ID A0A1P8CXM8_9CETA Unreviewed; 98 AA. AC A0A1P8CXM8; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 10-MAY-2017, entry version 2. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L {ECO:0000256|RuleBase:RU004419}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU004419}; GN Name=ND4L {ECO:0000313|EMBL:APD27955.1}; OS Bison schoetensacki. OG Mitochondrion {ECO:0000313|EMBL:APD27955.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bison. OX NCBI_TaxID=1920185 {ECO:0000313|EMBL:APD27955.1}; RN [1] {ECO:0000313|EMBL:APD27955.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28187706; RA Palacio P., Berthonaud V., Guerin C., Lambourdiere J., Maksud F., RA Philippe M., Plaire D., Stafford T., Marsolier-Kergoat M.C., RA Elalouf J.M.; RT "Genome data on the extinct Bison schoetensacki establish it as a RT sister species of the extant European bison (Bison bonasus)."; RL BMC Evol. Biol. 17:48-48(2017). 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|RuleBase:RU004419}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU004419}. CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. CC {ECO:0000256|RuleBase:RU004419}. 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; KU886087; APD27955.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR PANTHER; PTHR11434; PTHR11434; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU004419, KW ECO:0000313|EMBL:APD27955.1}; NAD {ECO:0000256|RuleBase:RU004419}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004419}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000256|RuleBase:RU004419}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 81 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 10797 MW; 4DB48B7DA59C1881 CRC64; MSMVYMNIMM AFTVSLVGLL MYRSHLMSSL LCLEGMMLSL FVMAALTILN SHFTLASMMP IILLVFAACE AALGLSLLVM VSNTYGTDYV QNLNLLQC //