NU1M_ELEMA
ID NU1M_ELEMA Reviewed; 318 AA.
AC Q2I3H4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03886};
DE AltName: Full=NADH dehydrogenase subunit 1;
GN Name=MT-ND1; Synonyms=MTND1, NADH1, ND1;
OS Elephas maximus (Indian elephant).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
OX NCBI_TaxID=9783;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA Chumakov I., Grigorenko A.P.;
RT "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT Mammuthus primigenius.";
RL PLoS Biol. 4:403-410(2006).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor. Essential for the catalytic activity and assembly of complex
CC I. {ECO:0000250|UniProtKB:P03886}.
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:0000250|UniProtKB:P03886};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits.
CC {ECO:0000250|UniProtKB:P03887}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; DQ316068; ABC17891.1; -; Genomic_DNA.
DR RefSeq; YP_626367.1; NC_005129.2.
DR AlphaFoldDB; Q2I3H4; -.
DR SMR; Q2I3H4; -.
DR GeneID; 2610367; -.
DR CTD; 4535; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
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_0000232846"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
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; 35789 MW; 6F71F66701E7971D CRC64;
MFLINVLTVT LPILPAVAFL TLVERKALGY MQLRKGPNVV GPYGLLQPIA DAIKLFTKEP
IYPQTSSKFL FTVAPILALT LALTVWAPLP MPYPLINLNL SLLFILAMSS LMVYSILWSG
WASNSKYALM GALRAVAQTI SYEVSMTTIT LSMVLMNGSF TLTAFATTQE HLWLIFPMWP
LMMMWFTSTL AETNRAPFDL TEGESELVSG FNVEYSAGPF ALFFMAEYAN IIMMNALTVI
LFMGTSCDPQ MPEISTINFV MKTIILTICF LWVRASYPRF RYDQLMYLLW KNFLPLTLAL
CMWHISILIS LACIPPQA