NU1M_CANLU
ID NU1M_CANLU Reviewed; 318 AA.
AC Q3L6Y8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=MT-ND1; Synonyms=MTND1, NADH1, ND1;
OS Canis lupus (Gray wolf).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9612;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15964215; DOI=10.1016/j.ympev.2005.04.025;
RA Delisle I., Strobeck C.;
RT "A phylogeny of the Caniformia (order Carnivora) based on 12 complete
RT protein-coding mitochondrial genes.";
RL Mol. Phylogenet. Evol. 37:192-201(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16809672; DOI=10.1101/gr.5117706;
RA Bjornerfeldt S., Webster M.T., Vila C.;
RT "Relaxation of selective constraint on dog mitochondrial DNA following
RT domestication.";
RL Genome Res. 16:990-994(2006).
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; AY598500; AAU00446.1; -; Genomic_DNA.
DR EMBL; DQ480503; ABE48155.1; -; Genomic_DNA.
DR EMBL; DQ480504; ABE48168.1; -; Genomic_DNA.
DR EMBL; DQ480505; ABE48181.1; -; Genomic_DNA.
DR EMBL; DQ480506; ABE48194.1; -; Genomic_DNA.
DR EMBL; DQ480507; ABE48207.1; -; Genomic_DNA.
DR EMBL; DQ480508; ABE48220.1; -; Genomic_DNA.
DR RefSeq; YP_626728.1; NC_008092.1.
DR AlphaFoldDB; Q3L6Y8; -.
DR SMR; Q3L6Y8; -.
DR GeneID; 4097764; -.
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 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_0000269893"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
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"
SQ SEQUENCE 318 AA; 35892 MW; 3A5CF63757213548 CRC64;
MFFINIISLI IPILLAVAFL TLVERKVLGY MQLRKGPNIV GPYGLLQPIA DAVKLFTKEP
LRPLTSSMSM FILAPILALS LALTMWIPLP MPYPLINMNL GVLFMLAMSS LAVYSILWSG
WASNSKYALI GALRAVAQTI SYEVTLAIIL LSVLLMNGSF TLSTLIITQE HMWLIFPAWP
LAMMWFISTL AETNRAPFDL TEGESELVSG FNVEYAAGPF ALFFLAEYAN IIMMNILTTI
LFFGAFHNPF MPELYSINFT MKTLLLTICF LWIRASYPRF RYDQLMHLLW KNFLPLTLAL
CMWHVALPII TASIPPQT