ID   NU1M_PONPY              Reviewed;         318 AA.
AC   Q9T9X9; P92718; P92724;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03886};
DE   AltName: Full=NADH dehydrogenase subunit 1;
GN   Name=MT-ND1; Synonyms=MTND1, NADH1, ND1;
OS   Pongo pygmaeus (Bornean orangutan).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA   Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT   "Recent African origin of modern humans revealed by complete sequences of
RT   hominoid mitochondrial DNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-68.
RC   STRAIN=Isolate Anna, and Isolate Dennis;
RX   PubMed=8875856; DOI=10.1007/bf02337514;
RA   Xu X., Arnason U.;
RT   "The mitochondrial DNA molecule of Sumatran orangutan and a molecular
RT   proposal for two (Bornean and Sumatran) species of orangutan.";
RL   J. Mol. Evol. 43:431-437(1996).
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:P03886}.
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:P03886};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits.
CC       {ECO:0000250|UniProtKB:P03887}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR   EMBL; D38115; BAA85285.1; -; Genomic_DNA.
DR   EMBL; X97718; CAA66304.1; -; Genomic_DNA.
DR   EMBL; X97713; CAA66299.1; -; Genomic_DNA.
DR   RefSeq; NP_008225.1; NC_001646.1.
DR   AlphaFoldDB; Q9T9X9; -.
DR   SMR; Q9T9X9; -.
DR   GeneID; 807903; -.
DR   CTD; 4535; -.
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   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 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..318
FT                   /note="NADH-ubiquinone oxidoreductase chain 1"
FT                   /id="PRO_0000117463"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         68
FT                   /note="T -> I (in strain: Isolate Anna)"
FT                   /evidence="ECO:0000269|PubMed:8875856"
FT                   /id="VAR_019555"
FT   CONFLICT        168
FT                   /note="T -> P (in Ref. 1; BAA85285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="H -> N (in Ref. 1; BAA85285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="S -> Q (in Ref. 1; BAA85285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  35517 MW;  F0896D5333E00B1D CRC64;
     MPVINLLLLT MSILIAMAFL MLTERKILGY TQLRKGPNIV GPCGLLQPFA DALKLFTKEP
     LKPSTSTTIL YIVSPALALT IALLLWTPLP MPNPLINLNL GLLFILATSS LTVYSILWSG
     WASNSNYALI GTLRAVAQTI SYEITLALIL LSVLLMSGSF NLSTLITTQE HSWLLLPSWP
     LALMWFISTL AETNRAPFDL TEGESELVSG FNTEYAAGPF ALFFMAEYTN IILMNALTAM
     IFLGTTFNIH SPELHTTLFT IKTLLLTSLF LWIRSTYPRF RYDQLMHLLW KNFLPLTLAL
     LMWHISMPIT TSGIPPQT