ID NU4M_PIG Reviewed; 459 AA. AC O79881; Q9TDR2; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 130. 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=MT-ND4; Synonyms=MTND4, NADH4, ND4; OS Sus scrofa (Pig). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9732457; DOI=10.1007/pl00006388; RA Ursing B.M., Arnason U.; RT "The complete mitochondrial DNA sequence of the pig (Sus scrofa)."; RL J. Mol. Evol. 47:302-306(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Landrace; RX PubMed=10433971; DOI=10.1016/s0378-1119(99)00247-4; RA Lin C.S., Sun Y.L., Liu C.Y., Yang P.C., Chang L.C., Cheng I.C., RA Mao S.J.T., Huang M.C.; RT "Complete nucleotide sequence of pig (Sus scrofa) mitochondrial genome and RT dating evolutionary divergence within artiodactyla."; RL Gene 236:107-114(1999). 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; AJ002189; CAA05237.1; -; Genomic_DNA. DR EMBL; AF034253; AAD34194.1; -; Genomic_DNA. DR PIR; T10981; T10981. DR RefSeq; NP_008643.1; NC_000845.1. DR PDB; 5GPN; EM; 5.40 A; h=1-459. DR PDB; 5GUP; EM; 4.00 A; q=1-459. DR PDB; 7V2C; EM; 2.90 A; r=1-459. DR PDB; 7V2D; EM; 3.30 A; r=1-459. DR PDB; 7V2E; EM; 2.80 A; r=1-459. DR PDB; 7V2F; EM; 3.10 A; r=1-459. DR PDB; 7V2H; EM; 2.50 A; r=1-459. DR PDB; 7V2K; EM; 2.70 A; r=1-459. DR PDB; 7V2R; EM; 2.60 A; r=1-459. DR PDB; 7V30; EM; 2.70 A; r=1-459. DR PDB; 7V31; EM; 2.90 A; r=1-459. DR PDB; 7V32; EM; 3.20 A; r=1-459. DR PDB; 7V33; EM; 2.60 A; r=1-459. DR PDB; 7V3M; EM; 2.90 A; r=1-459. DR PDB; 7VBL; EM; 2.60 A; r=1-459. DR PDB; 7VBP; EM; 2.80 A; r=1-459. DR PDB; 7VC0; EM; 2.60 A; r=1-459. DR PDB; 7VWL; EM; 2.70 A; r=1-459. DR PDB; 7VXS; EM; 2.90 A; r=1-459. DR PDB; 7VY1; EM; 3.30 A; r=1-459. DR PDB; 7VY9; EM; 2.90 A; r=1-459. DR PDB; 7VYE; EM; 3.10 A; r=1-459. DR PDB; 7VYG; EM; 2.90 A; r=1-459. DR PDB; 7VYI; EM; 3.10 A; r=1-459. DR PDB; 7VYS; EM; 2.50 A; r=1-458. DR PDB; 7VZ8; EM; 2.70 A; r=1-459. DR PDB; 7VZV; EM; 3.20 A; r=1-459. DR PDB; 7VZW; EM; 3.20 A; r=1-459. DR PDB; 7W00; EM; 3.50 A; r=1-459. DR PDB; 7W0H; EM; 3.40 A; r=1-459. DR PDB; 7W0R; EM; 2.80 A; r=1-459. DR PDB; 7W1O; EM; 3.50 A; r=1-459. DR PDB; 7W1P; EM; 3.10 A; r=1-459. DR PDB; 7W1T; EM; 3.00 A; r=1-459. DR PDB; 7W1U; EM; 3.20 A; r=1-459. DR PDB; 7W1V; EM; 3.00 A; r=1-459. DR PDB; 7W1Z; EM; 2.60 A; r=1-459. DR PDB; 7W20; EM; 3.00 A; r=1-459. DR PDB; 7W2L; EM; 3.00 A; r=1-459. DR PDB; 7W2R; EM; 2.90 A; r=1-459. DR PDB; 7W2U; EM; 2.60 A; r=1-459. DR PDB; 7W2Y; EM; 2.70 A; r=1-459. DR PDB; 7W31; EM; 3.10 A; r=1-459. DR PDB; 7W32; EM; 2.90 A; r=1-459. DR PDB; 7W35; EM; 3.00 A; r=1-459. DR PDB; 7W4C; EM; 2.70 A; r=1-459. DR PDB; 7W4D; EM; 3.00 A; r=1-459. DR PDB; 7W4E; EM; 3.00 A; r=1-459. DR PDBsum; 5GPN; -. DR PDBsum; 5GUP; -. DR PDBsum; 7V2C; -. DR PDBsum; 7V2D; -. DR PDBsum; 7V2E; -. DR PDBsum; 7V2F; -. DR PDBsum; 7V2H; -. DR PDBsum; 7V2K; -. DR