ID   NU4LM_LEPSH             Reviewed;          98 AA.
AC   Q00GQ9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 39.
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   Lepilemur sahamalazensis (Sahamalaza sportive lemur).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lepilemuridae; Lepilemur.
OX   NCBI_TaxID=342398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate LAZA5.01, and Isolate LAZA5.10;
RA   Louis E.E. Jr., Engberg S.E., Lei R., Geng H., Sommer J.A.,
RA   Randriamampionona R., Randriamanana J.C., Zaonarivelo J.R.,
RA   Andriantompohavana R., Randria G., Ramaromilanto B., Rakotoarisoa G.,
RA   Rooney A., Brenneman R.A.;
RT   "Molecular and morphological analyses of the sportive lemurs (family
RT   Megaladapidae: genus Lepilemur) reveals 11 previously unrecognized
RT   species.";
RL   (In) Baker R.J. (eds.);
RL   Texas Tech University Special Publications, pp.49:1-47, Texas Tech
RL   University, Lubbock (2006).
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:0000250|UniProtKB:P03902}.
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:0000250|UniProtKB:P03902}.
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; DQ529737; ABG74266.1; -; Genomic_DNA.
DR   EMBL; DQ529738; ABG74270.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00GQ9; -.
DR   SMR; Q00GQ9; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..98
FT                   /note="NADH-ubiquinone oxidoreductase chain 4L"
FT                   /id="PRO_0000275040"
FT   TRANSMEM        2..22
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"
SQ   SEQUENCE   98 AA;  10749 MW;  26767AD53AC4CE26 CRC64;
     MPSISTNITL AFTIALTGML VFRSHLMSSL LCLEGMMLAM FILSILFIMN LHYTVSFIMP
     ILLLVLAACE AAIGLALLVM VSNTYGLDHI QNLNLLQC