NDUV2_BOVIN
ID NDUV2_BOVIN Reviewed; 249 AA.
AC P04394; Q3T0G9;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=NADH dehydrogenase subunit II;
DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFV2;
OS Bos taurus (Bovine).
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 [MRNA].
RX PubMed=2500970; DOI=10.1021/bi00434a021;
RA Pilkington S.J., Walker J.E.;
RT "Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of
RT import precursors of the bovine and human 24-kDa subunit.";
RL Biochemistry 28:3257-3264(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-249.
RC TISSUE=Brain;
RX PubMed=2598272; DOI=10.1007/bf00393404;
RA Chomyn A., Tsai Lai S.S.-A.;
RT "cDNA of the 24 kDa subunit of the bovine respiratory chain NADH
RT dehydrogenase: high sequence conservation in mammals and tissue-specific
RT and growth-dependent expression.";
RL Curr. Genet. 16:117-125(1989).
RN [4]
RP PROTEIN SEQUENCE OF 33-249.
RC TISSUE=Heart;
RX PubMed=6861757; DOI=10.1111/j.1432-1033.1983.tb07543.x;
RA von Bahr-Lindstroem H., Galante Y.M., Persson M., Joernvall H.;
RT "The primary structure of subunit II of NADH dehydrogenase from bovine-
RT heart mitochondria.";
RL Eur. J. Biochem. 134:145-150(1983).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [6]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
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. {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (PubMed:10852722,
CC PubMed:18721790). This is a component of the flavoprotein-sulfur (FP)
CC fragment of the enzyme. {ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25209663}; Matrix side
CC {ECO:0000305|PubMed:25209663}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X14724; CAA32848.1; -; mRNA.
DR EMBL; BC102401; AAI02402.1; -; mRNA.
DR EMBL; M22539; AAA87358.1; -; mRNA.
DR PIR; B30113; B30113.
DR RefSeq; NP_776990.1; NM_174565.3.
DR PDB; 5LC5; EM; 4.35 A; E=1-249.
DR PDB; 5LDW; EM; 4.27 A; E=33-249.
DR PDB; 5LDX; EM; 5.60 A; E=33-249.
DR PDB; 5O31; EM; 4.13 A; E=33-249.
DR PDB; 7QSD; EM; 3.10 A; E=1-249.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P04394; -.
DR SMR; P04394; -.
DR CORUM; P04394; -.
DR DIP; DIP-38821N; -.
DR IntAct; P04394; 3.
DR STRING; 9913.ENSBTAP00000052906; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P04394; -.
DR PeptideAtlas; P04394; -.
DR PRIDE; P04394; -.
DR Ensembl; ENSBTAT00000006405; ENSBTAP00000052906; ENSBTAG00000004871.
DR GeneID; 282290; -.
DR KEGG; bta:282290; -.
DR CTD; 4729; -.
DR VEuPathDB; HostDB:ENSBTAG00000004871; -.
DR VGNC; VGNC:31975; NDUFV2.
DR eggNOG; KOG3196; Eukaryota.
DR GeneTree; ENSGT00390000017580; -.
DR HOGENOM; CLU_054362_1_0_1; -.
DR InParanoid; P04394; -.
DR OMA; VGKFHVQ; -.
DR OrthoDB; 1396088at2759; -.
DR TreeFam; TF300004; -.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-6799198; Complex I biogenesis.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000004871; Expressed in spermatocyte and 105 other 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:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Acetylation; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6861757"
FT CHAIN 33..249
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT mitochondrial"
FT /id="PRO_0000020002"
FT REGION 213..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6J6"
FT MOD_RES 193
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P19404"
FT CONFLICT 89..97
FT /note="QNGWLPISA -> SSGTSYPDVLKBZZZPPGGAAIILW (in Ref. 4;
FT AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27308 MW; 8F7E8259F08EBF65 CRC64;
MFLSAALRAR AAGLAAHWGK HIRNLHKTAV QNGAGGALFV HRDTPENNPE TPFDFTPENY
KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEILQVPPM RVYEVATFYT
MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC
VNAPMVQIND NYYEDLTPKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG
PGFGVQAGL
