ID A0A1P8CXM8_9CETA Unreviewed; 98 AA. AC A0A1P8CXM8; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-APR-2021, entry version 12. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L {ECO:0000256|RuleBase:RU004419}; DE EC=7.1.1.2 {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; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC 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., Elalouf J.M.; RT "Genome data on the extinct Bison schoetensacki establish it as a sister RT 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 chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|RuleBase:RU004419}. 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:RU004419}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC membrane {ECO:0000256|ARBA:ARBA00004225, CC ECO:0000256|RuleBase:RU004419}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004225, ECO:0000256|RuleBase:RU004419}. CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. CC {ECO:0000256|ARBA:ARBA00010519, 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 SMR; A0A1P8CXM8; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; 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:UniProtKB-UniRule. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR InterPro; IPR039428; NUOK/Mnh_C1-like. DR PANTHER; PTHR11434; PTHR11434; 1. DR Pfam; PF00420; Oxidored_q2; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU004419}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004419}; KW Mitochondrion {ECO:0000256|RuleBase:RU004419, ECO:0000313|EMBL:APD27955.1}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004419}; KW Respiratory chain {ECO:0000256|RuleBase:RU004419}; KW Translocase {ECO:0000256|RuleBase:RU004419}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU004419}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU004419}; Transport {ECO:0000256|RuleBase:RU004419}; KW Ubiquinone {ECO:0000256|RuleBase:RU004419}. FT TRANSMEM 6..22 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004419" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004419" FT TRANSMEM 61..81 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004419" SQ SEQUENCE 98 AA; 10797 MW; 4DB48B7DA59C1881 CRC64; MSMVYMNIMM AFTVSLVGLL MYRSHLMSSL LCLEGMMLSL FVMAALTILN SHFTLASMMP IILLVFAACE AALGLSLLVM VSNTYGTDYV QNLNLLQC //