ID   NDUS3_MOUSE             Reviewed;         263 AA.
AC   Q9DCT2; Q8BTZ3; Q8R073;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;
DE            EC=7.1.1.2 {ECO:0000269|PubMed:31916679, ECO:0000269|PubMed:33148885};
DE   AltName: Full=Complex I-30kD;
DE            Short=CI-30kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 30 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufs3;
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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, 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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   PROTEIN SEQUENCE OF 109-121; 125-135; 186-198; 200-210 AND 218-245, AND
RP   IDENTIFICATION 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   [5]
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   [6]
RP   INTERACTION WITH RAB5IF.
RX   PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA   Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA   Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA   Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA   Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA   Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT   "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT   Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL   IScience 19:1114-1132(2019).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=31916679; DOI=10.15252/emmm.201910674;
RA   Pereira C.V., Peralta S., Arguello T., Bacman S.R., Diaz F., Moraes C.T.;
RT   "Myopathy reversion in mice after restauration of mitochondrial complex
RT   I.";
RL   EMBO Mol. Med. 12:e10674-e10674(2020).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=33148885; DOI=10.1172/jci.insight.141183;
RA   Peralta S., Pinto M., Arguello T., Garcia S., Diaz F., Moraes C.T.;
RT   "Metformin delays neurological symptom onset in a mouse model of neuronal
RT   complex I deficiency.";
RL   JCI Insight 5:0-0(2020).
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 (PubMed:31916679, PubMed:33148885). Essential for the
CC       catalytic activity and assembly of complex I (PubMed:31916679,
CC       PubMed:33148885). {ECO:0000269|PubMed:31916679,
CC       ECO:0000269|PubMed:33148885}.
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:0000269|PubMed:31916679, ECO:0000269|PubMed:33148885};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits (By similarity).
CC       Interacts with NDUFAF3 (By similarity). Interacts with RAB5IF
CC       (PubMed:31536960). Found in subcomplexes containing subunits NDUFS2,
CC       MT-ND1 and NDUFA13 (By similarity). {ECO:0000250|UniProtKB:O75489,
CC       ECO:0000269|PubMed:31536960}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:O75489}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O75489}; Matrix side
CC       {ECO:0000250|UniProtKB:O75489}.
CC   -!- DISRUPTION PHENOTYPE: Conditional knockout (KO) in the forebrain
CC       neurons results in reduced complex I activity, altered brain energy
CC       metabolism, increased locomotor activity with impaired motor
CC       coordination, balance and stereotyped behavior, neuroinflammation in
CC       cortex and hippocampus, and neuronal death in hippocampus
CC       (PubMed:33148885). Conditional KO in skeletal muscle results in
CC       development of a progressive myopathy resulting in premature death,
CC       muscle degeneration accompanied by increased mitochondrial
CC       proliferation and serum lactic acidosis and a decrease in complex I
CC       activity, assembly and expression in muscle (PubMed:31916679).
CC       {ECO:0000269|PubMed:31916679, ECO:0000269|PubMed:33148885}.
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AK002501; BAB22149.1; -; mRNA.
DR   EMBL; AK088337; BAC40291.1; -; mRNA.
DR   EMBL; AL672241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027270; AAH27270.1; -; mRNA.
DR   EMBL; BC119267; AAI19268.1; -; mRNA.
DR   EMBL; BC119269; AAI19270.1; -; mRNA.
DR   CCDS; CCDS16418.1; -.
DR   RefSeq; NP_080964.1; NM_026688.2.
DR   PDB; 6G2J; EM; 3.30 A; C=1-263.
DR   PDB; 6G72; EM; 3.90 A; C=1-263.
DR   PDB; 6ZR2; EM; 3.10 A; C=1-263.
DR   PDB; 6ZTQ; EM; 3.00 A; C=1-263.
DR   PDB; 7AK5; EM; 3.17 A; C=1-263.
DR   PDB; 7AK6; EM; 3.82 A; C=1-263.
DR   PDB; 7B93; EM; 3.04 A; C=1-263.
DR   PDB; 7PSA; EM; 3.40 A; C=1-263.
DR   PDB; 8OLT; EM; 2.84 A; C=1-263.
