ID A0A343RQL8_MAMPR Unreviewed; 318 AA. AC A0A343RQL8; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 16-JAN-2019, entry version 3. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU000473}; GN Name=ND1 {ECO:0000313|EMBL:AUF72756.1}; OS Mammuthus primigenius (Siberian woolly mammoth). OG Mitochondrion {ECO:0000313|EMBL:AUF72756.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Mammuthus. OX NCBI_TaxID=37349 {ECO:0000313|EMBL:AUF72756.1}; RN [1] {ECO:0000313|EMBL:AUF72756.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JK2769 {ECO:0000313|EMBL:AUF72756.1}; RA Fellows Yates J.A., Drucker D.G., Reiter E., Heumos S., Welker F., RA Munzel S.C., Wojtal P., Laznickova-Galetova M., Conard N.J., RA Herbig A., Bocherens H., Krause J.; RT "Central European Woolly Mammoth Population Dynamics: Insights from RT Late Pleistocene Mitochondrial Genomes."; RL Sci. Rep. 7:17715-17715(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=7.1.1.2; Evidence={ECO:0000256|RuleBase:RU000473}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000471}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000256|RuleBase:RU000471}. 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; MF579938; AUF72756.1; -; Genomic_DNA. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000473, KW ECO:0000313|EMBL:AUF72756.1}; NAD {ECO:0000256|RuleBase:RU000471}; KW Transmembrane {ECO:0000256|RuleBase:RU000471, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000256|RuleBase:RU000473}. FT TRANSMEM 69 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 101 120 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 220 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 254 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 293 314 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 318 AA; 35718 MW; 693816461EBAB823 CRC64; MFLINVLTVT LPILLAVAFL TLVERKALGY MQLRKGPNVV GPYGLLQPIA DAIKLFTKEP VXPQTSSKFL FTVAPILALT LALTVWAPLP MPYPLINLNL SLLFILAMSS LMVYSILWSG WASNSKYALM GALRAVAQTI SYEVSMTTII LSMVLMNGSF TLTAFATTQE HLWLIFPMWP LMMMWFTSTL AETNRAPFDL TEGESELVSG FNVEYSAGPF ALFFMAEYAN IIMMNALTVI LFMGTSCNPQ MPEISTINFV VKTIILTICF LWVRASYPRF RYDQLMYLLW KNFLPLTLAL CMWHISILIS LACIPPQA //