PDBsum; 7V2R; -. DR PDBsum; 7V30; -. DR PDBsum; 7V31; -. DR PDBsum; 7V32; -. DR PDBsum; 7V33; -. DR PDBsum; 7V3M; -. DR PDBsum; 7VBL; -. DR PDBsum; 7VBP; -. DR PDBsum; 7VC0; -. DR PDBsum; 7VWL; -. DR PDBsum; 7VXS; -. DR PDBsum; 7VY1; -. DR PDBsum; 7VY9; -. DR PDBsum; 7VYE; -. DR PDBsum; 7VYG; -. DR PDBsum; 7VYI; -. DR PDBsum; 7VYS; -. DR PDBsum; 7VZ8; -. DR PDBsum; 7VZV; -. DR PDBsum; 7VZW; -. DR PDBsum; 7W00; -. DR PDBsum; 7W0H; -. DR PDBsum; 7W0R; -. DR PDBsum; 7W1O; -. DR PDBsum; 7W1P; -. DR PDBsum; 7W1T; -. DR PDBsum; 7W1U; -. DR PDBsum; 7W1V; -. DR PDBsum; 7W1Z; -. DR PDBsum; 7W20; -. DR PDBsum; 7W2L; -. DR PDBsum; 7W2R; -. DR PDBsum; 7W2U; -. DR PDBsum; 7W2Y; -. DR PDBsum; 7W31; -. DR PDBsum; 7W32; -. DR PDBsum; 7W35; -. DR PDBsum; 7W4C; -. DR PDBsum; 7W4D; -. DR PDBsum; 7W4E; -. DR AlphaFoldDB; O79881; -. DR EMDB; EMD-32249; -. DR EMDB; EMD-32255; -. DR EMDB; EMD-32256; -. DR EMDB; EMD-32257; -. DR EMDB; EMD-32259; -. DR EMDB; EMD-32260; -. DR EMDB; EMD-32263; -. DR EMDB; EMD-32264; -. DR EMDB; EMD-32265; -. DR EMDB; EMD-32266; -. DR EMDB; EMD-32267; -. DR EMDB; EMD-32269; -. DR EMDB; EMD-32270; -. DR EMDB; EMD-32271; -. DR EMDB; EMD-32300; -. DR EMDB; EMD-32301; -. DR EMDB; EMD-32302; -. DR EMDB; EMD-32303; -. DR EMDB; EMD-32304; -. DR EMDB; EMD-32305; -. DR EMDB; EMD-32306; -. DR EMDB; EMD-32307; -. DR EMDB; EMD-32308; -. DR EMDB; EMD-32309; -. DR EMDB; EMD-32312; -. DR EMDB; EMD-9534; -. DR EMDB; EMD-9539; -. DR SMR; O79881; -. DR STRING; 9823.ENSSSCP00000019144; -. DR PaxDb; 9823-ENSSSCP00000019144; -. DR PeptideAtlas; O79881; -. DR Ensembl; ENSSSCT00000019682.3; ENSSSCP00000019144.3; ENSSSCG00000018087.3. DR Ensembl; ENSSSCT00070061684.1; ENSSSCP00070052587.1; ENSSSCG00070030647.1. DR GeneID; 808510; -. DR KEGG; ssc:808510; -. DR CTD; 4538; -. DR VGNC; VGNC:99795; MT-ND4. DR eggNOG; KOG4845; Eukaryota. DR GeneTree; ENSGT00730000111316; -. DR HOGENOM; CLU_007100_4_0_1; -. DR InParanoid; O79881; -. DR OMA; ITRWGNQ; -. DR OrthoDB; 1946151at2759; -. DR TreeFam; TF343520; -. DR Reactome; R-SSC-611105; Respiratory electron transport. DR Reactome; R-SSC-6799198; Complex I biogenesis. DR ChiTaRS; ND4; pig. DR Proteomes; UP000008227; Mitochondrion. DR Proteomes; UP000314985; Mitochondrion. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000018087; Expressed in prefrontal cortex and 44 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central. 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: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 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. DR Genevisible; O79881; SS. PE 1: Evidence at protein level; KW 3D-structure; Electron transport; Membrane; Mitochondrion; KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain; KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1..459 FT /note="NADH-ubiquinone oxidoreductase chain 