NU4M_CAEEL
ID NU4M_CAEEL Reviewed; 409 AA.
AC P24892;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2 {ECO:0000255|RuleBase:RU003297};
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=nduo-4 {ECO:0000312|WormBase:MTCE.25};
GN Synonyms=nd4 {ECO:0000312|WormBase:MTCE.25};
GN ORFNames=MTCE.25 {ECO:0000312|WormBase:MTCE.25};
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 GLY-11; TRP-20; GLY-26;
RP CYS-30; CYS-45; SER-51; SER-61; GLY-64; VAL-70 AND SER-317.
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.
CC {ECO:0000250|UniProtKB:P03910}.
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:0000255|RuleBase:RU003297};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03910}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; AY171193; AAO16251.1; -; Genomic_DNA.
DR EMBL; AY171194; AAO16255.1; -; Genomic_DNA.
DR EMBL; AY171195; AAO16259.1; -; Genomic_DNA.
DR EMBL; AY171196; AAO16263.1; -; Genomic_DNA.
DR EMBL; AY171197; AAO16267.1; -; Genomic_DNA.
DR EMBL; AY171198; AAO16271.1; -; Genomic_DNA.
DR EMBL; AY171199; AAO16275.1; -; Genomic_DNA.
DR EMBL; AY171200; AAO16279.1; -; Genomic_DNA.
DR EMBL; AY171201; AAO16283.1; -; Genomic_DNA.
DR EMBL; AY171202; AAO16287.1; -; Genomic_DNA.
DR EMBL; AY171203; AAO16291.1; -; Genomic_DNA.
DR EMBL; AY171204; AAO16295.1; -; Genomic_DNA.
DR EMBL; AY171205; AAO16299.1; -; Genomic_DNA.
DR EMBL; AY171206; AAO16303.1; -; Genomic_DNA.
DR EMBL; AY171207; AAO16307.1; -; Genomic_DNA.
DR EMBL; X54252; CAA38158.1; -; Genomic_DNA.
DR PIR; S26033; S26033.
DR RefSeq; NP_006960.1; NC_001328.1.
DR AlphaFoldDB; P24892; -.
DR SMR; P24892; -.
DR IntAct; P24892; 2.
DR STRING; 6239.MTCE.25; -.
DR EPD; P24892; -.
DR PaxDb; P24892; -.
DR EnsemblMetazoa; MTCE.25.1; MTCE.25.1; WBGene00010963.
DR GeneID; 2565705; -.
DR KEGG; cel:ND4; -.
DR CTD; 4538; -.
DR WormBase; MTCE.25; CE35349; WBGene00010963; nduo-4.
DR eggNOG; KOG4845; Eukaryota.
DR GeneTree; ENSGT00730000111316; -.
DR HOGENOM; CLU_621950_0_0_1; -.
DR InParanoid; P24892; -.
DR OrthoDB; 996580at2759; -.
DR PhylomeDB; P24892; -.
DR PRO; PR:P24892; -.
DR Proteomes; UP000001940; Mitochondrion.
DR Bgee; WBGene00010963; Expressed in pharyngeal muscle cell (C elegans) and 4 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:0048039; F:ubiquinone binding; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; NAD; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..409
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000117911"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 11
FT /note="W -> G (in strain: AB1)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 20
FT /note="L -> W (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 26
FT /note="S -> G (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 30
FT /note="F -> C (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 45
FT /note="Y -> C (in strain: CB4856)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 51
FT /note="I -> S (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 61
FT /note="I -> S (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 64
FT /note="S -> G (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 70
FT /note="L -> V (in strain: PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 317
FT /note="G -> S (in strain: PB303)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 392..409
FT /note="SAPLVLMMYNVFWLSVFY -> QHH (in strain: KR314)"
SQ SEQUENCE 409 AA; 47207 MW; AFBFE452A5814F7C CRC64;
MLEFLFISLL WLFKPIYFLL FTVMFSFLIF NNFSWGGLFL VLDSYSFILL IVMSLFILGI
IVISEKNNNL LILSEILVFI CIIFFIPSNM MMLYMFFELS MFPILVMILG YGSQIEKINS
SYYLMFYAAF CSFPFLFVYF KSNFLLVFTY YNFVISWEMF FILSLSFMMK FPIYFLHLWL
PKAHVEAPTT ASMLLAGLLL KLGTAGFLRI LGSLSFVHNN VWILIAFLGM ILGSFCCVFQ
SDSKALAAYS SVTHMSFLLL SLVFITMSSK ISSVMLMLAH GYTSTLMFYL IGEFYHTSGS
RMIYFMSSFF SSSMIMGILF SVVFLSNSGV PPSLSFLSEF LVISNSMLIS KSMFVMIFIY
FVVSFYYSLF LITSSLMGKG YHNFNTWNVG FSAPLVLMMY NVFWLSVFY
