NU2M_MOUSE
ID NU2M_MOUSE Reviewed; 345 AA.
AC P03893;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000305};
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE AltName: Full=NADH dehydrogenase subunit 2;
GN Name=mt-Nd2 {ECO:0000312|MGI:MGI:102500}; Synonyms=Nd2;
OS Mus musculus (Mouse).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT "Sequence and gene organization of mouse mitochondrial DNA.";
RL Cell 26:167-180(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12954771; DOI=10.1093/nar/gkg739;
RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S.,
RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y.,
RA Enriquez J.A.;
RT "Revisiting the mouse mitochondrial DNA sequence.";
RL Nucleic Acids Res. 31:5349-5355(2003).
RN [3]
RP PROTEIN SEQUENCE OF 237-272 AND 296-312, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; J01420; AAB48645.1; -; Genomic_DNA.
DR EMBL; V00711; CAA24081.1; -; Genomic_DNA.
DR EMBL; AY172335; AAN85123.1; -; Genomic_DNA.
DR EMBL; AY339599; AAP89024.1; -; Genomic_DNA.
DR PIR; A00416; QXMS2M.
DR RefSeq; NP_904329.1; NC_005089.1.
DR PDB; 6G2J; EM; 3.30 A; N=1-345.
DR PDB; 6G72; EM; 3.90 A; N=1-345.
DR PDB; 6ZR2; EM; 3.10 A; N=1-345.
DR PDB; 6ZTQ; EM; 3.00 A; N=1-345.
DR PDB; 7AK5; EM; 3.17 A; N=1-345.
DR PDB; 7AK6; EM; 3.82 A; N=1-345.
DR PDB; 7B93; EM; 3.04 A; N=1-345.
DR PDB; 7PSA; EM; 3.40 A; N=1-345.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; P03893; -.
DR SMR; P03893; -.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR IntAct; P03893; 3.
DR MINT; P03893; -.
DR STRING; 10090.ENSMUSP00000080992; -.
DR PhosphoSitePlus; P03893; -.
DR jPOST; P03893; -.
DR PaxDb; P03893; -.
DR PRIDE; P03893; -.
DR ProteomicsDB; 287843; -.
DR Antibodypedia; 47876; 63 antibodies from 19 providers.
DR Ensembl; ENSMUST00000082396; ENSMUSP00000080992; ENSMUSG00000064345.
DR GeneID; 17717; -.
DR KEGG; mmu:17717; -.
DR CTD; 4536; -.
DR MGI; MGI:102500; mt-Nd2.
DR VEuPathDB; HostDB:ENSMUSG00000064345; -.
DR eggNOG; KOG4668; Eukaryota.
DR GeneTree; ENSGT00730000111348; -.
DR HOGENOM; CLU_007100_1_3_1; -.
DR InParanoid; P03893; -.
DR OMA; HFWVPEV; -.
DR OrthoDB; 1153818at2759; -.
DR PhylomeDB; P03893; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR ChiTaRS; mt-Nd2; mouse.
DR PRO; PR:P03893; -.
DR Proteomes; UP000000589; Mitochondrion.
DR RNAct; P03893; protein.
DR Bgee; ENSMUSG00000064345; Expressed in dentate gyrus of hippocampal formation granule cell and 60 other tissues.
DR ExpressionAtlas; P03893; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:MGI.
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; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..345
FT /note="NADH-ubiquinone oxidoreductase chain 2"
FT /id="PRO_0000117607"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..171
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 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 294
FT /note="T -> I (in Ref. 1; AAB48645/CAA24081 and 2;
FT AAP89024)"
FT /evidence="ECO:0000305"
FT HELIX 3..21
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 50..81
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:7AK5"
FT HELIX 199..222
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 276..301
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 345 AA; 38752 MW; F6855CA2CA3F2E59 CRC64;
MNPITLAIIY FTIFLGPVIT MSSTNLMLMW VGLEFSLLAI IPMLINKKNP RSTEAATKYF
VTQATASMII LLAIVLNYKQ LGTWMFQQQT NGLILNMTLM ALSMKLGLAP FHFWLPEVTQ
GIPLHMGLIL LTWQKIAPLS ILIQIYPLLN STIILMLAIT SIFMGAWGGL NQTQMRKIMA
YSSIAHMGWM LAILPYNPSL TLLNLMIYII LTAPMFMALM LNNSMTINSI SLLWNKTPAM
LTMISLMLLS LGGLPPLTGF LPKWIIITEL MKNNCLIMAT LMAMMALLNL FFYTRLIYST
SLTMFPTNNN SKMMTHQTKT KPNLMFSTLA IMSTMTLPLA PQLIT
