ID A0A898NYE5_MUNMU Unreviewed; 459 AA. AC A0A898NYE5; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 13-SEP-2023, entry version 9. 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:QSJ55892.1}; OS Muntiacus muntjak aureus (Himalayan red muntjac). OG Mitochondrion {ECO:0000313|EMBL:QSJ55892.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae; OC Muntiacinae; Muntiacus. OX NCBI_TaxID=2815728 {ECO:0000313|EMBL:QSJ55892.1}; RN [1] {ECO:0000313|EMBL:QSJ55892.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UK2 {ECO:0000313|EMBL:QSJ55892.1}; RA Singh B., Kumar A., Uniyal V.P., Gupta S.K. Sr.; RT "Phylogeography and population genetic structure of red muntjacs: Evidence RT of recent divergence of new lineage from India."; RL BMC Ecol Evol 0:0-0(2021). 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|ARBA:ARBA00024313, 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 -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex CC I) which is composed of 45 different subunits. CC {ECO:0000256|ARBA:ARBA00024376}. 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; MT671404; QSJ55892.1; -; Genomic_DNA. DR AlphaFoldDB; A0A898NYE5; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW. 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:SF1; 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:QSJ55892.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; 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|ARBA:ARBA00022448, 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 193..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..278 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 285..304 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 351..369 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 389..412 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 459 AA; 52051 MW; F39214AA91757615 CRC64; MLKYIIPTIM LMPLTWLSKG SMIWINSTTH SLLISLTGLL LMNQFSDNSL NFSLMFFSDS LSTPLLILTM WLLPLMLMAS QHHLSKESLT RKKLYITMLI LLQLFLIMTF TAMELILFYI LFEATLVPTL IIITRWGNQT ERLNAGLYFL FYTLVGSLPL LVALVYLQNI TGSLNFLVLQ YWMQPLSNSW SNVFMWLACM MAFMVKMPLY GLHLWLPKAH VEAPIAGSMV LAAILLKLGG YGMLRITTFL NPLTEFMAYP FIMLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIVA ILIQTPWSNM GATALMIAHG LTSSMLFCLA NSNYERIHSR TMILARGLQT FLPLMATWWL LASLTNLALP PTINLVGELF VVMSSFSWSN ITIILMGLNM VITALYSLYM LIMTQRGKYT HHINNISPSF TRENALMSLH ILPLLLLSFN PKIILGTLY //