ID D8FRZ0_ONCKE Unreviewed; 460 AA. AC D8FRZ0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 05-DEC-2018, entry version 36. 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; OC Salmoniformes; 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 RT 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 CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone. {ECO:0000256|RuleBase:RU003297}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566; CC EC=7.1.1.2; Evidence={ECO:0000256|RuleBase:RU003297}; CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {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|RuleBase:RU003297, ECO:0000256|SAAS:SAAS00707377}. 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:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; 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 ECO:0000256|SAAS:SAAS00707373}; KW Mitochondrion {ECO:0000256|RuleBase:RU003297, KW ECO:0000313|EMBL:BAJ09720.1}; KW NAD {ECO:0000256|RuleBase:RU003297, ECO:0000256|SAAS:SAAS00707374}; KW Respiratory chain {ECO:0000256|RuleBase:RU003297}; KW Transmembrane {ECO:0000256|RuleBase:RU003297, KW ECO:0000256|SAAS:SAAS00707385}; KW Transmembrane helix {ECO:0000256|RuleBase:RU003297, KW ECO:0000256|SAAS:SAAS00707361}; KW Transport {ECO:0000256|RuleBase:RU003297}; KW Ubiquinone {ECO:0000256|RuleBase:RU003297, KW ECO:0000256|SAAS:SAAS00699082}. FT TRANSMEM 21 42 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 62 81 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 93 111 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 117 137 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 149 168 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 195 217 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 224 243 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 258 279 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 286 304 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 310 331 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 352 370 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 390 413 Helical. {ECO:0000256|RuleBase:RU003297}. FT TRANSMEM 434 450 Helical. {ECO:0000256|RuleBase:RU003297}. FT DOMAIN 1 110 Oxidored_q5_N. {ECO:0000259|Pfam: FT PF01059}. FT DOMAIN 113 404 Proton_antipo_M. {ECO:0000259|Pfam: FT 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 //