NU4M_BOVIN
ID NU4M_BOVIN Reviewed; 459 AA.
AC P03910; Q8SE30;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03905};
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=MT-ND4; Synonyms=MTND4, NADH4, ND4;
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 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 [4]
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. Essential for the catalytic activity and assembly of complex
CC I. {ECO:0000250|UniProtKB:P03905}.
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:P03905};
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}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MASS SPECTROMETRY: Mass=52130.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; V00654; CAA24009.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF490528; AAM08326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF490529; AAM08339.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF493541; AAM12798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF493542; AAM12811.1; ALT_SEQ; Genomic_DNA.
DR PIR; A00439; QXBO4M.
DR RefSeq; YP_209214.1; NC_006853.1.
DR PDB; 5LC5; EM; 4.35 A; M=3-459.
DR PDB; 5LDW; EM; 4.27 A; M=1-459.
DR PDB; 5LDX; EM; 5.60 A; M=1-459.
DR PDB; 5O31; EM; 4.13 A; M=1-459.
DR PDB; 7QSD; EM; 3.10 A; M=1-459.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P03910; -.
DR SMR; P03910; -.
DR CORUM; P03910; -.
DR DIP; DIP-38798N; -.
DR IntAct; P03910; 1.
DR STRING; 9913.ENSBTAP00000053150; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P03910; -.
DR PRIDE; P03910; -.
DR Ensembl; ENSBTAT00000060552; ENSBTAP00000053150; ENSBTAG00000043577.
DR GeneID; 3283886; -.
DR KEGG; bta:3283886; -.
DR CTD; 4538; -.
DR VEuPathDB; HostDB:ENSBTAG00000043577; -.
DR eggNOG; KOG4845; Eukaryota.
DR GeneTree; ENSGT00730000111316; -.
DR HOGENOM; CLU_007100_4_0_1; -.
DR InParanoid; P03910; -.
DR OMA; ITRWGNQ; -.
DR OrthoDB; 996580at2759; -.
DR TreeFam; TF343520; -.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-6799198; Complex I biogenesis.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043577; Expressed in occipital lobe and 103 other tissues.
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; ISS:UniProtKB.
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 InterPro; IPR000260; NADH4_N.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF01059; Oxidored_q5_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Formylation; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..459
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000117906"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17060615"
SQ SEQUENCE 459 AA; 52099 MW; EE7061AA41977CB4 CRC64;
MLKYIIPTIM LMPLTWLSKN NMIWVNSTAH SLLISFTSLL LMNQFGDNSL NFSLLFFSDS
LSTPLLILTM WLLPLMLMAS QHHLSKENLT RKKLFITMLI SLQLFLIMTF TAMELILFYI
LFEATLVPTL IIITRWGNQT ERLNAGLYFL FYTLAGSLPL LVALIYIQNT VGSLNFLMLQ
YWVQPVHNSW SNVFMWLACM MAFMVKMPLY GLHLWLPKAH VEAPIAGSMV LAAVLLKLGG
YGMLRITLIL NPMTDFMAYP FIMLSLWGMI MTSSICLRQT DLKSLIAYSS VSHMALVIVA
ILIQTPWSYM GATALMIAHG LTSSMLFCLA NSNYERIHSR TMILARGLQT LLPLMATWWL
LASLTNLALP PTINLIGELF VVMSTFSWSN ITIILMGVNM VITALYSLYM LIMTQRGKYT
YHINNISPSF TRENALMSLH ILPLLLLTLN PKIILGPLY
