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Q9DCT2

- NDUS3_MOUSE

UniProt

Q9DCT2 - NDUS3_MOUSE

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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

Gene

Ndufs3

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

Functioni

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.By similarity

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
NADH + acceptor = NAD+ + reduced acceptor.

GO - Molecular functioni

  1. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  2. NADH dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of cell growth Source: UniProtKB
  2. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  3. reactive oxygen species metabolic process Source: UniProtKB
  4. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

NAD, Ubiquinone

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ndufs3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1915599. Ndufs3.

Subcellular locationi

Mitochondrion inner membrane By similarity
Note: Matrix and cytoplasmic side of the mitochondrial inner membrane.By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial membrane Source: UniProtKB
  3. mitochondrial respiratory chain complex I Source: UniProtKB
  4. mitochondrion Source: MGI
  5. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionBy similarityAdd
BLAST
Chaini36 – 263228NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrialPRO_0000019999Add
BLAST

Proteomic databases

MaxQBiQ9DCT2.
PaxDbiQ9DCT2.
PRIDEiQ9DCT2.

2D gel databases

World-2DPAGE0004:Q9DCT2.

PTM databases

PhosphoSiteiQ9DCT2.

Expressioni

Gene expression databases

BgeeiQ9DCT2.
CleanExiMM_NDUFS3.
GenevestigatoriQ9DCT2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi212816. 3 interactions.
DIPiDIP-32378N.
IntActiQ9DCT2. 6 interactions.
MINTiMINT-4112498.

Structurei

3D structure databases

ProteinModelPortaliQ9DCT2.
SMRiQ9DCT2. Positions 47-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I 30 kDa subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0852.
GeneTreeiENSGT00390000017480.
HOGENOMiHOG000009797.
HOVERGENiHBG000450.
InParanoidiQ9DCT2.
KOiK03936.
OMAiAECLPKY.
OrthoDBiEOG7R56TC.
PhylomeDBiQ9DCT2.
TreeFamiTF314794.

Family and domain databases

HAMAPiMF_01357. NDH1_NuoC.
InterProiIPR010218. NADH_DH_suC.
IPR001268. NADH_UbQ_OxRdtase_30kDa_su.
IPR020396. NADH_UbQ_OxRdtase_CS.
[Graphical view]
PfamiPF00329. Complex1_30kDa. 1 hit.
[Graphical view]
ProDomiPD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR01961. NuoC_fam. 1 hit.
PROSITEiPS00542. COMPLEX1_30K. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DCT2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAAARVWC RGLLGAASVG RGAGRPSVLW QHVRRESAAA DKRPTVRPRS
60 70 80 90 100
DVTHKQLSAF GEYVAEILPK YVQQVQVSCL DELEICIHPD GVIPTLTFLR
110 120 130 140 150
DHTNAQFKSL ADLTAVDVPT RQNRFEIVYN LLSLRFNSRI RVKTYADELT
160 170 180 190 200
PIDSIVSVHI AANWYEREVW DMFGVFFFNH PDLRRILTDY GFEGHPFRKD
210 220 230 240 250
FPLTGYVELR YDDEVKRVVA EPVELAQEFR KFDLNSPWEA FPAYRQPPES
260
LKLEAGDKKP ETK
Length:263
Mass (Da):30,149
Last modified:May 1, 2007 - v2
Checksum:i482F6C4D5E991B7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201G → D in BAB22149. (PubMed:16141072)Curated
Sequence conflicti23 – 231A → P in AAH27270. (PubMed:15489334)Curated
Sequence conflicti49 – 491R → W in AAH27270. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS16418.1.
RefSeqiNP_080964.1. NM_026688.2.
UniGeneiMm.30113.

Genome annotation databases

EnsembliENSMUST00000005647; ENSMUSP00000005647; ENSMUSG00000005510.
GeneIDi68349.
KEGGimmu:68349.
UCSCiuc008ktr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS16418.1.
RefSeqi NP_080964.1. NM_026688.2.
UniGenei Mm.30113.

3D structure databases

ProteinModelPortali Q9DCT2.
SMRi Q9DCT2. Positions 47-203.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212816. 3 interactions.
DIPi DIP-32378N.
IntActi Q9DCT2. 6 interactions.
MINTi MINT-4112498.

PTM databases

PhosphoSitei Q9DCT2.

2D gel databases

World-2DPAGE 0004:Q9DCT2.

Proteomic databases

MaxQBi Q9DCT2.
PaxDbi Q9DCT2.
PRIDEi Q9DCT2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005647 ; ENSMUSP00000005647 ; ENSMUSG00000005510 .
GeneIDi 68349.
KEGGi mmu:68349.
UCSCi uc008ktr.1. mouse.

Organism-specific databases

CTDi 4722.
MGIi MGI:1915599. Ndufs3.

Phylogenomic databases

eggNOGi COG0852.
GeneTreei ENSGT00390000017480.
HOGENOMi HOG000009797.
HOVERGENi HBG000450.
InParanoidi Q9DCT2.
KOi K03936.
OMAi AECLPKY.
OrthoDBi EOG7R56TC.
PhylomeDBi Q9DCT2.
TreeFami TF314794.

Miscellaneous databases

NextBioi 327045.
PROi Q9DCT2.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCT2.
CleanExi MM_NDUFS3.
Genevestigatori Q9DCT2.

Family and domain databases

HAMAPi MF_01357. NDH1_NuoC.
InterProi IPR010218. NADH_DH_suC.
IPR001268. NADH_UbQ_OxRdtase_30kDa_su.
IPR020396. NADH_UbQ_OxRdtase_CS.
[Graphical view ]
Pfami PF00329. Complex1_30kDa. 1 hit.
[Graphical view ]
ProDomi PD001581. NADH_UbQ_OxRdtase_30kDa_su. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
TIGRFAMsi TIGR01961. NuoC_fam. 1 hit.
PROSITEi PS00542. COMPLEX1_30K. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiNDUS3_MOUSE
AccessioniPrimary (citable) accession number: Q9DCT2
Secondary accession number(s): Q8BTZ3, Q8R073
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 121 of the entry and version 2 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

External Data

Dasty 3