ID A0A0U1XGS9_9PETR Unreviewed; 457 AA. AC A0A0U1XGS9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 27-MAR-2024, entry version 26. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4 {ECO:0000256|ARBA:ARBA00021006, ECO:0000256|RuleBase:RU003297}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003297}; GN Name=ND4 {ECO:0000313|EMBL:AIT96671.1}; OS Ichthyomyzon fossor. OG Mitochondrion {ECO:0000313|EMBL:AIT96671.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Ichthyomyzon. OX NCBI_TaxID=245073 {ECO:0000313|EMBL:AIT96671.1}; RN [1] {ECO:0000313|EMBL:AIT96671.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Muscle {ECO:0000313|EMBL:AIT96671.1}; RX PubMed=25319286; RA Ren J., Buchinger T., Pu J., Jia L., Li W.; RT "Complete mitochondrial genomes of paired species northern brook lamprey RT (Ichthyomyzon fossor) and silver lamprey (I. unicuspis)."; RL Mitochondrial DNA 1-2:0-0(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. Essential for the catalytic activity and assembly of complex CC I. {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|RuleBase:RU003297}; Multi-pass membrane protein CC {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; KM267716; AIT96671.1; -; Genomic_DNA. DR RefSeq; YP_009106936.1; NC_025552.1. DR AlphaFoldDB; A0A0U1XGS9; -. DR GeneID; 22161474; -. DR CTD; 4538; -. 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 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 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:AIT96671.1}; 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 94..112 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 118..137 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 149..167 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 196..218 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 230..253 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 259..279 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 286..304 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 310..332 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 353..371 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 391..415 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 436..455 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT DOMAIN 1..109 FT /note="NADH:ubiquinone oxidoreductase chain 4 N-terminal" FT /evidence="ECO:0000259|Pfam:PF01059" FT DOMAIN 112..403 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 457 AA; 51741 MW; DF6B2080A0F2D290 CRC64; MLKLIIPSMM MIPMTFLMKK NLLWTATTSF SFLIATLSTL MLNTNMTEHN LANPILSTDQ FSCPLIMLSC WLLPLTIMAS QMHMKTEPIT RQKTMISLLI LLQILLCITF GASNLLTFYI AFEATLIPTL LIITRWGNQK ERLTAGLYFL FYTLSASLPL LIALIVIQTR FNSLSTYIIP LSNLTLLSNT SWSETMWWVA CFLAFLIKMP LYIFHLWLPK AHVEAPIAGS MVLAAILLKL GGYGMIRMSS LFIPLTKDLA IPFMIIAMWG MIVSSSICLR QTDLKSMIAY SSINHMNLVV AGIFSMTPWA WSGALAMMIA HGLVSSGLFC LANITYERTH TRSIFMNRGL KTLFPLMSFW WLMMTFANMA LPPFPNFTAE ILIITSMFNW SNWTILLLGL SMTLTTLFSL NMLIMTQHEH PNKHAPINPS TTREHLLMLM HMAPIILLII NPSPIMI //