NU2M_BOVIN
ID NU2M_BOVIN Reviewed; 347 AA.
AC P03892; Q8SFW9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
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 Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=17060615; DOI=10.1073/pnas.0607719103;
RA Carroll J., Fearnley I.M., Walker J.E.;
RT "Definition of the mitochondrial proteome by measurement of molecular
RT masses of membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16170-16175(2006).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
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:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- MASS SPECTROMETRY: Mass=39283.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
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DR EMBL; V00654; CAA23998.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08323.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08336.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12790.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12803.1; -; Genomic_DNA.
DR PIR; A00415; QXBO2M.
DR PDB; 5LC5; EM; 4.35 A; N=2-345.
DR PDB; 5LDW; EM; 4.27 A; N=1-347.
DR PDB; 5LDX; EM; 5.60 A; N=1-347.
DR PDB; 5O31; EM; 4.13 A; N=1-347.
DR PDB; 7QSD; EM; 3.10 A; N=1-347.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P03892; -.
DR SMR; P03892; -.
DR CORUM; P03892; -.
DR DIP; DIP-38799N; -.
DR IntAct; P03892; 1.
DR STRING; 9913.ENSBTAP00000053160; -.
DR ChEMBL; CHEMBL2112; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P03892; -.
DR eggNOG; KOG4668; Eukaryota.
DR InParanoid; P03892; -.
DR Proteomes; UP000009136; Mitochondrion.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Formylation; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..347
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117559"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
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"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17060615"
FT VARIANT 227
FT /note="T -> I (in strain: F)"
SQ SEQUENCE 347 AA; 39254 MW; 24105538A1374585 CRC64;
MNPIIFIIIL LTIMLGTIIV MISSHWLLVW IGFEMNMLAI IPIMMKNHNP RATEASTKYF
LTQSTASMLL MMAVIINLMF SGQWTVMKLF NPMASMLMTM ALAMKLGMAP FHFWVPEVTQ
GIPLSSGLIL LTWQKLAPMS VLYQIFPSIN LNLILTLSVL SILIGGWGGL NQTQLRKIMA
YSSIAHMGWM TAVLPYNPTM TLLNLIIYII MTSTMFTMFM ANSTTTTLSL SHTWNKTPIM
TVLILATLLS MGGLPPLSGF MPKWMIIQEM TKNNSIILPT FMAITALLNL YFYMRLTYST
TLTMFPSTNN MKMKWQFPLM KKMTFLPTMV VLSTMMLPLT PMLSVLE
