NU1M_BOVIN
ID NU1M_BOVIN Reviewed; 318 AA.
AC P03887;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2 {ECO:0000269|PubMed:3141400};
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=MT-ND1; Synonyms=MTND1, NADH1, ND1;
OS Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-15, FORMYLATION AT MET-1, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=3141400; DOI=10.1016/s0021-9258(18)37571-9;
RA Yagi T., Hatefi Y.;
RT "Identification of the dicyclohexylcarbodiimide-binding subunit of NADH-
RT ubiquinone oxidoreductase (Complex I).";
RL J. Biol. Chem. 263:16150-16155(1988).
RN [4]
RP SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=17060615; DOI=10.1073/pnas.0607719103;
RA Carroll J., Fearnley I.M., Walker J.E.;
RT "Definition of the mitochondrial proteome by measurement of molecular
RT masses of membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16170-16175(2006).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
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 (PubMed:3141400). Essential for the catalytic activity of
CC complex I (PubMed:3141400). Essential for the assembly of complex I (By
CC similarity). {ECO:0000250|UniProtKB:P03886,
CC ECO:0000269|PubMed:3141400}.
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:0000269|PubMed:3141400};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits.
CC {ECO:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- MASS SPECTROMETRY: Mass=35699.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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; V00654; CAA23997.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08322.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08335.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12789.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12802.1; -; Genomic_DNA.
DR PIR; A00408; QXBO1M.
DR PDB; 5LC5; EM; 4.35 A; H=3-315.
DR PDB; 5LDW; EM; 4.27 A; H=1-318.
DR PDB; 5LDX; EM; 5.60 A; H=1-318.
DR PDB; 5O31; EM; 4.13 A; H=1-318.
DR PDB; 7QSD; EM; 3.10 A; H=1-318.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P03887; -.
DR SMR; P03887; -.
DR CORUM; P03887; -.
DR DIP; DIP-38830N; -.
DR IntAct; P03887; 1.
DR STRING; 9913.ENSBTAP00000053145; -.
DR BindingDB; P03887; -.
DR ChEMBL; CHEMBL4497; -.
DR DrugCentral; P03887; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P03887; -.
DR eggNOG; KOG4770; Eukaryota.
DR InParanoid; P03887; -.
DR Proteomes; UP000009136; Mitochondrion.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
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; Direct protein sequencing; Electron transport; Formylation;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..318
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117354"
FT TRANSMEM 2..22
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 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17060615,
FT ECO:0000269|PubMed:3141400"
SQ SEQUENCE 318 AA; 35670 MW; 638727DBA839B1C3 CRC64;
MFMINILMLI IPILLAVAFL TLVERKVLGY MQLRKGPNVV GPYGLLQPIA DAIKLFIKEP
LRPATSSASM FILAPIMALG LALTMWIPLP MPYPLINMNL GVLFMLAMSS LAVYSILWSG
WASNSKYALI GALRAVAQTI SYEVTLAIIL LSVLLMSGSF TLSTLITTQE QMWLILPAWP
LAMMWFISTL AETNRAPFDL TEGESELVSG FNVEYAAGPF ALFFMAEYAN IIMMNIFTAI
LFLGTSHNPH MPELYTINFT IKSLLLTMSF LWIRASYPRF RYDQLMHLLW KNFLPLTLAL
CMWHVSLPIL TSGIPPQT