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Q9DCT2 (NDUS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-30kD
Short name=CI-30kD
NADH-ubiquinone oxidoreductase 30 kDa subunit
Gene names
Name:Ndufs3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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. HAMAP-Rule MF_01357

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). HAMAP-Rule MF_01357

NADH + acceptor = NAD+ + reduced acceptor. HAMAP-Rule MF_01357

Subunit structure

Complex I is composed of 45 different subunits By similarity. Interacts with NDUFAF3 By similarity.

Subcellular location

Mitochondrion inner membrane By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity. HAMAP-Rule MF_01357

Sequence similarities

Belongs to the complex I 30 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 263228NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial HAMAP-Rule MF_01357
PRO_0000019999

Experimental info

Sequence conflict201G → D in BAB22149. Ref.1
Sequence conflict231A → P in AAH27270. Ref.3
Sequence conflict491R → W in AAH27270. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9DCT2 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 482F6C4D5E991B7F

FASTA26330,149
        10         20         30         40         50         60 
MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS DVTHKQLSAF 

        70         80         90        100        110        120 
GEYVAEILPK YVQQVQVSCL DELEICIHPD GVIPTLTFLR DHTNAQFKSL ADLTAVDVPT 

       130        140        150        160        170        180 
RQNRFEIVYN LLSLRFNSRI RVKTYADELT PIDSIVSVHI AANWYEREVW DMFGVFFFNH 

       190        200        210        220        230        240 
PDLRRILTDY GFEGHPFRKD FPLTGYVELR YDDEVKRVVA EPVELAQEFR KFDLNSPWEA 

       250        260 
FPAYRQPPES LKLEAGDKKP ETK 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J and NOD.
Tissue: Kidney and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Tissue: Brain.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 109-121; 125-135; 186-198; 200-210 AND 218-245, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002501 mRNA. Translation: BAB22149.1.
AK088337 mRNA. Translation: BAC40291.1.
AL672241 Genomic DNA. Translation: CAM15313.1.
BC027270 mRNA. Translation: AAH27270.1.
BC119267 mRNA. Translation: AAI19268.1.
BC119269 mRNA. Translation: AAI19270.1.
RefSeqNP_080964.1. NM_026688.2.
UniGeneMm.30113.

3D structure databases

ProteinModelPortalQ9DCT2.
SMRQ9DCT2. Positions 47-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212816. 3 interactions.
DIPDIP-32378N.
IntActQ9DCT2. 6 interactions.
MINTMINT-4112498.

PTM databases

PhosphoSiteQ9DCT2.

2D gel databases

World-2DPAGE0004:Q9DCT2.

Proteomic databases

PaxDbQ9DCT2.
PRIDEQ9DCT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005647; ENSMUSP00000005647; ENSMUSG00000005510.
GeneID68349.
KEGGmmu:68349.
UCSCuc008ktr.1. mouse.

Organism-specific databases

CTD4722.
MGIMGI:1915599. Ndufs3.

Phylogenomic databases

eggNOGCOG0852.
GeneTreeENSGT00390000017480.
HOGENOMHOG000009797.
HOVERGENHBG000450.
InParanoidQ9DCT2.
KOK03936.
OMAQQVQVTC.
OrthoDBEOG7R56TC.
PhylomeDBQ9DCT2.
TreeFamTF314794.

Gene expression databases

BgeeQ9DCT2.
CleanExMM_NDUFS3.
GenevestigatorQ9DCT2.

Family and domain databases

HAMAPMF_01357. NDH1_NuoC.
InterProIPR010218. NADH_DH_suC.
IPR001268. NADH_UbQ_OxRdtase_30kDa_su.
IPR020396. NADH_UbQ_OxRdtase_CS.
[Graphical view]
PfamPF00329. Complex1_30kDa. 1 hit.
[Graphical view]
ProDomPD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01961. NuoC_fam. 1 hit.
PROSITEPS00542. COMPLEX1_30K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio327045.
PROQ9DCT2.
SOURCESearch...

Entry information

Entry nameNDUS3_MOUSE
AccessionPrimary (citable) accession number: Q9DCT2
Secondary accession number(s): Q8BTZ3, Q8R073
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot