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Database: UniProt
Entry: NU3M_BOVIN
LinkDB: NU3M_BOVIN
Original site: NU3M_BOVIN 
ID   NU3M_BOVIN              Reviewed;         115 AA.
AC   P03898; Q8SEI7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 3 {ECO:0000250|UniProtKB:P03897};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03897};
DE   AltName: Full=NADH dehydrogenase subunit 3;
GN   Name=MT-ND3 {ECO:0000250|UniProtKB:P03897}; Synonyms=MTND3, NADH3, ND3;
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 of complex I.
CC       {ECO:0000250|UniProtKB:P03897}.
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:P03897};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits (PubMed:25209663).
CC       Interacts with TMEM186 (By similarity). Interacts with TMEM242 (By
CC       similarity). {ECO:0000250|UniProtKB:P03897,
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=13082.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17060615};
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family. {ECO:0000305}.
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DR   EMBL; V00654; CAA24008.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF490528; AAM08324.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF490529; AAM08337.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF493541; AAM12796.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF493542; AAM12809.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A00423; QXBO3M.
DR   RefSeq; YP_209212.2; NC_006853.1.
DR   PDB; 5LC5; EM; 4.35 A; A=2-112.
DR   PDB; 5LDW; EM; 4.27 A; A=1-115.
DR   PDB; 5LDX; EM; 5.60 A; A=1-115.
DR   PDB; 5O31; EM; 4.13 A; A=1-115.
DR   PDB; 7DGQ; EM; 5.00 A; 3=1-115.
DR   PDB; 7DGR; EM; 4.60 A; 3=1-115.
DR   PDB; 7DGS; EM; 7.80 A; 3=1-115.
DR   PDB; 7DGZ; EM; 3.80 A; 3=1-115.
DR   PDB; 7DH0; EM; 4.20 A; 3=1-115.
DR   PDB; 7DKF; EM; 8.30 A; 32=1-115.
DR   PDB; 7QSD; EM; 3.10 A; A=1-115.
DR   PDB; 7QSK; EM; 2.84 A; A=1-115.
DR   PDB; 7QSL; EM; 2.76 A; A=1-115.
DR   PDB; 7QSM; EM; 2.30 A; A=1-115.
DR   PDB; 7QSN; EM; 2.81 A; A=1-115.
DR   PDB; 7QSO; EM; 3.02 A; A=1-115.
DR   PDB; 7R41; EM; 2.30 A; A=1-115.
DR   PDB; 7R42; EM; 2.30 A; A=1-115.
DR   PDB; 7R43; EM; 2.40 A; A=1-115.
DR   PDB; 7R44; EM; 2.40 A; A=1-115.
DR   PDB; 7R45; EM; 2.40 A; A=1-115.
DR   PDB; 7R46; EM; 2.40 A; A=1-115.
DR   PDB; 7R47; EM; 2.30 A; A=1-115.
DR   PDB; 7R48; EM; 2.30 A; A=1-115.
DR   PDB; 7R4C; EM; 2.30 A; A=1-115.
DR   PDB; 7R4D; EM; 2.30 A; A=1-115.
DR   PDB; 7R4F; EM; 2.40 A; A=1-115.
DR   PDB; 7R4G; EM; 2.50 A; A=1-115.
DR   PDBsum; 5LC5; -.
DR   PDBsum; 5LDW; -.
DR   PDBsum; 5LDX; -.
DR   PDBsum; 5O31; -.
DR   PDBsum; 7DGQ; -.
DR   PDBsum; 7DGR; -.
DR   PDBsum; 7DGS; -.
DR   PDBsum; 7DGZ; -.
DR   PDBsum; 7DH0; -.
DR   PDBsum; 7DKF; -.
DR   PDBsum; 7QSD; -.
DR   PDBsum; 7QSK; -.
DR   PDBsum; 7QSL; -.
DR   PDBsum; 7QSM; -.
