ID E3T1W4_PIG Unreviewed; 459 AA. AC E3T1W4; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-OCT-2020, entry version 38. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4 {ECO:0000256|RuleBase:RU003297}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003297}; GN Name=ND4 {ECO:0000313|EMBL:ACZ44406.1}; OS Sus scrofa taivanus. OG Mitochondrion {ECO:0000313|EMBL:ACZ44406.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=310261 {ECO:0000313|EMBL:ACZ44406.1}; RN [1] {ECO:0000313|EMBL:ACZ44406.1} RP NUCLEOTIDE SEQUENCE. RA Ju Y.T., Wu C.Y., Jiang Y.N.; RT "Intra-population genetic structure of Lan-Yu pig (Sus scrofa) by analysis RT of mitochondrial genomic sequences."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|RuleBase:RU003297}. 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:0000256|ARBA:ARBA00000766, CC ECO:0000256|RuleBase:RU003297}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC membrane {ECO:0000256|ARBA:ARBA00004225, CC ECO:0000256|RuleBase:RU003297}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004225, ECO:0000256|RuleBase:RU003297}. CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. CC {ECO:0000256|ARBA:ARBA00009025, ECO:0000256|RuleBase:RU003297}. 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; GU147934; ACZ44406.1; -; Genomic_DNA. DR RefSeq; YP_004021584.1; NC_014692.1. DR GeneID; 9978381; -. DR CTD; 4538; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. 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 PANTHER; PTHR43507; PTHR43507; 1. DR Pfam; PF01059; Oxidored_q5_N; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01437; NUOXDRDTASE4. DR TIGRFAMs; TIGR01972; NDH_I_M; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU003297}; KW Membrane {ECO:0000256|RuleBase:RU003297}; KW Mitochondrion {ECO:0000256|RuleBase:RU003297, ECO:0000313|EMBL:ACZ44406.1}; KW NAD {ECO:0000256|RuleBase:RU003297}; KW Respiratory chain {ECO:0000256|RuleBase:RU003297}; KW Transmembrane {ECO:0000256|RuleBase:RU003297}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003297}; KW Transport {ECO:0000256|RuleBase:RU003297}; KW Ubiquinone {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 61..80 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 92..110 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 116..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 145..167 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 193..216 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 223..244 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 256..277 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 284..303 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 309..330 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 351..369 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 389..414 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 435..455 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT DOMAIN 1..109 FT /note="Oxidored_q5_N" FT /evidence="ECO:0000259|Pfam:PF01059" FT DOMAIN 112..403 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 459 AA; 51863 MW; 57ED6F89388E8935 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 LIITQRGKYT HHINNIKPSF TRENALMALH ILPLLLLTLN PKMILGPLY //