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Protein

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial

Gene

Ndufa10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).By similarity

Cofactori

FADNote: Binds 1 FAD per subunit.

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: MGI

GO - Biological processi

  • mitochondrial electron transport, NADH to ubiquinone Source: MGI
  • response to drug Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.
R-MMU-6799198. Complex I biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
Alternative name(s):
Complex I-42kD
Short name:
CI-42kD
NADH-ubiquinone oxidoreductase 42 kDa subunit
Gene namesi
Name:Ndufa10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914523. Ndufa10.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrial respiratory chain complex I Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionBy similarityAdd
BLAST
Chaini36 – 355320NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrialPRO_0000019989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221N6-acetyllysine; alternateCombined sources
Modified residuei122 – 1221N6-succinyllysine; alternateCombined sources
Modified residuei285 – 2851N6-succinyllysineCombined sources

Post-translational modificationi

Acetylation of Lys-242 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99LC3.
MaxQBiQ99LC3.
PaxDbiQ99LC3.
PRIDEiQ99LC3.

2D gel databases

REPRODUCTION-2DPAGEQ99LC3.

PTM databases

iPTMnetiQ99LC3.
PhosphoSiteiQ99LC3.

Expressioni

Gene expression databases

BgeeiQ99LC3.
ExpressionAtlasiQ99LC3. baseline and differential.
GenevisibleiQ99LC3. MM.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction (By similarity).By similarity

Protein-protein interaction databases

BioGridi212064. 1 interaction.
IntActiQ99LC3. 5 interactions.
MINTiMINT-1860822.
STRINGi10090.ENSMUSP00000027478.

Structurei

3D structure databases

ProteinModelPortaliQ99LC3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I NDUFA10 subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3877. Eukaryota.
ENOG41101CN. LUCA.
GeneTreeiENSGT00390000016151.
HOGENOMiHOG000267026.
HOVERGENiHBG002308.
InParanoidiQ99LC3.
KOiK03954.
OMAiKPHLVIY.
OrthoDBiEOG741Z21.
PhylomeDBiQ99LC3.
TreeFamiTF314616.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031314. DNK_dom.
IPR015828. NDUFA10.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01712. dNK. 1 hit.
[Graphical view]
PIRSFiPIRSF000543. NADH_UQ_42KD. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99LC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRLLRLVP ASAPARGLAA GAQRVGRIHT SVHCKLRYGL LAAILGDKTT
60 70 80 90 100
KKLHEYSRVI TVDGNICSGK NKLAKEIAQQ LGMKHYPEAG IQYSSTTTGD
110 120 130 140 150
GRPLDIEFSG SCSLEKFYDD PKSNDGNSYR LQSWLYASRL LQYADALEHL
160 170 180 190 200
LSTGQGVVLE RSIYSDFVFL EAMYNQGYIR KQCVDHYNEI KRLTLPEYLP
210 220 230 240 250
PHAVIYIDVP VPEVQSRIQK KGDPHEMKVT SAYLQDIENA YKKTFLPKMS
260 270 280 290 300
EMCEVLVYDS WEAEDPTKVV EDIEYLKYNK GPWLKQDDWT FHYLRMLVQD
310 320 330 340 350
KTEVLNYTTI PVYLPEITIG AHQGSRIYNS FRELPGRKYA PGYNAEVGDK

WIWLK
Length:355
Mass (Da):40,603
Last modified:June 1, 2001 - v1
Checksum:i75364533B079A688
GO

Sequence cautioni

The sequence BAB23961.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911K → E in BAB23961 (PubMed:16141072).Curated
Sequence conflicti266 – 2661P → T in BAC32674 (PubMed:16141072).Curated
Sequence conflicti294 – 2941L → S in BAB23961 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003439 mRNA. Translation: AAH03439.1.
AK005339 mRNA. Translation: BAB23961.2. Different initiation.
AK145979 mRNA. Translation: BAE26801.1.
AK046292 mRNA. Translation: BAC32674.1.
CCDSiCCDS15167.1.
RefSeqiNP_077159.1. NM_024197.1.
UniGeneiMm.248778.

Genome annotation databases

EnsembliENSMUST00000027478; ENSMUSP00000027478; ENSMUSG00000026260.
GeneIDi67273.
KEGGimmu:67273.
UCSCiuc007cbh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003439 mRNA. Translation: AAH03439.1.
AK005339 mRNA. Translation: BAB23961.2. Different initiation.
AK145979 mRNA. Translation: BAE26801.1.
AK046292 mRNA. Translation: BAC32674.1.
CCDSiCCDS15167.1.
RefSeqiNP_077159.1. NM_024197.1.
UniGeneiMm.248778.

3D structure databases

ProteinModelPortaliQ99LC3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212064. 1 interaction.
IntActiQ99LC3. 5 interactions.
MINTiMINT-1860822.
STRINGi10090.ENSMUSP00000027478.

PTM databases

iPTMnetiQ99LC3.
PhosphoSiteiQ99LC3.

2D gel databases

REPRODUCTION-2DPAGEQ99LC3.

Proteomic databases

EPDiQ99LC3.
MaxQBiQ99LC3.
PaxDbiQ99LC3.
PRIDEiQ99LC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027478; ENSMUSP00000027478; ENSMUSG00000026260.
GeneIDi67273.
KEGGimmu:67273.
UCSCiuc007cbh.1. mouse.

Organism-specific databases

CTDi4705.
MGIiMGI:1914523. Ndufa10.

Phylogenomic databases

eggNOGiKOG3877. Eukaryota.
ENOG41101CN. LUCA.
GeneTreeiENSGT00390000016151.
HOGENOMiHOG000267026.
HOVERGENiHBG002308.
InParanoidiQ99LC3.
KOiK03954.
OMAiKPHLVIY.
OrthoDBiEOG741Z21.
PhylomeDBiQ99LC3.
TreeFamiTF314616.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.
R-MMU-6799198. Complex I biogenesis.

Miscellaneous databases

ChiTaRSiNdufa10. mouse.
NextBioi324076.
PROiQ99LC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LC3.
ExpressionAtlasiQ99LC3. baseline and differential.
GenevisibleiQ99LC3. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031314. DNK_dom.
IPR015828. NDUFA10.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01712. dNK. 1 hit.
[Graphical view]
PIRSFiPIRSF000543. NADH_UQ_42KD. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-330.
    Strain: C57BL/6J.
    Tissue: Brain and Placenta.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-48; 59-70; 76-84; 131-161; 193-217; 229-243; 269-277; 286-295; 302-332 AND 339-350, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNDUAA_MOUSE
AccessioniPrimary (citable) accession number: Q99LC3
Secondary accession number(s): Q3UKK0, Q8BL57, Q9CW21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.