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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}.
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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
 
 
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