NDUAA_MOUSE
ID NDUAA_MOUSE Reviewed; 355 AA.
AC Q99LC3; Q3UKK0; Q8BL57; Q9CW21;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
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=Ndufa10;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-330.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Placenta;
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 [3]
RP PROTEIN SEQUENCE OF 38-48; 59-70; 76-84; 131-161; 193-217; 229-243;
RP 269-277; 286-295; 302-332 AND 339-350, AND IDENTIFICATION BY MASS
RP 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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-285, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, 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 [7]
RP FUNCTION, PHOSPHORYLATION AT SER-250, AND MUTAGENESIS OF SER-250.
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).
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:24652937}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Complex I is composed of 45 different subunits. This a
CC component of the hydrophobic protein fraction.
CC {ECO:0000250|UniProtKB:O95299}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O95299}.
CC -!- PTM: Phosphorylation at Ser-250 by PINK1 is required for the binding
CC and/or reduction of the complex I substrate ubiquinone.
CC {ECO:0000269|PubMed:24652937}.
CC -!- PTM: Acetylation of Lys-242 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the complex I NDUFA10 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23961.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC003439; AAH03439.1; -; mRNA.
DR EMBL; AK005339; BAB23961.2; ALT_INIT; mRNA.
DR EMBL; AK145979; BAE26801.1; -; mRNA.
DR EMBL; AK046292; BAC32674.1; -; mRNA.
DR CCDS; CCDS15167.1; -.
DR RefSeq; NP_077159.1; NM_024197.1.
DR PDB; 6G2J; EM; 3.30 A; O=1-355.
DR PDB; 6G72; EM; 3.90 A; O=1-355.
DR PDB; 6ZR2; EM; 3.10 A; O=1-355.
DR PDB; 6ZTQ; EM; 3.00 A; O=1-355.
DR PDB; 7AK5; EM; 3.17 A; O=1-355.
DR PDB; 7AK6; EM; 3.82 A; O=1-355.
DR PDB; 7B93; EM; 3.04 A; O=1-355.
DR PDB; 7PSA; EM; 3.40 A; O=1-355.
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; Q99LC3; -.
DR SMR; Q99LC3; -.
DR BioGRID; 212064; 75.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q99LC3; -.
DR IntAct; Q99LC3; 7.
DR STRING; 10090.ENSMUSP00000027478; -.
DR iPTMnet; Q99LC3; -.
DR PhosphoSitePlus; Q99LC3; -.
DR SwissPalm; Q99LC3; -.
DR REPRODUCTION-2DPAGE; Q99LC3; -.
DR EPD; Q99LC3; -.
DR jPOST; Q99LC3; -.
DR MaxQB; Q99LC3; -.
DR PaxDb; Q99LC3; -.
DR PeptideAtlas; Q99LC3; -.
DR PRIDE; Q99LC3; -.
DR ProteomicsDB; 253046; -.
DR Antibodypedia; 34509; 196 antibodies from 29 providers.
DR DNASU; 67273; -.
DR Ensembl; ENSMUST00000027478; ENSMUSP00000027478; ENSMUSG00000026260.
DR GeneID; 67273; -.
DR KEGG; mmu:67273; -.
DR UCSC; uc007cbh.1; mouse.
DR CTD; 4705; -.
DR MGI; MGI:1914523; Ndufa10.
DR VEuPathDB; HostDB:ENSMUSG00000026260; -.
DR eggNOG; KOG3877; Eukaryota.
DR GeneTree; ENSGT00390000016151; -.
DR HOGENOM; CLU_050591_0_0_1; -.
DR InParanoid; Q99LC3; -.
DR OMA; MFRQGYI; -.
DR OrthoDB; 1147235at2759; -.
DR PhylomeDB; Q99LC3; -.
DR TreeFam; TF314616; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 67273; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Ndufa10; mouse.
DR PRO; PR:Q99LC3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99LC3; protein.
DR Bgee; ENSMUSG00000026260; Expressed in heart right ventricle and 258 other tissues.
DR ExpressionAtlas; Q99LC3; baseline and differential.
DR Genevisible; Q99LC3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
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 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW FAD; Flavoprotein; Mitochondrion; Phosphoprotein; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P34942"
FT CHAIN 36..355
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 10, mitochondrial"
FT /id="PRO_0000019989"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 250
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000269|PubMed:24652937"
FT MOD_RES 285
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 250
FT /note="S->A: Leads to mitochondrial depolarization."
FT /evidence="ECO:0000269|PubMed:24652937"
FT MUTAGEN 250
FT /note="S->D: Phosphomimetic mutant; able to rescue
FT mitochondrial depolarization in a Pink1 mutant background."
FT /evidence="ECO:0000269|PubMed:24652937"
FT CONFLICT 191
FT /note="K -> E (in Ref. 2; BAB23961)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="P -> T (in Ref. 2; BAC32674)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="L -> S (in Ref. 2; BAB23961)"
FT /evidence="ECO:0000305"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7B93"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 127..153
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:7AK5"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 355 AA; 40603 MW; 75364533B079A688 CRC64;
MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT KKLHEYSRVI
TVDGNICSGK NKLAKEIAQQ LGMKHYPEAG IQYSSTTTGD GRPLDIEFSG SCSLEKFYDD
PKSNDGNSYR LQSWLYASRL LQYADALEHL LSTGQGVVLE RSIYSDFVFL EAMYNQGYIR
KQCVDHYNEI KRLTLPEYLP PHAVIYIDVP VPEVQSRIQK KGDPHEMKVT SAYLQDIENA
YKKTFLPKMS EMCEVLVYDS WEAEDPTKVV EDIEYLKYNK GPWLKQDDWT FHYLRMLVQD
KTEVLNYTTI PVYLPEITIG AHQGSRIYNS FRELPGRKYA PGYNAEVGDK WIWLK
