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   27-MAR-2024, entry version 187.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial {ECO:0000250|UniProtKB:P19404};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P19404};
DE   AltName: Full=NADH-ubiquinone oxidoreductase 24 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufv2 {ECO:0000312|MGI:MGI:1920150};
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,
RC   Pancreas, 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).
RN   [6] {ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, CATALYTIC
RP   ACTIVITY, COFACTOR, AND SUBUNIT.
RX   PubMed=29915388; DOI=10.1038/s41594-018-0073-1;
RA   Agip A.A., Blaza J.N., Bridges H.R., Viscomi C., Rawson S., Muench S.P.,
RA   Hirst J.;
RT   "Cryo-EM structures of complex I from mouse heart mitochondria in two
RT   biochemically defined states.";
RL   Nat. Struct. Mol. Biol. 25:548-556(2018).
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. Parts of the peripheral arm of the enzyme, where the
CC       electrons from NADH are accepted by flavin mononucleotide (FMN) and
CC       then passed along a chain of iron-sulfur clusters by electron
CC       tunnelling to the final acceptor ubiquinone. Contains one iron-sulfur
CC       cluster. {ECO:0000250|UniProtKB:P19404}.
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:P19404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092;
CC         Evidence={ECO:0000250|UniProtKB:P19404};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P19404};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P19404};
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.
CC       {ECO:0000269|PubMed:29915388}.
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   PDB; 8OLT; EM; 2.84 A; E=1-248.
DR   PDB; 8OM1; EM; 2.39 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   PDBsum; 8OLT; -.
DR   PDBsum; 8OM1; -.
DR   AlphaFoldDB; Q9D6J6; -.
DR   EMDB; EMD-16962; -.
DR   EMDB; EMD-16965; -.
DR   SMR; Q9D6J6; -.
DR   BioGRID; 215635; 75.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9D6J6; -.
DR   IntAct; Q9D6J6; 6.
DR   MINT; Q9D6J6; -.
DR   STRING; 10090.ENSMUSP00000121557; -.
DR   GlyGen; Q9D6J6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D6J6; -.
DR   PhosphoSitePlus; Q9D6J6; -.
DR   SwissPalm; Q9D6J6; -.
DR   REPRODUCTION-2DPAGE; Q9D6J6; -.
DR   EPD; Q9D6J6; -.
DR   jPOST; Q9D6J6; -.
DR   MaxQB; Q9D6J6; -.
DR   PaxDb; 10090-ENSMUSP00000121557; -.
DR   PeptideAtlas; Q9D6J6; -.
DR   ProteomicsDB; 293649; -. [Q9D6J6-1]
DR   ProteomicsDB; 293650; -. [Q9D6J6-2]
DR   Pumba; Q9D6J6; -.
DR   Antibodypedia; 1273; 342 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000024909.15; ENSMUSP00000024909.10; ENSMUSG00000024099.16. [Q9D6J6-2]
DR   Ensembl; ENSMUST00000143987.9; ENSMUSP00000121557.2; ENSMUSG00000024099.16. [Q9D6J6-1]
DR   GeneID; 72900; -.
DR   KEGG; mmu:72900; -.
DR   UCSC; uc008dgw.2; mouse. [Q9D6J6-1]
DR   AGR; MGI:1920150; -.
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; IMSIYPE; -.
DR   OrthoDB; 177389at2759; -.
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 80 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 270 other cell types or tissues.
DR   ExpressionAtlas; Q9D6J6; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0048738; P:cardiac muscle tissue development; ISO:MGI.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   CDD; cd03064; TRX_Fd_NuoE; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR042128; NuoE_dom.
DR   InterPro; IPR041921; NuoE_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01958; nuoE_fam; 1.
DR   PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
DR   Genevisible; Q9D6J6; MM.
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:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         139
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         175
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         179
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
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..66
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           78..89
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           108..117
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           137..140
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           144..155
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:6G2J"
FT   STRAND          166..174
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           197..209
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   TURN            240..243
FT                   /evidence="ECO:0007829|PDB:8OM1"
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
//