4" FT /id="PRO_0000117970" FT TRANSMEM 22..42 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 193..213 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 351..371 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 391..413 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 435..455 FT /note="Helical" FT /evidence="ECO:0000255" FT CONFLICT 361 FT /note="M -> V (in Ref. 1; CAA05237)" FT /evidence="ECO:0000305" FT CONFLICT 428 FT /note="A -> P (in Ref. 1; CAA05237)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="Y -> YC (in Ref. 1; CAA05237)" FT /evidence="ECO:0000305" FT HELIX 2..16 FT /evidence="ECO:0007829|PDB:7V2H" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 23..38 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:7V2H" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:7V2H" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 62..80 FT /evidence="ECO:0007829|PDB:7V2H" FT TURN 81..86 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 89..109 FT /evidence="ECO:0007829|PDB:7V2H" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 115..124 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 126..136 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 142..171 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 190..206 FT /evidence="ECO:0007829|PDB:7V2H" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7V2E" FT HELIX 215..222 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:7V2H" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 237..246 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:7VC0" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 259..277 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 282..303 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 306..337 FT /evidence="ECO:0007829|PDB:7V2H" FT TURN 342..344 FT /evidence="ECO:0007829|PDB:7V2K" FT HELIX 348..351 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 353..366 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 373..388 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 392..415 FT /evidence="ECO:0007829|PDB:7V2H" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:7VXS" FT HELIX 431..449 FT /evidence="ECO:0007829|PDB:7V2H" FT HELIX 451..454 FT /evidence="ECO:0007829|PDB:7V2H" SQ SEQUENCE 459 AA; 51825 MW; 7625EF89388E92AF CRC64; MLKIIIPTTM LLPMTWMSKH NMIWINATVH SLLISLISLS LLNQLGENSL NFSLTFFSDS LSAPLLVLTT WLLPLMLMAS QSHLSKETTT RKKLYITMLI LLQLFLIMTF TATELILFYI LFEATLVPTL IIITRWGNQT ERLNAGLYFL FYTLAGSLPL LVALVYIQNT TGSLNFLIIH YWSHPLSNSW SNIFMWLACI MAFMVKMPLY GLHLWLPKAH VEAPIAGSMV LAAVLLKLGG YGMMRITTIL NPLTNYMAYP FLMLSMWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIVA IMIQTPWSFM GATALMIAHG LTSSMLFCLA NTNYERVHSR TMILARGLQT LLPLMATWWL MASLTNLALP PSINLIGELF IITASFSWSN ITIILMGMNM MITALYSLYM LITTQRGKYT HHINNIKASF TRENALMALH ILPLLLLTLN PKMILGPLY //