ID Q00GN8_LEPAN Unreviewed; 459 AA. AC Q00GN8; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 28-JUN-2023, entry version 78. 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:ADP68072.1}; OS Lepilemur ankaranensis (Ankarana sportive lemur) (Lepilemur septentrionalis OS ankaranensis). OG Mitochondrion {ECO:0000313|EMBL:ABG74291.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes; OC Lepilemuridae; Lepilemur. OX NCBI_TaxID=342401 {ECO:0000313|EMBL:ABG74291.1}; RN [1] {ECO:0000313|EMBL:ABG74291.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FIA5.1 {ECO:0000313|EMBL:ABG74175.1}, FIA5.11 RC {ECO:0000313|EMBL:ABG74203.1}, FIA5.12 {ECO:0000313|EMBL:ABG74207.1}, RC FIA5.13 {ECO:0000313|EMBL:ABG74211.1}, FIA5.5 RC {ECO:0000313|EMBL:ABG74179.1}, FIA5.6 {ECO:0000313|EMBL:ABG74183.1}, RC FIA5.9 {ECO:0000313|EMBL:ABG74195.1}, LABE5.1 RC {ECO:0000313|EMBL:ABG74275.1}, LABE5.17 {ECO:0000313|EMBL:ABG74291.1}, RC LABE5.2 {ECO:0000313|EMBL:ABG74279.1}, LABE5.3 RC {ECO:0000313|EMBL:ABG74283.1}, LABE5.4 {ECO:0000313|EMBL:ABG74287.1}, RC LAME5.6 {ECO:0000313|EMBL:ABG74167.1}, and LAME5.8 RC {ECO:0000313|EMBL:ABG74171.1}; RA Louis E.E.Jr., Engberg S.E., Lei R., Geng H., Sommer J.A., RA Randriamampionona R., Randriamanana J.C., Zaonarivelo J.R., RA Andriantompohavana R., Randria G., Prosper, Ramaromilanto B., RA Rakotoarisoa G., Rooney A., Brenneman R.A.; RT "Molecular and morphological analyses of the sportive lemurs (Family RT Megaladapidae: Genus Lepilemur) reveals 11 previously unrecognized RT species."; RL Spec. Publ. Mus. Tex. Tech. Univ. 49:1-47(2006). RN [2] {ECO:0000313|EMBL:ADP68072.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANAL5 {ECO:0000313|EMBL:ADP68072.1}; RX PubMed=28173059; DOI=10.1093/jhered/esw072; RA Lei R., Frasier C.L., Hawkins M.T., Engberg S.E., Bailey C.A., RA Johnson S.E., McLain A.T., Groves C.P., Perry G.H., Nash S.D., RA Mittermeier R.A., Louis E.E.; RT "Phylogenomic Reconstruction of Sportive Lemurs (genus Lepilemur) Recovered RT from Mitogenomes with Inferences for Madagascar Biogeography."; RL J. Hered. 108:107-119(2017). 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 inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. 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|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; DQ529712; ABG74167.1; -; Genomic_DNA. DR EMBL; DQ529713; ABG74171.1; -; Genomic_DNA. DR EMBL; DQ529714; ABG74175.1; -; Genomic_DNA. DR EMBL; DQ529715; ABG74179.1; -; Genomic_DNA. DR EMBL; DQ529716; ABG74183.1; -; Genomic_DNA. DR EMBL; DQ529719; ABG74195.1; -; Genomic_DNA. DR EMBL; DQ529721; ABG74203.1; -; Genomic_DNA. DR EMBL; DQ529722; ABG74207.1; -; Genomic_DNA. DR EMBL; DQ529723; ABG74211.1; -; Genomic_DNA. DR EMBL; DQ529739; ABG74275.1; -; Genomic_DNA. DR EMBL; DQ529740; ABG74279.1; -; Genomic_DNA. DR EMBL; DQ529741; ABG74283.1; -; Genomic_DNA. DR EMBL; DQ529742; ABG74287.1; -; Genomic_DNA. DR EMBL; DQ529743; ABG74291.1; -; Genomic_DNA. DR EMBL; HQ171056; ADP68072.1; -; Genomic_DNA. DR AlphaFoldDB; Q00GN8; -. DR SMR; Q00GN8; -. DR GO; GO:0005743; C:mitochondrial inner 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; 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. 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:ABG74291.1}; 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|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003297}; KW Ubiquinone {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..330 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003297" FT TRANSMEM 351..373 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; 52177 MW; 3BEAEAD636206142 CRC64; MLKIIIPTIM LLPVTWFSAN SMVWINITLH SLTISLMSLS FLNQTDSNSN NFSSTFFSDP LSSPLLTLTM WLLPLTIMAS QHHLSKEPWE RKKYFLFTLI SLQLFLIMTF TATELIMFYI LFESTLIPTL IIITRWGNQT ERLNAGLYFL FYTLIGSLPL LVALSFIQKH MGTLNLFMMT YWSQELPNSW SSNLMWMACI MAFMIKMPLY GLHLWLPKAH VEAPIAGSMI LAAILLKLGG YGMMRITTIL NPLTKFMAYP FLMLCLWGMI MTSLICLRQT DLKSLIAYSS VSHMALVIVA ILIQTPWSFM GATALMIAHG LTSSMLFCLA NSNYERIHNR TMLLARGLQS LLPLMSTWWL LASLTNLALP PSINLIGELF ITMATFSWSN MTIILTGLNM LITATYSLHM LAMTQRGKSL YHMHNLNPSL TRENTLMSMH IFPLLLLTLN PNILMGPTY //