ID   NU4M_PHOSU              Reviewed;         208 AA.
AC   O21515;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
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;
DE   Flags: Fragment;
GN   Name=MT-ND4; Synonyms=MTND4, NADH4, ND4;
OS   Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Phodopus.
OX   NCBI_TaxID=10044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9491603; DOI=10.1093/oxfordjournals.molbev.a025845;
RA   Engel S.R., Hogan K.M., Taylor J.F., Davis S.K.;
RT   "Molecular systematics and paleobiogeography of the South American
RT   sigmodontine rodents.";
RL   Mol. Biol. Evol. 15:35-49(1998).
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:0000250|UniProtKB:P03910}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; U83804; AAB87228.1; -; Genomic_DNA.
DR   AlphaFoldDB; O21515; -.
DR   SMR; O21515; -.
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; 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; 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.
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..>208
FT                   /note="NADH-ubiquinone oxidoreductase chain 4"
FT                   /id="PRO_0000117968"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         208
SQ   SEQUENCE   208 AA;  23774 MW;  F95ED0116E7675C3 CRC64;
     MLKIIIPSIM LIPLTWFSNN KKVWINVTSY SFVINMIALV TLWQVNDITT NFSTMFSTDS
     LSSPLTMLTI WLLPLMLLAS QKHIKNQTDF NKKMYISLLI TLQVLLIMTF SANELIMFYI
     LFEATLIPTL IIITRWGNQA ERLNAGLYFL FYTLIGSIPL LIALISIQNT LGTLNIMLLS
     LDSSPQTPTW SSHILWLACI MAFMIKMP