NDUAA_DROME
ID NDUAA_DROME Reviewed; 407 AA.
AC P91929; Q9VD54;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;
DE AltName: Full=Complex I-42kD;
DE Short=CI-42kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 42 kDa subunit;
DE Flags: Precursor;
GN Name=ND-42 {ECO:0000312|FlyBase:FBgn0019957};
GN Synonyms=NdufA10 {ECO:0000303|PubMed:28683319,
GN ECO:0000312|FlyBase:FBgn0019957};
GN ORFNames=CG6343 {ECO:0000312|FlyBase:FBgn0019957};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-205.
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP SICILY AND HSP83, INTERACTION WITH SICILY, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 1-MET--GLY-47.
RX PubMed=23509070; DOI=10.1083/jcb.201208033;
RA Zhang K., Li Z., Jaiswal M., Bayat V., Xiong B., Sandoval H., Charng W.L.,
RA David G., Haueter C., Yamamoto S., Graham B.H., Bellen H.J.;
RT "The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial
RT complex I subunit.";
RL J. Cell Biol. 200:807-820(2013).
RN [6]
RP MUTAGENESIS OF SER-281.
RX PubMed=25412178; DOI=10.1371/journal.pgen.1004815;
RA Pogson J.H., Ivatt R.M., Sanchez-Martinez A., Tufi R., Wilson E.,
RA Mortiboys H., Whitworth A.J.;
RT "The complex I subunit NDUFA10 selectively rescues Drosophila pink1 mutants
RT through a mechanism independent of mitophagy.";
RL PLoS Genet. 10:e1004815-e1004815(2014).
RN [7]
RP MUTAGENESIS OF SER-281.
RX PubMed=24652937; DOI=10.1126/science.1249161;
RA Morais V.A., Haddad D., Craessaerts K., De Bock P.J., Swerts J., Vilain S.,
RA Aerts L., Overbergh L., Gruenewald A., Seibler P., Klein C., Gevaert K.,
RA Verstreken P., De Strooper B.;
RT "PINK1 loss-of-function mutations affect mitochondrial complex I activity
RT via NdufA10 ubiquinone uncoupling.";
RL Science 344:203-207(2014).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=25594180; DOI=10.1016/j.cell.2014.12.019;
RA Liu L., Zhang K., Sandoval H., Yamamoto S., Jaiswal M., Sanz E., Li Z.,
RA Hui J., Graham B.H., Quintana A., Bellen H.J.;
RT "Glial lipid droplets and ROS induced by mitochondrial defects promote
RT neurodegeneration.";
RL Cell 160:177-190(2015).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=28683319; DOI=10.1016/j.celrep.2017.06.015;
RA Garcia C.J., Khajeh J., Coulanges E., Chen E.I., Owusu-Ansah E.;
RT "Regulation of Mitochondrial Complex I Biogenesis in Drosophila Flight
RT Muscles.";
RL Cell Rep. 20:264-278(2017).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:28683319}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This a
CC component of the hydrophobic protein fraction (PubMed:28683319). Forms
CC a complex including sicily, ND-42 and Hsp83; the complex is necessary
CC to chaperone ND-42 in the cytoplasm before mitochondrial import; the
CC interaction between sicily and ND-42 is direct and occurs preferably
CC between the unprocessed forms in the cytoplasm (PubMed:23509070).
CC {ECO:0000269|PubMed:23509070, ECO:0000269|PubMed:28683319}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:23509070, ECO:0000269|PubMed:28683319}. Cytoplasm
CC {ECO:0000269|PubMed:23509070}.
CC -!- TISSUE SPECIFICITY: Expressed in muscles (at protein level).
CC {ECO:0000269|PubMed:28683319}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to loss of ND-30
CC and reduced mitochondrial membrane respiratory chain NADH dehydrogenase
CC (Complex I) activity (PubMed:23509070). Larvae exhibit elevated
CC reactive oxygen species (ROS) and an up-regulation of Hsp60
CC (PubMed:23509070). RNAi-mediated knockdown in the eye results in
CC retinal degeneration exacerbated with aging and accompanied by high
CC levels of ROS and accumulation of lipid droplets in the glia
CC (PubMed:23509070, PubMed:25594180). RNAi-mediated knockdown in neurons
CC results in lipid droplet accumulation and increased levels of
CC peroxidated lipids (PubMed:25594180). {ECO:0000269|PubMed:23509070,
CC ECO:0000269|PubMed:25594180}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA10 subunit family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF55947.1; -; Genomic_DNA.
