ID E9LAN3_HUMAN Unreviewed; 603 AA. AC E9LAN3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 15-MAR-2017, entry version 36. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00061106}; DE EC=1.6.5.3 {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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA van der Veen L., Quintana-Murci L., Spedini G., Destro-Bisol G., RA Comas D.; RT "Insights into the demographic history of African Pygmies from RT complete mitochondrial genomes."; RL Mol. Biol. Evol. 28:1099-1110(2011). 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|SAAS:SAAS00061107}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00061104}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00061113}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00061113}. 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 STRING; 9606.ENSP00000354813; -. DR PaxDb; E9LAN3; -. DR eggNOG; KOG4668; Eukaryota. DR eggNOG; COG1009; LUCA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. 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 InterPro; IPR010934; NADH_DH_su5_C. DR InterPro; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|SAAS:SAAS00061110}; KW Membrane {ECO:0000256|SAAS:SAAS00093326, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00448066, ECO:0000313|EMBL:ADL15592.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00061114}; KW NAD {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00061109}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00093267}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00061105}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00093342, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00093282, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00061102}; KW Ubiquinone {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00061120}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 603 NADH-ubiquinone oxidoreductase chain 5. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003243214. FT TRANSMEM 84 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 172 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 266 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 272 294 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 319 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 368 386 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 406 433 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 454 472 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 484 507 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 584 602 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 65 121 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 134 418 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 422 602 NADH5_C. {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 //