DR   PDBsum; 7QSN; -.
DR   PDBsum; 7QSO; -.
DR   PDBsum; 7R41; -.
DR   PDBsum; 7R42; -.
DR   PDBsum; 7R43; -.
DR   PDBsum; 7R44; -.
DR   PDBsum; 7R45; -.
DR   PDBsum; 7R46; -.
DR   PDBsum; 7R47; -.
DR   PDBsum; 7R48; -.
DR   PDBsum; 7R4C; -.
DR   PDBsum; 7R4D; -.
DR   PDBsum; 7R4F; -.
DR   PDBsum; 7R4G; -.
DR   AlphaFoldDB; P03898; -.
DR   EMDB; EMD-14127; -.
DR   EMDB; EMD-14251; -.
DR   EMDB; EMD-14256; -.
DR   EMDB; EMD-14261; -.
DR   EMDB; EMD-14266; -.
DR   EMDB; EMD-14272; -.
DR   EMDB; EMD-14277; -.
DR   EMDB; EMD-14282; -.
DR   EMDB; EMD-14287; -.
DR   EMDB; EMD-14292; -.
DR   EMDB; EMD-14297; -.
DR   EMDB; EMD-14302; -.
DR   EMDB; EMD-14307; -.
DR   EMDB; EMD-30673; -.
DR   EMDB; EMD-30674; -.
DR   EMDB; EMD-30675; -.
DR   EMDB; EMD-30676; -.
DR   EMDB; EMD-30677; -.
DR   EMDB; EMD-30706; -.
DR   EMDB; EMD-3731; -.
DR   EMDB; EMD-4032; -.
DR   EMDB; EMD-4040; -.
DR   EMDB; EMD-4041; -.
DR   SMR; P03898; -.
DR   CORUM; P03898; -.
DR   DIP; DIP-38829N; -.
DR   IntAct; P03898; 2.
DR   MINT; P03898; -.
DR   STRING; 9913.ENSBTAP00000053159; -.
DR   ChEMBL; CHEMBL4498; -.
DR   TCDB; 3.D.1.6.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; 9913-ENSBTAP00000053159; -.
DR   Ensembl; ENSBTAT00000060547.1; ENSBTAP00000053159.1; ENSBTAG00000043568.1.
DR   GeneID; 3283884; -.
DR   KEGG; bta:3283884; -.
DR   CTD; 4537; -.
DR   VEuPathDB; HostDB:ENSBTAG00000043568; -.
DR   eggNOG; KOG4662; Eukaryota.
DR   GeneTree; ENSGT00390000011605; -.
DR   HOGENOM; CLU_119549_3_1_1; -.
DR   InParanoid; P03898; -.
DR   OMA; RFPVKYY; -.
DR   OrthoDB; 5487322at2759; -.
DR   TreeFam; TF343336; -.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   Reactome; R-BTA-6799198; Complex I biogenesis.
DR   Proteomes; UP000009136; Mitochondrion.
DR   Bgee; ENSBTAG00000043568; Expressed in laryngeal cartilage and 103 other cell types or tissues.
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   Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR   PANTHER; PTHR11058:SF9; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
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..115
FT                   /note="NADH-ubiquinone oxidoreductase chain 3"
FT                   /id="PRO_0000117716"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:17060615"
FT   HELIX           2..23
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   HELIX           31..34
FT                   /evidence="ECO:0007829|PDB:7QSL"
FT   HELIX           53..72
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   HELIX           84..107
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:7QSM"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:7QSO"
SQ   SEQUENCE   115 AA;  13055 MW;  A55C1B856B1C3515 CRC64;
     MNLMLALLTN FTLATLLVII AFWLPQLNVY SEKTSPYECG FDPMGSARLP FSMKFFLVAI
     TFLLFDLEIA LLLPLPWASQ TANLNTMLTM ALFLIILLAV SLAYEWTQKG LEWTE
//
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