NU5M_BOVIN
ID NU5M_BOVIN Reviewed; 606 AA.
AC P03920; Q8SEN2; Q8SFW8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5;
DE EC=7.1.1.2 {ECO:0000250|UniProtKB:P03915};
DE AltName: Full=NADH dehydrogenase subunit 5;
GN Name=MT-ND5; Synonyms=MTND5, NADH5, ND5;
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], AND VARIANT THR-90.
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:P03915}.
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:P03915};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits.
CC {ECO:0000269|PubMed:25209663}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17060615}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- MASS SPECTROMETRY: Mass=68319.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17060615};
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; V00654; CAA24005.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08327.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08340.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12799.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12812.1; -; Genomic_DNA.
DR PIR; A00450; QXBO5M.
DR PDB; 5LC5; EM; 4.35 A; L=2-605.
DR PDB; 5LDW; EM; 4.27 A; L=1-606.
DR PDB; 5LDX; EM; 5.60 A; L=1-606.
DR PDB; 5O31; EM; 4.13 A; L=1-606.
DR PDB; 7QSD; EM; 3.10 A; L=1-606.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P03920; -.
DR SMR; P03920; -.
DR CORUM; P03920; -.
DR DIP; DIP-38827N; -.
DR IntAct; P03920; 1.
DR STRING; 9913.ENSBTAP00000053152; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P03920; -.
DR PRIDE; P03920; -.
DR eggNOG; KOG4668; Eukaryota.
DR InParanoid; P03920; -.
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:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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; IPR010934; NADH_DH_su5_C.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF06455; NADH5_C; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 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..606
FT /note="NADH-ubiquinone oxidoreductase chain 5"
FT /id="PRO_0000118068"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17060615"
FT VARIANT 90
FT /note="I -> T (in strain: F)"
FT /evidence="ECO:0000269|Ref.2"
FT CONFLICT 401
FT /note="T -> K (in Ref. 1; CAA24005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 68286 MW; 3DC4371F0328B068 CRC64;
MNMFSSLSLV TLLLLTMPIM MMSFNTYKPS NYPLYVKTAI SYAFITSMIP TMMFIHSGQE
LIISNWHWLT IQTLKLSLSF KMDYFSMMFI PVALFVTWSI MEFSMWYMYS DPNINKFFKY
LLLFLITMLI LVTANNLFQL FIGWEGVGIM SFLLIGWWYG RADANTAALQ AILYNRIGDI
GFILAMAWFL TNLNTWDLQQ IFMLNPSDSN MPLIGLALAA TGKSAQFGLH PWLPSAMEGP
TPVSALLHSS TMVVAGIFLL IRFYPLTENN KYIQSITLCL GAITTLFTAM CALTQNDIKK
IIAFSTSSQL GLMMVTIGIN QPYLAFLHIC THAFFKAMLF MCSGSIIHSL NDEQDIRKMG
GLFKAMPFTT TALIVGSLAL TGMPFLTGFY SKDLIIEAAN TSYTNAWALL MTLIATSFTA
IYSTRIIFFA LLGQPRFPTL VNINENNPLL INSIKRLLIG SLFAGYIISN NIPPTTIPQM
TMPYYLKTTA LIVTILGFIL ALEISNMTKN LKYHYPSNAF KFSTLLGYFP TIMHRLAPYM
NLSMSQKSAS SLLDLIWLEA ILPKTISLAQ MKASTLVTNQ KGLIKLYFLS FLITILISMI
LFNFHE