DR EMBL; AY051764; AAK93188.1; -; mRNA.
DR EMBL; Y10911; CAA71852.1; -; mRNA.
DR RefSeq; NP_001262821.1; NM_001275892.1.
DR RefSeq; NP_524445.1; NM_079721.4.
DR RefSeq; NP_732692.1; NM_169990.3.
DR AlphaFoldDB; P91929; -.
DR SMR; P91929; -.
DR BioGRID; 67552; 17.
DR DIP; DIP-21667N; -.
DR IntAct; P91929; 3.
DR STRING; 7227.FBpp0083570; -.
DR PaxDb; P91929; -.
DR PRIDE; P91929; -.
DR DNASU; 42591; -.
DR EnsemblMetazoa; FBtr0084172; FBpp0083570; FBgn0019957.
DR EnsemblMetazoa; FBtr0084173; FBpp0083571; FBgn0019957.
DR EnsemblMetazoa; FBtr0335194; FBpp0307181; FBgn0019957.
DR GeneID; 42591; -.
DR KEGG; dme:Dmel_CG6343; -.
DR CTD; 42591; -.
DR FlyBase; FBgn0019957; ND-42.
DR VEuPathDB; VectorBase:FBgn0019957; -.
DR eggNOG; KOG3877; Eukaryota.
DR GeneTree; ENSGT00390000016151; -.
DR HOGENOM; CLU_050591_1_0_1; -.
DR InParanoid; P91929; -.
DR OMA; MFRQGYI; -.
DR OrthoDB; 1147235at2759; -.
DR PhylomeDB; P91929; -.
DR Reactome; R-DME-611105; Respiratory electron transport.
DR Reactome; R-DME-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 42591; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42591; -.
DR PRO; PR:P91929; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0019957; Expressed in mouthpart and 45 other tissues.
DR ExpressionAtlas; P91929; baseline and differential.
DR Genevisible; P91929; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:FlyBase.
DR CDD; cd02030; NDUO42; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR015828; NDUFA10.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000543; NADH_UQ_42KD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Electron transport; FAD; Flavoprotein; Mitochondrion;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:23509070"
FT CHAIN 61..407
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 10, mitochondrial"
FT /id="PRO_0000019990"
FT MUTAGEN 1..47
FT /note="Missing: Localizes to cytoplasm."
FT /evidence="ECO:0000269|PubMed:23509070"
FT MUTAGEN 281
FT /note="S->A: Does not rescue the phenotype of Pink1-null
FT mutants which are unable to maintain neurotransmitter
FT release at neuromuscular junctions (NMJ) during high-
FT frequency stimulation (10 Hz). Rescues the climbing deficit
FT of Pink1-null mutants."
FT /evidence="ECO:0000269|PubMed:24652937,
FT ECO:0000269|PubMed:25412178"
FT MUTAGEN 281
FT /note="S->D: Rescues some phenotypes of Pink1-null mutants
FT by re-enabling maintained neurotransmitter release at
FT neuromuscular junctions (NMJ) during high-frequency
FT stimulation (10 Hz), by restoring mitochondria cristae
FT structural organization and by improving climbing activity;
FT does not restore muscle morphology and rescues only
FT partially flight defects in the same mutants."
FT /evidence="ECO:0000269|PubMed:24652937,
FT ECO:0000269|PubMed:25412178"
FT CONFLICT 177
FT /note="H -> R (in Ref. 4; CAA71852)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="M -> L (in Ref. 4; CAA71852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46898 MW; 4B5F4EC7DED9B8D4 CRC64;
MTAVFRVGLV RLVSRATQSP NLLQAQTNAL PAAFQQRCSI SGKTMRGGPR VPKAAPYPYK
TKKYSVFNAI FDKTSKRFDE NSKVICVEGP IAAGKSKFAK ELAEELDMEY YPAVDLDLIY
INSYGYDMRK LDPQLPPSCR SYDVRNFCLD PSHDLAAQFQ IRMYMLRYSQ YIDALQHVLS
TGQGVVLERS PYSDFVFMEA MFRQGYLSRG ARSVYNELRQ NTIGELLKPH LVIYLDLPVD
AVKKQIKARN VDYEVQSKVF SDAYLSDLEQ LYKQQYLKDI STHAELLIYD WTAGGETEVV
VEDIERIDFN QFEADIHNKK MLDWRFPLEA EWCEARIKYC HEKPDLMNYF NVPRFDVPEL
VRSADDGKVW RDVWFNAPGM KYRPGYNADM GDEGLLTKTK IGINQGI
