NU2M_CAEEL
ID NU2M_CAEEL Reviewed; 282 AA.
AC P24889;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=nduo-2 {ECO:0000312|WormBase:MTCE.16};
GN Synonyms=nd2 {ECO:0000312|WormBase:MTCE.16};
GN ORFNames=MTCE.16 {ECO:0000312|WormBase:MTCE.16};
OS Caenorhabditis elegans.
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-66; TYR-112 AND
RP SER-194.
RC STRAIN=AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856,
RC CB4857, CB4858, KR314, PB303, PB306, RW7000, and TR403;
RX PubMed=12644560; DOI=10.1093/molbev/msg044;
RA Denver D.R., Morris K., Thomas W.K.;
RT "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT outcrossing.";
RL Mol. Biol. Evol. 20:393-400(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1551572; DOI=10.1093/genetics/130.3.471;
RA Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.;
RT "The mitochondrial genomes of two nematodes, Caenorhabditis elegans and
RT Ascaris suum.";
RL Genetics 130:471-498(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=2235493; DOI=10.1093/nar/18.20.6113;
RA Okimoto R., Macfarlane J.L., Wolstenholme D.R.;
RT "Evidence for the frequent use of TTG as the translation initiation codon
RT of mitochondrial protein genes in the nematodes, Ascaris suum and
RT Caenorhabditis elegans.";
RL Nucleic Acids Res. 18:6113-6118(1990).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; AY171163; AAO16340.1; -; Genomic_DNA.
DR EMBL; AY171164; AAO16341.1; -; Genomic_DNA.
DR EMBL; AY171165; AAO16342.1; -; Genomic_DNA.
DR EMBL; AY171166; AAO16343.1; -; Genomic_DNA.
DR EMBL; AY171167; AAO16344.1; -; Genomic_DNA.
DR EMBL; AY171168; AAO16345.1; -; Genomic_DNA.
DR EMBL; AY171169; AAO16346.1; -; Genomic_DNA.
DR EMBL; AY171170; AAO16347.1; -; Genomic_DNA.
DR EMBL; AY171171; AAO16348.1; -; Genomic_DNA.
DR EMBL; AY171172; AAO16349.1; -; Genomic_DNA.
DR EMBL; AY171173; AAO16350.1; -; Genomic_DNA.
DR EMBL; AY171174; AAO16351.1; -; Genomic_DNA.
DR EMBL; AY171175; AAO16352.1; -; Genomic_DNA.
DR EMBL; AY171176; AAO16353.1; -; Genomic_DNA.
DR EMBL; AY171177; AAO16354.1; -; Genomic_DNA.
DR EMBL; X54252; CAA38155.1; -; Genomic_DNA.
DR PIR; S26030; S26030.
DR RefSeq; NP_006957.1; NC_001328.1.
DR AlphaFoldDB; P24889; -.
DR SMR; P24889; -.
DR STRING; 6239.MTCE.16; -.
DR PaxDb; P24889; -.
DR EnsemblMetazoa; MTCE.16.1; MTCE.16.1; WBGene00010961.
DR GeneID; 2565695; -.
DR KEGG; cel:ND2; -.
DR CTD; 4536; -.
DR WormBase; MTCE.16; CE35347; WBGene00010961; nduo-2.
DR HOGENOM; CLU_987775_0_0_1; -.
DR InParanoid; P24889; -.
DR OrthoDB; 1153818at2759; -.
DR PRO; PR:P24889; -.
DR Proteomes; UP000001940; Mitochondrion.
DR Bgee; WBGene00010961; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:WormBase.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..282
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117564"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 66
FT /note="C -> F (in strain: AB1, AB2, CB4852, CB4853, CB4854,
FT CB4855, CB4857, CB4858, KR314 and PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 112
FT /note="F -> Y (in strain: CB4855)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 194
FT /note="G -> S (in strain: AB1, AB2, CB4852, CB4853, CB4854,
FT CB4855, CB4857, CB4858, KR314 and PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
SQ SEQUENCE 282 AA; 33306 MW; 86C05BEA9DAC8204 CRC64;
MIVFISLFTL FLTLLSILTN NVIVWWSIFL LMTVVFILLN KSSKSYTSIF NYFVIQESLG
LLFLLCSGGL LQFFIILLKI GVAPLHFWIF NVTNNIFNYG LMWFLTFQKL PFLTILLQIF
WLSSVYILLF GLLICYVQIF VMKSYKNLLI ISSTESFNWI VLGVFFSMFN TFYLFIYYFV
LMVLLISKFS KTSGYNFINW ETTLVFLNIP FSVSFFVKIF SLSEIFKYDS FFTLFLLFTM
FLSVLAFSFW LINLSMKNNE ETSNNNKMNY FIIFPLMVIS II
