR EMBL; BC109716; AAI09717.1; -; mRNA. DR PIR; S22371; S22371. DR RefSeq; NP_001033111.1; NM_001038022.1. DR RefSeq; XP_005209312.1; XM_005209255.3. DR RefSeq; XP_005209313.1; XM_005209256.1. DR PDB; 5LC5; EM; 4.35 A; B=64-210. DR PDB; 5LDW; EM; 4.27 A; B=38-216. DR PDB; 5LDX; EM; 5.60 A; B=38-216. DR PDB; 5LNK; EM; 3.90 A; 6=38-216. DR PDB; 5O31; EM; 4.13 A; B=38-216. DR PDB; 7DGQ; EM; 5.00 A; D=38-216. DR PDB; 7DGR; EM; 4.60 A; D=38-216. DR PDB; 7DGS; EM; 7.80 A; D=38-216. DR PDB; 7DGZ; EM; 3.80 A; D=38-216. DR PDB; 7DH0; EM; 4.20 A; D=38-216. DR PDB; 7DKF; EM; 8.30 A; D2=38-216. DR PDB; 7QSD; EM; 3.10 A; B=1-216. DR PDB; 7QSK; EM; 2.84 A; B=1-216. DR PDB; 7QSL; EM; 2.76 A; B=1-216. DR PDB; 7QSM; EM; 2.30 A; B=1-216. DR PDB; 7QSN; EM; 2.81 A; B=1-216. DR PDB; 7QSO; EM; 3.02 A; B=1-216. DR PDB; 7R41; EM; 2.30 A; B=1-216. DR PDB; 7R42; EM; 2.30 A; B=1-216. DR PDB; 7R43; EM; 2.40 A; B=1-216. DR PDB; 7R44; EM; 2.40 A; B=1-216. DR PDB; 7R45; EM; 2.40 A; B=1-216. DR PDB; 7R46; EM; 2.40 A; B=1-216. DR PDB; 7R47; EM; 2.30 A; B=1-216. DR PDB; 7R48; EM; 2.30 A; B=1-216. DR PDB; 7R4C; EM; 2.30 A; B=1-216. DR PDB; 7R4D; EM; 2.30 A; B=1-216. DR PDB; 7R4F; EM; 2.40 A; B=1-216. DR PDB; 7R4G; EM; 2.50 A; B=1-216. DR PDBsum; 5LC5; -. DR PDBsum; 5LDW; -. DR PDBsum; 5LDX; -. DR PDBsum; 5LNK; -. 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; P42026; -. 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-4093; -. DR SMR; P42026; -. DR CORUM; P42026; -. DR DIP; DIP-38820N; -. DR IntAct; P42026; 2. DR STRING; 9913.ENSBTAP00000051744; -. DR TCDB; 3.D.1.6.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR PaxDb; 9913-ENSBTAP00000025870; -. DR PeptideAtlas; P42026; -. DR Ensembl; ENSBTAT00000025870.5; ENSBTAP00000025870.4; ENSBTAG00000019419.6. DR Ensembl; ENSBTAT00000053067.2; ENSBTAP00000051744.2; ENSBTAG00000019419.6. DR GeneID; 338079; -. DR KEGG; bta:338079; -. DR CTD; 374291; -. DR VEuPathDB; HostDB:ENSBTAG00000019419; -. DR VGNC; VGNC:31972; NDUFS7. DR eggNOG; KOG1687; Eukaryota. DR GeneTree; ENSGT00390000006565; -. DR HOGENOM; CLU_055737_1_2_1; -. DR InParanoid; P42026; -. DR OMA; GCGGIEM; -. DR OrthoDB; 33762at2759; -. DR TreeFam; TF312859; -. DR Reactome; R-BTA-611105; Respiratory electron transport. DR Reactome; R-BTA-6799198; Complex I biogenesis. DR Proteomes; UP000009136; Chromosome 7. DR Bgee; ENSBTAG00000019419; Expressed in laryngeal cartilage and 108 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: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; ISS:UniProtKB. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB. DR Gene3D; 3.40.50.12280; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR NCBIfam; TIGR01957; nuoB_fam; 1. DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR SUPFAM; SSF56770; HydA/Nqo6-like; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; KW Hydroxylation; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome; KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone. FT TRANSIT 1..37 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:1577158" FT CHAIN 38..216 FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein FT 7, mitochondrial" FT /id="PRO_0000020026" FT BINDING 91 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 92 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 156 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 186 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT MOD_RES 114 FT /note="Hydroxyarginine" FT /evidence="ECO:0000269|PubMed:23836892" FT HELIX 63..80 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 92..100 FT /evidence="ECO:0007829|PDB:7QSM" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:7QSD" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 121..127 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 134..143 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:7QSO" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 190..205 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 209..214 FT /evidence="ECO:0007829|PDB:7QSM" SQ SEQUENCE 216 AA; 23771 MW; 514B8A63C59BE641 CRC64; MAALAALRLL HPILAVRSGV GAALQVRGVH SSMAADSPSS TQPAVSQARA VVPKPAALPS SRGEYVVAKL DDLINWARRS SLWPMTFGLA CCAVEMMHMA APRYDMDRFG VVFRASPRQS DVMIVAGTLT NKMAPALRKV YDQMPEPRYV VSMGSCANGG GYYHYSYSVV RGCDRIVPVD IYVPGCPPTA EALLYGILQL QKKIKREKRL RIWYRR //