NU1M_ASCSU
ID NU1M_ASCSU Reviewed; 290 AA.
AC P24875;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=ND1;
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 inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; X54253; CAA38165.1; -; Genomic_DNA.
DR PIR; S26016; S26016.
DR RefSeq; NP_006943.1; NC_001327.1.
DR AlphaFoldDB; P24875; -.
DR SMR; P24875; -.
DR GeneID; 807667; -.
DR CTD; 4535; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner 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 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..290
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117348"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 290 AA; 33673 MW; 0873ECFFDA6F1D1F CRC64;
MILMLVQVIL IMIFVIQSIA FVTLYERHLL GGSQQRIGPN KVSFMGFLQA IFDGVKLLKK
EQMTPLNSSE ISFILVPGIF FIVMYLEWFV LPFFYDFMTF EYSILFFLCL IGFSVYTTLV
SGMVSKSKYG MVGAIRASSQ SVSYEIAFSL YLLAIVMHIN MFCFFSFFNL SLFIVYLPFL
FMVLAELNRA PFDFAEGESE LVSGYNVEYS SVAFVLLFLG EYGALLFFST LTSVLFFGFS
YVVIYCMFTI LVFVRSSYPR FRYDLMMYFF WFKLLPVSLI FLGYFVIFLF