DR   PDB; 8OM1; EM; 2.39 A; C=1-263.
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; Q9DCT2; -.
DR   EMDB; EMD-11377; -.
DR   EMDB; EMD-11424; -.
DR   EMDB; EMD-11810; -.
DR   EMDB; EMD-11811; -.
DR   EMDB; EMD-12095; -.
DR   EMDB; EMD-13611; -.
DR   EMDB; EMD-16962; -.
DR   EMDB; EMD-16965; -.
DR   EMDB; EMD-4345; -.
DR   EMDB; EMD-4356; -.
DR   SMR; Q9DCT2; -.
DR   BioGRID; 212816; 83.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9DCT2; -.
DR   DIP; DIP-32378N; -.
DR   IntAct; Q9DCT2; 10.
DR   MINT; Q9DCT2; -.
DR   STRING; 10090.ENSMUSP00000005647; -.
DR   GlyGen; Q9DCT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DCT2; -.
DR   PhosphoSitePlus; Q9DCT2; -.
DR   SwissPalm; Q9DCT2; -.
DR   EPD; Q9DCT2; -.
DR   jPOST; Q9DCT2; -.
DR   MaxQB; Q9DCT2; -.
DR   PaxDb; 10090-ENSMUSP00000005647; -.
DR   PeptideAtlas; Q9DCT2; -.
DR   ProteomicsDB; 253047; -.
DR   Pumba; Q9DCT2; -.
DR   TopDownProteomics; Q9DCT2; -.
DR   Antibodypedia; 1262; 352 antibodies from 35 providers.
DR   Ensembl; ENSMUST00000005647.4; ENSMUSP00000005647.4; ENSMUSG00000005510.10.
DR   GeneID; 68349; -.
DR   KEGG; mmu:68349; -.
DR   UCSC; uc008ktr.1; mouse.
DR   AGR; MGI:1915599; -.
DR   CTD; 4722; -.
DR   MGI; MGI:1915599; Ndufs3.
DR   VEuPathDB; HostDB:ENSMUSG00000005510; -.
DR   eggNOG; KOG1713; Eukaryota.
DR   GeneTree; ENSGT00390000017480; -.
DR   HOGENOM; CLU_042628_0_1_1; -.
DR   InParanoid; Q9DCT2; -.
DR   OMA; PCRKNRF; -.
DR   OrthoDB; 875497at2759; -.
DR   PhylomeDB; Q9DCT2; -.
DR   TreeFam; TF314794; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR   BioGRID-ORCS; 68349; 15 hits in 77 CRISPR screens.
DR   ChiTaRS; Ndufs3; mouse.
DR   PRO; PR:Q9DCT2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9DCT2; Protein.
DR   Bgee; ENSMUSG00000005510; Expressed in quadriceps femoris and 90 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0031966; C:mitochondrial 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:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR   NCBIfam; TIGR01961; NuoC_fam; 1.
DR   PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; Nqo5-like; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
DR   World-2DPAGE; 0004:Q9DCT2; -.
DR   Genevisible; Q9DCT2; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW   Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW   Transport; Ubiquinone.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..263
FT                   /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT                   3, mitochondrial"
FT                   /id="PRO_0000019999"
FT   CONFLICT        20
FT                   /note="G -> D (in Ref. 1; BAB22149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="A -> P (in Ref. 3; AAH27270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="R -> W (in Ref. 3; AAH27270)"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           52..67
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          125..133
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            134..137
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          138..146
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           162..173
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:7B93"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:7AK5"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            213..216
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:8OM1"
SQ   SEQUENCE   263 AA;  30149 MW;  482F6C4D5E991B7F CRC64;
     MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF
     GEYVAEILPK YVQQVQVSCL DELEICIHPD GVIPTLTFLR DHTNAQFKSL ADLTAVDVPT
     RQNRFEIVYN LLSLRFNSRI RVKTYADELT PIDSIVSVHI AANWYEREVW DMFGVFFFNH
     PDLRRILTDY GFEGHPFRKD FPLTGYVELR YDDEVKRVVA EPVELAQEFR KFDLNSPWEA
     FPAYRQPPES LKLEAGDKKP ETK
//