NU1M_RAT
ID NU1M_RAT Reviewed; 318 AA.
AC P03889; O63197; Q37653;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03886};
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=Mtnd1; Synonyms=mt-Nd1, Nd1;
OS Rattus norvegicus (Rat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3190884;
RA Quagliariello C., Spena A.;
RT "Nucleotide sequence of the NADH dehydrogenase gene in mitochondrial DNA
RT from rat liver.";
RL Boll. Soc. Ital. Biol. Sper. 64:211-218(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=3399396; DOI=10.1093/nar/16.13.6233;
RA Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT "Nucleotide sequence of rat mitochondrial NADH dehydrogenase subunit 1.
RT GTG, a new initiator codon in vertebrate mitochondrial genome.";
RL Nucleic Acids Res. 16:6233-6233(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2504926; DOI=10.1007/bf02602930;
RA Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT "The complete nucleotide sequence of the Rattus norvegicus mitochondrial
RT genome: cryptic signals revealed by comparative analysis between
RT vertebrates.";
RL J. Mol. Evol. 28:497-516(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC STRAIN=Brown Norway, and Lewis; TISSUE=Spleen;
RX PubMed=1672544; DOI=10.1084/jem.173.4.823;
RA Davies J.D., Wilson D.H., Hermel E., Lindahl K.F., Butcher G.W.,
RA Wilson D.B.;
RT "Generation of T cells with lytic specificity for atypical antigens. I. A
RT mitochondrial antigen in the rat.";
RL J. Exp. Med. 173:823-832(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-9 IN COMPLEX WITH MHC.
RX PubMed=7664344; DOI=10.1016/0092-8674(95)90037-3;
RA Wang C.R., Castano A.R., Peterson P.A., Slaughter C., Lindahl K.F.,
RA Deisenhofer J.;
RT "Nonclassical binding of formylated peptide in crystal structure of the MHC
RT class Ib molecule H2-M3.";
RL Cell 82:655-664(1995).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor. Essential for the catalytic activity and assembly of complex
CC I. {ECO:0000250|UniProtKB:P03886}.
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:0000250|UniProtKB:P03886};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:P03887}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; M35826; AAA68204.1; -; Genomic_DNA.
DR EMBL; X07479; CAB50772.1; -; Genomic_DNA.
DR EMBL; X14848; CAA32954.1; -; Genomic_DNA.
DR EMBL; AY172581; AAN77594.1; -; Genomic_DNA.
DR EMBL; X56833; CAA40164.1; -; Genomic_DNA.
DR PIR; S04747; QQRT1M.
DR RefSeq; AP_004892.1; AC_000022.2.
DR RefSeq; YP_665629.1; NC_001665.2.
DR PDB; 1MHC; X-ray; 2.10 A; C/F=1-9.
DR PDBsum; 1MHC; -.
DR AlphaFoldDB; P03889; -.
DR SMR; P03889; -.
DR STRING; 10116.ENSRNOP00000049172; -.
DR PaxDb; P03889; -.
DR PRIDE; P03889; -.
DR Ensembl; ENSRNOT00000047550; ENSRNOP00000049172; ENSRNOG00000030644.
DR GeneID; 26193; -.
DR KEGG; rno:26193; -.
DR CTD; 4535; -.
DR RGD; 620555; mt-Nd1.
DR eggNOG; KOG4770; Eukaryota.
DR GeneTree; ENSGT00390000006621; -.
DR HOGENOM; CLU_015134_0_1_1; -.
DR InParanoid; P03889; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1214989at2759; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR EvolutionaryTrace; P03889; -.
DR PRO; PR:P03889; -.
DR Proteomes; UP000002494; Mitochondrion.
DR Bgee; ENSRNOG00000030644; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; P03889; baseline and differential.
DR Genevisible; P03889; RN.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..318
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117468"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 1..4
FT /note="MYFI -> M (in Ref. 1; AAA68204)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..19
FT /note="AF -> GL (in Ref. 1; AAA68204, 2; CAB50772 and 3;
FT CAA32954)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> S (in Ref. 5; CAA40164)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..40
FT /note="IV -> NE (in Ref. 1; AAA68204, 2; CAB50772, 3;
FT CAA32954 and 5; CAA40164)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> K (in Ref. 1; AAA68204, 2; CAB50772, 3;
FT CAA32954 and 5; CAA40164)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="L -> P (in Ref. 1; AAA68204, 2; CAB50772 and 3;
FT CAA32954)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="II -> LY (in Ref. 1; AAA68204, 2; CAB50772 and 3;
FT CAA32954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36145 MW; 747F012CD0893041 CRC64;
MYFINILTLL IPILIAMAFL TLVERKILGY MQLRKGPNIV GPYGILQPFA DAMKLFMKEP
MRPLTTSMSL FIIAPTLSLT LALSLWIPLP MPHPLINLNL GMLFILATSS LSVYSILWSG
WASNSKYSLF GALRAVAQTI SYEVTMAIIL LSVLLMSGSF SLQMLITTQE HIWLLIPAWP
MAMMWYISTL AETNRAPFDL TEGESELVSG FNVEYAAGPF ALFFMAEYTN IILMNALTSI
VFLGPLYHIN YPELYSTSFM TETLLLSTTF LWIRASYPRF RYDQLMHLLW KNFLPLTLAF
CMWYISLPIF LAGIPPYT
