ID A0A343ULZ4_9GOBI Unreviewed; 460 AA. AC A0A343ULZ4; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 12-AUG-2020, entry version 6. 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:AVE15017.1}; OS Eucyclogobius newberryi (tidewater goby). OG Mitochondrion {ECO:0000313|EMBL:AVE15017.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Gobionellinae; Eucyclogobius. OX NCBI_TaxID=166745 {ECO:0000313|EMBL:AVE15017.1}; RN [1] {ECO:0000313|EMBL:AVE15017.1} RP NUCLEOTIDE SEQUENCE. RA Gong L., Lu Z.-M., Guo B.-Y., Ye Y.-Y., Liu L.-Q.; RT "Characterization of the complete mitochondrial genome of the tidewater RT goby, Eucyclogobius newberryi (gobiiformes; gobiidae; gobionellinae) and RT its phylogenetic implications."; RL Conserv Genet Resour 0:0-0(2018). 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; MF038886; AVE15017.1; -; 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|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU003297}; Membrane {ECO:0000256|RuleBase:RU003297}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003297, ECO:0000313|EMBL:AVE15017.1}; KW 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 23..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 226..245 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 260..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..415 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 436..458 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; 50909 MW; FA4C98A3790E422F CRC64; MLKILIPTMM LIPTTWLAPS KHIWPSALAH SLIIAIFSLL WLSSPGETGW WLLSNLMALD PLSTPLLVLT CWLLPLMILA SQNHTSAEPV NRQRMYLMLL TSLQIFLIIA FSATEVLLFY VMFEATLIPT LILITRWGSQ GERLNAGTYF LFYTLAASLP LLVALLILQK TTGSLSLLPL PYAAAFPLIS VADKLWWAGC LLAFLVKMPL YGMHLWLPKA HVEAPIAGSM ILAAVLLKLG GYGMMRMMVV LEPLTKELSY PFIILALWGV IMTGSVCLRQ TDLKSLIAYS SVGHMGLVAG GILIQTPWGF TGALILMIAH GLTSSALLCL ANTNYERTHT RTMMLARGMQ MLLPLMTSWW FIATLANLAL PPLPNLMGEL MIITSLFNWS WMTIVLTGGG TLITAGYSLY MFLMTQRGPV PQHILALNPS HTREHLLLAL HLLPLLLLIL NPTLVWGWTA //