NU2M_CANLF
ID NU2M_CANLF Reviewed; 347 AA.
AC Q9ZZ65;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:P03891};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=MT-ND2 {ECO:0000250|UniProtKB:P03891}; Synonyms=MTND2, NADH2, ND2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=9878232; DOI=10.1006/mpev.1998.0513;
RA Kim K.S., Lee S.E., Jeong H.W., Ha J.H.;
RT "The complete nucleotide sequence of the domestic dog (Canis familiaris)
RT mitochondrial genome.";
RL Mol. Phylogenet. Evol. 10:210-220(1998).
RN [2]
RP SEQUENCE REVISION TO 2.
RA Kim K.S., Lee S.E., Jeong H.W., Jeong S.Y., Sohn H.S., Ha J.H.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Beagle;
RA Zhu S., Xu Q., Chang H.;
RT "The complete mitochondrial DNA sequence of the Beagle dog (Canis
RT familiaris).";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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:P03891}.
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:P03891};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Interacts with TMEM242
CC (By similarity). {ECO:0000250|UniProtKB:P03891,
CC ECO:0000250|UniProtKB:P03892}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; U96639; AAD04764.2; -; Genomic_DNA.
DR EMBL; AY729880; AAU12150.1; -; Genomic_DNA.
DR PIR; T11494; T11494.
DR RefSeq; NP_008472.4; NC_002008.4.
DR AlphaFoldDB; Q9ZZ65; -.
DR SMR; Q9ZZ65; -.
DR STRING; 9612.ENSCAFP00000030310; -.
DR PaxDb; Q9ZZ65; -.
DR GeneID; 804477; -.
DR KEGG; cfa:804477; -.
DR CTD; 4536; -.
DR eggNOG; KOG4668; Eukaryota.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; Q9ZZ65; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR TreeFam; TF343996; -.
DR Reactome; R-CFA-611105; Respiratory electron transport.
DR Reactome; R-CFA-6799198; Complex I biogenesis.
DR Proteomes; UP000002254; Mitochondrion.
DR Bgee; ENSCAFG00000022717; Expressed in spinal cord and 47 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
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 InterPro; IPR010933; NADH_DH_su2_C.
DR InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF06444; NADH_dehy_S2_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01436; NADHDHGNASE2.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..347
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117565"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 39102 MW; B2F64A18D6AEF80A CRC64;
MKPPILIIIM ATIMTGTMIV MLSSHWLLIW IGFEMNMLAI IPILMKKYNP RAMEASTKYF
LTQATASMLL MMGVTINLLY SGQWVISKIS NPIASIMMTT ALTMKLGLSP FHFWVPEVTQ
GITLMSGMIL LTWQKIAPMS ILYQISPSIN TNLLMLMALT SVLVGGWGGL NQTQLRKIMA
YSSIAHMGWM AAIITYNPTM MVLNLTLYIL MTLSTFMLFM LNSSTTTLSL SHMWNKFPLI
TSMILILMLS LGGLPPLSGF IPKWMIIQEL TKNNMIIIPT LMAITALLNL YFYLRLTYST
ALTMFPSTNN MKMKWQFEYT KKATLLPPLI ITSTMLLPLT PMLSVLD
