ID A0A0S2LM47_9EUTH Unreviewed; 318 AA. AC A0A0S2LM47; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 16-JAN-2019, entry version 5. 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:ALO62463.1}; OS Dasypus pilosus (hairy long-nosed armadillo). OG Mitochondrion {ECO:0000313|EMBL:ALO62463.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus. OX NCBI_TaxID=1756219 {ECO:0000313|EMBL:ALO62463.1}; RN [1] {ECO:0000313|EMBL:ALO62463.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26556496; DOI=10.1093/molbev/msv250; RA Gibb G.C., Condamine F.L., Kuch M., Enk J., Moraes-Barros N., RA Superina M., Poinar H.N., Delsuc F.; RT "Shotgun Mitogenomics Provides a Reference Phylogenetic Framework and RT Timescale for Living Xenarthrans."; RL Mol. Biol. Evol. 33:621-642(2016). 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; KT818544; ALO62463.1; -; Genomic_DNA. 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. 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:ALO62463.1}; 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 95 119 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 220 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 293 314 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 318 AA; 35584 MW; 5B5169DCFB99D916 CRC64; MHLINVLCLI IPILLAVAFL TLLERKILGY MQLRKGPNIV GPYGLLQPIA DAIKLFIKEP LRPATSSKLM FILAPTLALT LALSLWIPIP MPYPLINLNL GVLFILAMSS LAVYSILWSG WASNSKYALI GALRAVAQTI SYEVTLAIIL LSIMMTNGSF TLSTLTTTQE HMWLIFPLWP LAMMWFISTL AETNRAPFDL TEGESELVSG FNVEYAAGPF ALFFLAEYAN IIMMNALTAI LFFGAMHNPM FPELHTLNLV TKTLILTMMF LWVRASYPRF RYDQLMHLLW KSFLPLTLAL CMLHVSAPAT FAGVPPHM //