ID   NU4LM_MOUSE             Reviewed;          98 AA.
AC   P03903;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 4L;
DE            EC=7.1.1.2 {ECO:0000269|PubMed:29915388};
DE   AltName: Full=NADH dehydrogenase subunit 4L {ECO:0000250|UniProtKB:P03901};
GN   Name=Mtnd4l {ECO:0000312|MGI:MGI:102497}; Synonyms=mt-Nd4l, Nd4l;
OS   Mus musculus (Mouse).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA   Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT   "Sequence and gene organization of mouse mitochondrial DNA.";
RL   Cell 26:167-180(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=12954771; DOI=10.1093/nar/gkg739;
RA   Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S.,
RA   Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y.,
RA   Enriquez J.A.;
RT   "Revisiting the mouse mitochondrial DNA sequence.";
RL   Nucleic Acids Res. 31:5349-5355(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4] {ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RX   PubMed=29915388; DOI=10.1038/s41594-018-0073-1;
RA   Agip A.A., Blaza J.N., Bridges H.R., Viscomi C., Rawson S., Muench S.P.,
RA   Hirst J.;
RT   "Cryo-EM structures of complex I from mouse heart mitochondria in two
RT   biochemically defined states.";
RL   Nat. Struct. Mol. Biol. 25:548-556(2018).
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:29915388). Part of the enzyme membrane arm which is
CC       embedded in the lipid bilayer and involved in proton translocation
CC       (PubMed:29915388). {ECO:0000269|PubMed:29915388}.
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:0000305|PubMed:29915388};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092;
CC         Evidence={ECO:0000305|PubMed:29915388};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits.
CC       {ECO:0000269|PubMed:29915388}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03902}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4L family. {ECO:0000305}.
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DR   EMBL; J01420; AAB48652.1; -; Genomic_DNA.
DR   EMBL; V00711; CAA24087.1; -; Genomic_DNA.
DR   EMBL; AY172335; AAN85130.1; -; Genomic_DNA.
DR   PIR; A00430; QXMS4L.
DR   RefSeq; NP_904336.1; NC_005089.1.
DR   PDB; 6G2J; EM; 3.30 A; K=1-98.
DR   PDB; 6G72; EM; 3.90 A; K=1-98.
DR   PDB; 6ZR2; EM; 3.10 A; K=1-98.
DR   PDB; 6ZTQ; EM; 3.00 A; K=1-98.
DR   PDB; 7AK5; EM; 3.17 A; K=1-98.
DR   PDB; 7AK6; EM; 3.82 A; K=1-98.
DR   PDB; 7B93; EM; 3.04 A; K=1-98.
DR   PDB; 7PSA; EM; 3.40 A; K=1-98.
DR   PDB; 8OLT; EM; 2.84 A; K=1-98.
DR   PDB; 8OM1; EM; 2.39 A; K=1-98.
DR   PDBsum; 6G2J; -.
DR   PDBsum; 6G72; -.
DR   PDBsum; 6ZR2; -.
DR   PDBsum; 6ZTQ; -.
DR   PDBsum; 7AK5; -.
DR   PDBsum; 7AK6; -.
DR   PDBsum; 7B93; -.
DR   PDBsum; 7PSA; -.
DR   PDBsum; 8OLT; -.
DR   PDBsum; 8OM1; -.
DR   AlphaFoldDB; P03903; -.
DR   EMDB; EMD-11377; -.
DR   EMDB; EMD-11424; -.
DR   EMDB; EMD-11810; -.
DR   EMDB; EMD-11811; -.
DR   EMDB; EMD-12095; -.
DR   EMDB; EMD-13611; -.
DR   EMDB; EMD-16962; -.
DR   EMDB; EMD-16965; -.
DR   EMDB; EMD-4345; -.
DR   EMDB; EMD-4356; -.
DR   SMR; P03903; -.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   IntAct; P03903; 1.
DR   STRING; 10090.ENSMUSP00000081021; -.
DR   iPTMnet; P03903; -.
DR   SwissPalm; P03903; -.
DR   PaxDb; 10090-ENSMUSP00000081021; -.
DR   ProteomicsDB; 289947; -.
DR   Antibodypedia; 68604; 91 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000084013.1; ENSMUSP00000081021.1; ENSMUSG00000065947.1.
DR   GeneID; 17720; -.
DR   KEGG; mmu:17720; -.
DR   AGR; MGI:102497; -.
DR   CTD; 4539; -.
DR   MGI; MGI:102497; mt-Nd4l.
DR   VEuPathDB; HostDB:ENSMUSG00000065947; -.
DR   eggNOG; KOG4669; Eukaryota.
DR   GeneTree; ENSGT00390000004755; -.
DR   HOGENOM; CLU_182394_0_0_1; -.
DR   InParanoid; P03903; -.
DR   OMA; MYRSHLM; -.
DR   OrthoDB; 3030031at2759; -.
DR   PhylomeDB; P03903; -.
DR   ChiTaRS; mt-Nd4l; mouse.
DR   PRO; PR:P03903; -.
DR   Proteomes; UP000000589; Mitochondrion.
DR   RNAct; P03903; Protein.
DR   Bgee; ENSMUSG00000065947; Expressed in cerebellar cortex and 63 other cell types or tissues.
DR   ExpressionAtlas; P03903; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISO:MGI.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   Gene3D; 1.10.287.3510; -; 1.
DR   InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR   InterPro; IPR039428; NUOK/Mnh_C1-like.
DR   PANTHER; PTHR11434:SF0; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4L; 1.
DR   PANTHER; PTHR11434; NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L; 1.
DR   Pfam; PF00420; Oxidored_q2; 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..98
FT                   /note="NADH-ubiquinone oxidoreductase chain 4L"
FT                   /id="PRO_0000118448"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        63
FT                   /note="Missing (in Ref. 1; AAB48652/CAA24087)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..20
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           26..50
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           58..85
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:8OM1"
SQ   SEQUENCE   98 AA;  10607 MW;  48CAF698FF5F4C29 CRC64;
     MPSTFFNLTM AFSLSLLGTL MFRSHLMSTL LCLEGMVLSL FIMTSVTSLN SNSMSSMPIP
     ITILVFAACE AAVGLALLVK VSNTYGTDYV QNLNLLQC
//