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Reviewed, UniProtKB/Swiss-Prot Q9DC70 (NDUS7_MOUSE)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 20 kDa subunit
    Complex I-20kD
      Short name=CI-20kD
Gene names
Name: Ndufs7
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length224 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.

Catalytic activity

NADH + ubiquinone = NAD+ + ubiquinol.

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster Potential.

Subunit structure

Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 224189NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
PRO_0000020028

Sites

Metal binding991Iron-sulfur (4Fe-4S) Potential
Metal binding1001Iron-sulfur (4Fe-4S) Potential
Metal binding1641Iron-sulfur (4Fe-4S) Potential
Metal binding1941Iron-sulfur (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9DC70-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 234F3FF0ABC36A92

FASTA22424,683
        10         20         30         40         50         60 
MAALAAPGLL SVRILGLRTA QVQLRRVHQS VATEGPSPSP SPSLSSTQSA VSKAGAGAVV 

        70         80         90        100        110        120 
PKLSHLPRSR AEYVVTKLDD LINWARRSSL WPMTFGLACC AVEMMHMAAP RYDMDRFGVV 

       130        140        150        160        170        180 
FRASPRQADV MIVAGTLTNK MAPALRKVYD QMPEPRYVVS MGSCANGGGY YHYSYSVVRG 

       190        200        210        220 
CDRIVPVDIY VPGCPPTAEA LLYGILQLQR KIKREQKLKI WYRR 

« 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 78-86; 127-140 AND 157-179, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK003132 mRNA. Translation: BAB22592.1.
BC013503 mRNA. Translation: AAH13503.1.
IPIIPI00120232.
RefSeqNP_083548.1.
UniGeneMm.28712

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9DC70.

Genome annotation databases

EnsemblENSMUSG00000020153. Mus musculus. [Contig view]
GeneID75406.
KEGGmmu:75406.
NMPDRfig|10090.3.peg.14026.

Organism-specific databases

MGIMGI:1922656. Ndufs7.

Phylogenomic databases

HOVERGENQ9DC70.
OMAQ9DC70. AKIRTER.

Enzyme and pathway databases

BRENDA1.6.5.3. 244.
1.6.99.3. 244.

Gene expression databases

ArrayExpressQ9DC70.
BgeeQ9DC70.
CleanExMM_NDUFS7.
GermOnlineENSMUSG00000020153. Mus musculus.

Family and domain databases

InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UbQ_OxRdtase_su-20kDa.
IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB.
[Graphical view]
PANTHERPTHR11995:SF2. NADH_DH_20kDa. 1 hit.
PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 1 hit.
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. nuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio342928.
SOURCESearch...

Entry information

Entry nameNDUS7_MOUSE
AccessionPrimary (citable) accession number: Q9DC70
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents