ID E9LAN3_HUMAN Unreviewed; 603 AA. AC E9LAN3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 29-MAY-2024, entry version 67. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|ARBA:ARBA00021096, ECO:0000256|RuleBase:RU003404}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003404}; GN Name=ND5 {ECO:0000313|EMBL:ADL15592.1}; OS Homo sapiens (Human). OG Mitochondrion {ECO:0000313|EMBL:ADL15592.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ADL15592.1}; RN [1] {ECO:0000313|EMBL:ADL15592.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21041797; DOI=10.1093/molbev/msq294; RA Batini C., Lopes J., Behar D.M., Calafell F., Jorde L.B., van der Veen L., RA Quintana-Murci L., Spedini G., Destro-Bisol G., Comas D.; RT "Insights into the demographic history of African Pygmies from complete RT mitochondrial genomes."; RL Mol. Biol. Evol. 28:1099-1110(2011). 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|RuleBase:RU003404}. 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:RU003404}; 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}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|RuleBase:RU003404}. 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; HM771171; ADL15592.1; -; Genomic_DNA. DR AlphaFoldDB; E9LAN3; -. DR PeptideAtlas; E9LAN3; -. DR ChiTaRS; MT-ND5; human. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:TreeGrafter. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR InterPro; IPR010934; NADH_DH_su5_C. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003404}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003404}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Signal {ECO:0000256|SAM:SignalP}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003404}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003404}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003404}; KW Ubiquinone {ECO:0000256|RuleBase:RU003404}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..603 FT /note="NADH-ubiquinone oxidoreductase chain 5" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003243214" FT TRANSMEM 84..105 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 117..134 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 172..191 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 211..233 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 245..266 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 272..294 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 301..319 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 325..347 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 368..386 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 406..433 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 454..472 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 484..507 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 584..602 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT DOMAIN 68..118 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 134..419 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 422..602 FT /note="NADH dehydrogenase subunit 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06455" SQ SEQUENCE 603 AA; 67045 MW; 76D91B5DCF1E5943 CRC64; MTMHTTMTTL TLTSLIPPIL TTLVNPNKKN SYPHYVKSIV ASTFIISLFP TTMFMCLDQE VIISNWHWAT TQTTQLSLSF KLDYFSMMFI PVALFVTWSI MEFSLWYMNS DPNINQFFKY LLIFLITMLI LVTANNLFQL FIGWEGVGIM SFLLISWWYA RADANTAAIQ AILYNRIGDM GFILALAWFI LHSNSWDPQQ MALLNANPSL TPLLGLLLAA AGKSAQLGLH PWLPSAMEGP TPVSALLHSS TMVVAGIFLL IRFHPLAENS PLIQTLTLCL GAITTLFAAV CALTQNDIKK IVAFSTSSQL GLMMVTIGIN QPHLAFLHIC THAFFKAMLF MCSGSIIHNL NNEQDIRKMG GLLKTMPLTS TSLTIGSLAL AGMPFLTGFY SKDHIIETAN MSYTNAWALS ITLIATSLTS AYSTRMILLT LTGQPRFPTL TNINENNPTL LNPIKRLAAG SLFAGFLITN NISPASPFQT TIPLYLKLTA LAVTFLGLLT ALDLNYLTNK LKMKSPLCTF YFSNMLGFYP SITHRTIPYL GLLTSQNLPL LLLDLTWLEK LLPKTISQHQ ISTSIITSTQ KGMIKLYFLS FFFPLILTLL LIT //