ID   NU4LM_ECHTE             Reviewed;          98 AA.
AC   Q9G385; Q7YD90;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   Echinops telfairi (Lesser hedgehog tenrec).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mouchaty S.K., Gullberg A., Janke A., Arnason U.;
RT   "Phylogenetic position of the tenrecs (Mammalia: Tenrecidae) of Madagascar
RT   based on analysis of the complete mitochondrial genome sequence of Echinops
RT   telfairi.";
RL   Zool. Scr. 29:307-317(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12655143; DOI=10.1266/ggs.78.107;
RA   Nikaido M., Cao Y., Okada N., Hasegawa M.;
RT   "The phylogenetic relationships of insectivores with special reference to
RT   the lesser hedgehog tenrec as inferred from the complete sequence of their
RT   mitochondrial genome.";
RL   Genes Genet. Syst. 78:107-112(2003).
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; AJ400734; CAC19400.1; -; Genomic_DNA.
DR   EMBL; AJ245806; CAC69926.1; -; Genomic_DNA.
DR   EMBL; AB099484; BAC78895.1; -; Genomic_DNA.
DR   RefSeq; NP_072065.1; NC_002631.2.
DR   AlphaFoldDB; Q9G385; -.
DR   SMR; Q9G385; -.
DR   GeneID; 802334; -.
DR   CTD; 4539; -.
DR   HOGENOM; CLU_182394_0_0_1; -.
DR   OrthoDB; 1538435at2759; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:Ensembl.
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_0000275010"
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   CONFLICT        17
FT                   /note="M -> V (in Ref. 2; BAC78895)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   98 AA;  10937 MW;  629B90FD57A60208 CRC64;
     MPVIYINLIA AFFMAFMGLL IYRSHLMSSL LCLEGMMLSL FILNSTLALS MHFTLYSMMP
     IILLVFAACE AALGLSLLVM VSNTYGLDYV QNLNLLQC