ID NU4M_MOUSE Reviewed; 459 AA. AC P03911; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 163. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4; DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03905}; DE AltName: Full=NADH dehydrogenase subunit 4; GN Name=Mtnd4; Synonyms=mt-Nd4, Nd4; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=12954771; DOI=10.1093/nar/gkg739; RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S., RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y., RA Enriquez J.A.; RT "Revisiting the mouse mitochondrial DNA sequence."; RL Nucleic Acids Res. 31:5349-5355(2003). RN [3] RP PROTEIN SEQUENCE OF 246-255 AND 419-432, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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. Essential for the catalytic activity and assembly of complex CC I. {ECO:0000250|UniProtKB:P03905}. 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:P03905}; CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits. CC {ECO:0000250|UniProtKB:P03910}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {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; J01420; AAB48653.1; -; Genomic_DNA. DR EMBL; V00711; CAA24091.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY172335; AAN85131.1; -; Genomic_DNA. DR PIR; A00440; QXMS4M. DR RefSeq; NP_904337.1; NC_005089.1. DR PDB; 6G2J; EM; 3.30 A; M=1-459. DR PDB; 6G72; EM; 3.90 A; M=1-459. DR PDB; 6ZR2; EM; 3.10 A; M=1-459. DR PDB; 6ZTQ; EM; 3.00 A; M=1-459. DR PDB; 7AK5; EM; 3.17 A; M=1-459. DR PDB; 7AK6; EM; 3.82 A; M=1-459. DR PDB; 7B93; EM; 3.04 A; M=1-459. DR PDB; 7PSA; EM; 3.40 A; M=1-459. DR PDB; 8OLT; EM; 2.84 A; M=1-459. DR PDB; 8OM1; EM; 2.39 A; M=1-459. DR PDBsum; 6G2J; -. DR PDBsum; 6G72; -. DR PDBsum; 6ZR2; -. DR PDBsum; 6ZTQ; -. DR PDBsum; 7AK5; -. DR PDBsum; 7AK6; -. DR PDBsum; 7B93; -. DR PDBsum; 7PSA; -. DR PDBsum; 8OLT; -. DR PDBsum; 8OM1; -. DR AlphaFoldDB; P03911; -. DR EMDB; EMD-11377; -. DR EMDB; EMD-11424; -. DR EMDB; EMD-11810; -. DR EMDB; EMD-11811; -. DR EMDB; EMD-12095; -. DR EMDB; EMD-13611; -. DR EMDB; EMD-16962; -. DR EMDB; EMD-16965; -. DR EMDB; EMD-4345; -. DR EMDB; EMD-4356; -. DR SMR; P03911; -. DR BioGRID; 201550; 5. DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I. DR CORUM; P03911; -. DR IntAct; P03911; 5. DR MINT; P03911; -. DR STRING; 10090.ENSMUSP00000081000; -. DR GlyGen; P03911; 1 site, 1 O-linked glycan (1 site). DR PhosphoSitePlus; P03911; -. DR SwissPalm; P03911; -. DR jPOST; P03911; -. DR PaxDb; 10090-ENSMUSP00000081000; -. DR PeptideAtlas; P03911; -. DR ProteomicsDB; 293774; -. DR Pumba; P03911; -. DR Antibodypedia; 35362; 36 antibodies from 12 providers. DR Ensembl; ENSMUST00000082414.1; ENSMUSP00000081000.1; ENSMUSG00000064363.1. DR GeneID; 17719; -. DR KEGG; mmu:17719; -. DR AGR; MGI:102498; -. DR CTD; 4538; -. DR MGI; MGI:102498; mt-Nd4. DR VEuPathDB; HostDB:ENSMUSG00000064363; -. DR eggNOG; KOG4845; Eukaryota. DR GeneTree; ENSGT00730000111316; -. DR HOGENOM; CLU_007100_4_0_1; -. DR InParanoid; P03911; -. DR OMA; ITRWGNQ; -. DR OrthoDB; 1946151at2759; -. DR PhylomeDB; P03911; -. DR TreeFam; TF343520; -. DR Reactome; R-MMU-611105; Respiratory electron transport. DR Reactome; R-MMU-6799198; Complex I biogenesis. DR ChiTaRS; mt-Nd4; mouse. DR PRO; PR:P03911; -. DR Proteomes; UP000000589; Mitochondrion. DR RNAct; P03911; Protein. DR Bgee; ENSMUSG00000064363; Expressed in hypothalamus and 63 other cell types or tissues. DR ExpressionAtlas; P03911; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB. DR GO; GO:0048039; F:ubiquinone binding; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. 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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR InterPro; IPR000260; NADH4_N. DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4. DR InterPro; IPR003918; NADH_UbQ_OxRdtase. DR InterPro; IPR001750; ND/Mrp_mem. DR NCBIfam; TIGR01972; NDH_I_M; 1. DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1. DR PANTHER; PTHR43507:SF20; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1. DR Pfam; PF01059; Oxidored_q5_N; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01437; NUOXDRDTASE4. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Electron transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; NAD; Reference proteome; KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport; Ubiquinone. FT CHAIN 1..459 FT /note="NADH-ubiquinone oxidoreductase chain 4" FT /id="PRO_0000117957" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 90..110 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 194..214 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 257..277 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 284..303 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 308..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 350..370 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 392..412 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 434..454 FT /note="Helical" FT /evidence="ECO:0000255" FT HELIX 2..17 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 23..38 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 62..84 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 89..111 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 115..124 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 126..136 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 142..171 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 190..206 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 215..222 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 235..246 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:8OM1" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 259..275 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 282..303 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 306..337 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 353..366 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:6ZTQ" FT HELIX 373..388 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 392..415 FT /evidence="ECO:0007829|PDB:8OM1" FT STRAND 416..418 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 431..449 FT /evidence="ECO:0007829|PDB:8OM1" FT HELIX 451..454 FT /evidence="ECO:0007829|PDB:8OM1" SQ SEQUENCE 459 AA; 51882 MW; 62727CC11CCD137D CRC64; MLKIILPSLM LLPLTWLSSP KKTWTNVTSY SFLISLTSLT LLWQTDENYK NFSNMFSSDP LSTPLIILTA WLLPLMLMAS QNHLKKDNNV LQKLYISMLI SLQILLIMTF SATELIMFYI LFEATLIPTL IIITRWGNQT ERLNAGIYFL FYTLIGSIPL LIALILIQNH VGTLNLMILS FTTHTLDASW SNNLLWLACM MAFLIKMPLY GVHLWLPKAH VEAPIAGSMI LAAILLKLGS YGMIRISIIL DPLTKYMAYP FILLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIAS IMIQTPWSFM GATMLMIAHG LTSSLLFCLA NSNYERIHSR TMIMARGLQM VFPLMATWWL MASLANLALP PSINLMGELF ITMSLFSWSN FTIILMGINI IITGMYSMYM IITTQRGKLT NHMINLQPSH TRELTLMALH MIPLILLTTS PKLITGLTM //