ID D8FRZ0_ONCKE Unreviewed; 460 AA. AC D8FRZ0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 02-JUN-2021, entry version 44. 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:BAJ09720.1}; OS Oncorhynchus keta (Chum salmon) (Salmo keta). OG Mitochondrion {ECO:0000313|EMBL:BAJ09720.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8018 {ECO:0000313|EMBL:BAJ09720.1}; RN [1] {ECO:0000313|EMBL:BAJ09720.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Dorsal muscle {ECO:0000313|EMBL:BAJ09720.1}; RX PubMed=16284423; DOI=10.1266/ggs.80.297; RA Shigenobu Y., Saitoh K., Hayashizaki K., Ida H.; RT "Nonsynonymous site heteroplasmy in fish mitochondrial DNA."; RL Genes Genet. Syst. 80:297-301(2005). RN [2] {ECO:0000313|EMBL:BAJ09720.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Dorsal muscle {ECO:0000313|EMBL:BAJ09720.1}; RA Shigenobu Y., Saitoh K.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAJ09720.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Dorsal muscle {ECO:0000313|EMBL:BAJ09720.1}; RX PubMed=20616872; DOI=10.1139/G10-026; RA Garvin M.R., Saitoh K., Churikov D.Y., Brykov V.A., Gharrett A.J.; RT "Single nucleotide polymorphisms in chum salmon (Oncorhynchus keta) RT mitochondrial DNA derived from restriction site haplotype information."; RL Genome 53:501-507(2010). RN [4] {ECO:0000313|EMBL:BAJ09720.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Dorsal muscle {ECO:0000313|EMBL:BAJ09720.1}; RA Ishiguro N.B., Saitoh K., Miya M., Nishida M.; RT "Salmoniform mitochondrial genome."; RL Submitted (JUN-2010) 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; AP010773; BAJ09720.1; -; Genomic_DNA. DR RefSeq; YP_006280903.1; NC_017838.1. DR GeneID; 12486869; -. 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|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003297}; NAD {ECO:0000256|RuleBase:RU003297}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU003297}; KW Transmembrane {ECO:0000256|RuleBase:RU003297}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003297}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003297}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 21..42 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 62..81 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 93..111 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 149..168 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 195..217 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 224..243 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 258..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..331 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 352..370 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 390..413 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 434..450 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT DOMAIN 1..110 FT /note="Oxidored_q5_N" FT /evidence="ECO:0000259|Pfam:PF01059" FT DOMAIN 113..404 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" SQ SEQUENCE 460 AA; 51610 MW; F00F1F6455FEDC33 CRC64; MLKILIPTLM LFPTIWLSPA KWLWTTSIAQ SLIIALASLT WLKWSSETGW SSSNLYLATD PLSTPLLVLT CWLLPLMILA SQNHLSPEPL NRQRTYISLL VSLQTFLILA FGATEIIMFY IMFEATLLPT LIIITRWGNQ TERLNAGTYF LFYTLAGSLP LLVALLLMQN DNGTLSMFTL QYTQPLHLLT WGDKLWWAAC LLAFLVKMPL YGVHLWLPKA HVEAPIAGSM ILAAVLLKLG GYGMMRMMVM LDPLTKELAY PFIVLALWGI IMTGSICLRQ TDLKSLIAYS SVGHMGLVAG GILIQTPWGF TGAIILMIAH GLASSALFCL ANTSYERTHS RTMLLARGMQ MILPLMTTWW FIASLANLAL PPLPNLMGEL MIITSMFNWS YWTLILTGLG TLITASYSLY LFLMTQRGPL PSHIIALEPT HTREHLLIIL HLIPIVLLIL KPELMWGWCF //