NU1M_SCYCA
ID NU1M_SCYCA Reviewed; 324 AA.
AC O21408;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 79.
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 Scyliorhinus canicula (Small-spotted catshark) (Squalus canicula).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=7830;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9254918; DOI=10.1093/oxfordjournals.molbev.a025821;
RA Delarbre C., Barriel V., Tillier S., Janvier P., Gachelin G.;
RT "The main features of the craniate mitochondrial DNA between the ND1 and
RT the COI genes were established in the common ancestor with the lancelet.";
RL Mol. Biol. Evol. 14:807-813(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Muscle;
RX PubMed=9725850; DOI=10.1093/genetics/150.1.331;
RA Delarbre C., Spruyt N., Delmarre C., Gallut C., Barriel V., Janvier P.,
RA Laudet V., Gachelin G.;
RT "The complete nucleotide sequence of the mitochondrial DNA of the dogfish,
RT Scyliorhinus canicula.";
RL Genetics 150:331-344(1998).
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; Y09526; CAA70713.1; -; Genomic_DNA.
DR EMBL; Y16067; CAA76019.1; -; Genomic_DNA.
DR PIR; T11300; T11300.
DR RefSeq; NP_007614.1; NC_001950.1.
DR AlphaFoldDB; O21408; -.
DR SMR; O21408; -.
DR GeneID; 808294; -.
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..324
FT /note="NADH-ubiquinone oxidoreductase chain 1"
FT /id="PRO_0000117475"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 324 AA; 36162 MW; 31BB717684B67E76 CRC64;
MLQTTLLYLI NPLAYIIPIL LATAFLTLIE RKILGYMQFR KGPNIVGPYG LLQPIADGLK
LFIKEPIRPS ASSRSYFLAT PTVALALALL MWMPLPLPHS IINLNLGLLF ILAISSLTVY
TILGSGWASN SKYALMGALR AVAQTISYEV SLGLILLSMI IFAGGFTLHT FNLAQETIWL
LIPGWPLAFM WYISTLAETN RAPFDLTEGE SELVSGFNIE YAAGPFALFF LAEYTNILLM
NTLSVILFMG TSYNPLMPQI SSLSLMMKAS MLTVLFLWIR ASYPRFRYDQ LMHLVWKNFL
PLTLAIILWH MALPLATTSL PPLT
