NU4LM_BOVIN
ID NU4LM_BOVIN Reviewed; 98 AA.
AC P03902; Q8SFX7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4L;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 4L;
GN Name=MT-ND4L; Synonyms=MTND4L, NADH4L, ND4L;
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 SUBUNIT, IDENTIFICATION IN COMPLEX I, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
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. {ECO:0000269|PubMed:18721790}.
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 -!- 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:18721790,
CC ECO:0000269|PubMed:25209663}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MASS SPECTROMETRY: Mass=10825.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
CC -!- SIMILARITY: Belongs to the complex I subunit 4L family. {ECO:0000305}.
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DR EMBL; V00654; CAA24004.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08325.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08338.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12797.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12810.1; -; Genomic_DNA.
DR PIR; A00429; QXBO4L.
DR RefSeq; YP_209213.1; NC_006853.1.
DR PDB; 5LC5; EM; 4.35 A; K=2-96.
DR PDB; 5LDW; EM; 4.27 A; K=1-98.
DR PDB; 5LDX; EM; 5.60 A; K=1-98.
DR PDB; 5O31; EM; 4.13 A; K=1-98.
DR PDB; 7QSD; EM; 3.10 A; K=1-98.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P03902; -.
DR SMR; P03902; -.
DR CORUM; P03902; -.
DR DIP; DIP-62099N; -.
DR STRING; 9913.ENSBTAP00000053153; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P03902; -.
DR Ensembl; ENSBTAT00000060543; ENSBTAP00000053153; ENSBTAG00000043559.
DR GeneID; 3283885; -.
DR KEGG; bta:3283885; -.
DR CTD; 4539; -.
DR VEuPathDB; HostDB:ENSBTAG00000043559; -.
DR eggNOG; KOG4669; Eukaryota.
DR GeneTree; ENSGT00390000004755; -.
DR HOGENOM; CLU_182394_0_0_1; -.
DR InParanoid; P03902; -.
DR OMA; YRSHLMS; -.
DR OrthoDB; 1538435at2759; -.
DR TreeFam; TF338190; -.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043559; Expressed in spermatocyte and 104 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; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 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..98
FT /note="NADH-ubiquinone oxidoreductase chain 4L"
FT /id="PRO_0000118396"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17060615"
FT VARIANT 65
FT /note="V -> A (in strain: 66)"
SQ SEQUENCE 98 AA; 10797 MW; 4DB48B7DA59C1881 CRC64;
MSMVYMNIMM AFTVSLVGLL MYRSHLMSSL LCLEGMMLSL FVMAALTILN SHFTLASMMP
IILLVFAACE AALGLSLLVM VSNTYGTDYV QNLNLLQC
