ID A0A0U1XRK5_ATLCA Unreviewed; 324 AA. AC A0A0U1XRK5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 13-APR-2016, entry version 2. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU000473}; GN Name=ND1 {ECO:0000313|EMBL:AIY61400.1}; OS Atlantoraja castelnaui (Spotback skate) (Raja castelnaui). OG Mitochondrion {ECO:0000313|EMBL:AIY61400.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Batoidea; Rajiformes; Atlantoraja. OX NCBI_TaxID=1072469 {ECO:0000313|EMBL:AIY61400.1}; RN [1] {ECO:0000313|EMBL:AIY61400.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25418618; RA Duckett D.J., Naylor G.J.; RT "The complete mitochondrial genome of the endangered spotback skate, RT Atlantoraja castelnaui."; RL Mitochondrial DNA 1-2:0-0(2014). RN [2] {ECO:0000313|EMBL:AIY61400.1} RP NUCLEOTIDE SEQUENCE. RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A., RA Brescovit A.D., Santos A.J.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {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; KM507724; AIY61400.1; -; Genomic_DNA. DR RefSeq; YP_009112278.1; NC_025942.1. DR GeneID; 22549067; -. 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:AIY61400.1}; NAD {ECO:0000256|RuleBase:RU000471}; KW Oxidoreductase {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 6 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 260 279 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 320 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 324 AA; 36273 MW; B5DFF52C10933167 CRC64; MMNNILIYII HPLTYIIPVL LATAFLTLVE RKILGYMQLR KGPNVVGPYG LLQPIADGLK LFTKEPIRPS FSSHFLFLIT PTAALTLALL MWMPLPLPHS ILNLNLGLLF ILAISSLTVY TILGSGWASN SKYALMGALR AVAQTISYEV TLGLILLSLV IMTGSFTLHT FNLTQETIWL LIPAWPLAMM WYISTLAETN RAPFDLTEGE SELVSGFNIE YAGGPFALFF LAEYSNILMM NTLSVILFMG TSYNPTMPQI STLSLMIKAT LLTILFLWIR ASYPRFRYDQ LMHLVWKNFL PLTLALILWH ITLPASLASL PPLT //