ID M9ZZJ1_ZIPCA Unreviewed; 459 AA. AC M9ZZJ1; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-OCT-2020, entry version 32. 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:AGK37996.1}; OS Ziphius cavirostris (Cuvier's beaked whale) (Goose-beaked whale). OG Mitochondrion {ECO:0000313|EMBL:AGK37996.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; OC Ziphiidae; Ziphius. OX NCBI_TaxID=9760 {ECO:0000313|EMBL:AGK37996.1}; RN [1] {ECO:0000313|EMBL:AGK37996.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SWFSC ID z0079887 {ECO:0000313|EMBL:AGK37996.1}; RA Morin P.A., Duchene S., Lee N., Durban J., Claridge D.; RT "Preliminary analysis of mitochondrial genome phylogeography of RT Blainville's, Cuvier's and Gervais' beaked whales."; RL Submitted (MAR-2013) 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; KC776699; AGK37996.1; -; Genomic_DNA. 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:AGK37996.1}; 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..42 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 54..73 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 94..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 194..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..329 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 350..369 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 389..414 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT DOMAIN 77..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; 51517 MW; 5F6D49C3BAF24AD8 CRC64; MLKFIIPXXX XXXXXXXXXX XXIXXXXXAH SLLISFTSLL LLNQFXDNSL NYSLTXXXXX XXXXXXXXXX XXXXXXLXAS QSHLLKEPLT RKKLYITMLI TLQALLIMTF TAMELILXYI MFEATXVPTL IIITRWGNQT ERLNAGLYFL FYTLVGSLPL LVALTYLQNT MGTLNFLLLQ HWAQPLSPSW SNTLMWLACM MAFLVKMPLY GLHLWLPKAH VEAPIAGSMV LAAVLLKLGG YGMLRITPLL NPLTEHMAYP FLMLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIAA ILIQTPWSFM GATALMIAHG LTSSMLFCLA NSNYERIHSR TMILARGLQI FLPLMAAWWL LASMTNLALP PTINLIGELL VVMSAFSWSN LTIILMGTNI VITALYSLYM LIMTQRGKHT HHINNLTPSF TREHALMALH IMPLLLLSLN PKIILGPLY //