NU4M_ASCSU
ID NU4M_ASCSU Reviewed; 409 AA.
AC P24880;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 4;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 4;
GN Name=ND4;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Body wall muscle, and Egg;
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).
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 membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; X54253; CAA38170.1; -; Genomic_DNA.
DR PIR; S26021; S26021.
DR RefSeq; NP_006948.1; NC_001327.1.
DR AlphaFoldDB; P24880; -.
DR SMR; P24880; -.
DR GeneID; 807666; -.
DR CTD; 4538; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; 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; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..409
FT /note="NADH-ubiquinone oxidoreductase chain 4"
FT /id="PRO_0000117893"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
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 246..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 409 AA; 47065 MW; A4B135C1CA5587B6 CRC64;
MLDILLFSLY FFFEPVLFFF FMVVFGFVAL NNYSWLGCFY FFDSFSFILL IVMSLFILGV
VLLSESNFML LLLSEVLVVV CVFFFVPSNV ILMYMYFELS MFPILVMILG YGSQIEKINS
SYYLIFYAAL CSFPFLFVYF KSFFFISLVY FDFNLSWEMV FVLSLSFMMK FPVYFLHLWL
PKAHVEAPTT ASMLLAGLLL KLGTAGFLRI LGCLSFVHNN VWIVLAFLGM ILASFCCMFQ
SDAKALAAYS SITHMSFVLM ALVFIIMSGK TGGVILMLAH GYTSTLMFYL VGEFYHVSGS
RMVYYMSSFF GSGMIMALLF AVVFLSNMGT PPSLSFLSEF IVISSSLNMM KFSFWVLFVY
FFSAFYYSIY LLTSSVMGKG YVNFSIWNVG FSVPLVFMMY NIFWMSVFF