NDUV2_MOUSE
ID NDUV2_MOUSE Reviewed; 248 AA.
AC Q9D6J6; Q3U9L9; Q8BU07; Q8K2L0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufv2;
OS Mus musculus (Mouse).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Cerebellum, Heart, Hippocampus, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 42-61; 68-123; 129-153 AND 199-208, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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:0000250|UniProtKB:P04394}.
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. This is a component of
CC the flavoprotein-sulfur (FP) fragment of the enzyme (By similarity).
CC {ECO:0000250|UniProtKB:P04394}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P04394}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04394}; Matrix side
CC {ECO:0000250|UniProtKB:P04394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6J6-2; Sequence=VSP_025017;
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AK013511; BAB28888.1; -; mRNA.
DR EMBL; AK078351; BAC37233.1; -; mRNA.
DR EMBL; AK088193; BAC40201.1; -; mRNA.
DR EMBL; AK146998; BAE27595.1; -; mRNA.
DR EMBL; AK150404; BAE29530.1; -; mRNA.
DR EMBL; AK151729; BAE30647.1; -; mRNA.
DR EMBL; AK159460; BAE35102.1; -; mRNA.
DR EMBL; AK166539; BAE38841.1; -; mRNA.
DR EMBL; AK169143; BAE40922.1; -; mRNA.
DR EMBL; BC030946; AAH30946.1; -; mRNA.
DR CCDS; CCDS37679.1; -. [Q9D6J6-1]
DR CCDS; CCDS70836.1; -. [Q9D6J6-2]
DR RefSeq; NP_001265344.1; NM_001278415.1. [Q9D6J6-2]
DR RefSeq; NP_082664.1; NM_028388.3. [Q9D6J6-1]
DR PDB; 6G2J; EM; 3.30 A; E=1-248.
DR PDB; 6G72; EM; 3.90 A; E=1-248.
DR PDB; 6ZR2; EM; 3.10 A; E=1-248.
DR PDB; 6ZTQ; EM; 3.00 A; E=1-248.
DR PDB; 7AK5; EM; 3.17 A; E=1-245.
DR PDB; 7AK6; EM; 3.82 A; E=1-248.
DR PDB; 7B93; EM; 3.04 A; E=1-248.
DR PDB; 7PSA; EM; 3.40 A; E=1-248.
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; Q9D6J6; -.
DR SMR; Q9D6J6; -.
DR BioGRID; 215635; 72.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q9D6J6; -.
DR IntAct; Q9D6J6; 6.
DR MINT; Q9D6J6; -.
DR STRING; 10090.ENSMUSP00000121557; -.
DR iPTMnet; Q9D6J6; -.
DR PhosphoSitePlus; Q9D6J6; -.
DR SwissPalm; Q9D6J6; -.
DR REPRODUCTION-2DPAGE; Q9D6J6; -.
DR EPD; Q9D6J6; -.
DR jPOST; Q9D6J6; -.
DR MaxQB; Q9D6J6; -.
DR PaxDb; Q9D6J6; -.
DR PeptideAtlas; Q9D6J6; -.
DR PRIDE; Q9D6J6; -.
DR ProteomicsDB; 293649; -. [Q9D6J6-1]
DR ProteomicsDB; 293650; -. [Q9D6J6-2]
DR Antibodypedia; 1273; 287 antibodies from 32 providers.
DR Ensembl; ENSMUST00000024909; ENSMUSP00000024909; ENSMUSG00000024099. [Q9D6J6-2]
DR Ensembl; ENSMUST00000143987; ENSMUSP00000121557; ENSMUSG00000024099. [Q9D6J6-1]
DR GeneID; 72900; -.
DR KEGG; mmu:72900; -.
DR UCSC; uc008dgw.2; mouse. [Q9D6J6-1]
DR CTD; 4729; -.
DR MGI; MGI:1920150; Ndufv2.
DR VEuPathDB; HostDB:ENSMUSG00000024099; -.
DR eggNOG; KOG3196; Eukaryota.
DR GeneTree; ENSGT00390000017580; -.
DR HOGENOM; CLU_054362_1_1_1; -.
DR InParanoid; Q9D6J6; -.
DR OMA; VGKFHVQ; -.
DR OrthoDB; 1396088at2759; -.
DR PhylomeDB; Q9D6J6; -.
DR TreeFam; TF300004; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 72900; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Ndufv2; mouse.
DR PRO; PR:Q9D6J6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D6J6; protein.
DR Bgee; ENSMUSG00000024099; Expressed in interventricular septum and 266 other tissues.
DR ExpressionAtlas; Q9D6J6; baseline and differential.
DR Genevisible; Q9D6J6; MM.
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; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISO:MGI.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
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; Alternative splicing;
KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..248
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 2,
FT mitochondrial"
FT /id="PRO_0000020004"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 175
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 179
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 192
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P19404"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025017"
FT CONFLICT 64
FT /note="A -> T (in Ref. 1; BAB28888)"
FT /evidence="ECO:0000305"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6G2J"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 248 AA; 27285 MW; DE0111BE49A1867E CRC64;
MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK
RIEAIVKNYP EGHQAAAVLP VLDLAQRQNG WLPISAMNKV AEVLQVPPMR VYEVATFYTM
YNRKPVGKYH IQVCTTTPCM LRDSDSILET LQRKLGIKVG ETTPDKLFTL IEVECLGACV
NAPMVQINDN YYEDLTPKDI EEIIDELKAG KVPKPGPRSG RFCCEPAGGL TSLTEPPKGP
GFGVQAGL
