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Q9D6J6 (NDUV2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
NADH-ubiquinone oxidoreductase 24 kDa subunit
Gene names
Name:Ndufv2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length248 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 2Fe-2S cluster Potential.

Subunit structure

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

Subcellular location

Mitochondrion inner membrane By similarity.

Sequence similarities

Belongs to the complex I 24 kDa subunit family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D6J6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9D6J6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion
Chain32 – 248217NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
PRO_0000020004

Sites

Metal binding1341Iron-sulfur (2Fe-2S) Potential
Metal binding1391Iron-sulfur (2Fe-2S) Potential
Metal binding1751Iron-sulfur (2Fe-2S) Potential
Metal binding1791Iron-sulfur (2Fe-2S) Potential

Natural variations

Alternative sequence1 – 9696Missing in isoform 2.
VSP_025017

Experimental info

Sequence conflict641A → T in BAB28888. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: DE0111BE49A1867E

FASTA24827,285
        10         20         30         40         50         60 
MFSLALRARA TGLAAQWGRH ARNLHKTAVH NGAGGALFVH RDTPENNPDT PFDFTPENYK 

        70         80         90        100        110        120 
RIEAIVKNYP EGHQAAAVLP VLDLAQRQNG WLPISAMNKV AEVLQVPPMR VYEVATFYTM 

       130        140        150        160        170        180 
YNRKPVGKYH IQVCTTTPCM LRDSDSILET LQRKLGIKVG ETTPDKLFTL IEVECLGACV 

       190        200        210        220        230        240 
NAPMVQINDN YYEDLTPKDI EEIIDELKAG KVPKPGPRSG RFCCEPAGGL TSLTEPPKGP 


GFGVQAGL

« Hide

Isoform 2 [UniParc].

Checksum: 19813D8C2F6A63A3
Show »

FASTA15216,736

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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Cerebellum, Heart, Hippocampus and Thymus.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Mammary tumor.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 42-61; 68-123; 129-153 AND 199-208, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK013511 mRNA. Translation: BAB28888.1.
AK078351 mRNA. Translation: BAC37233.1.
AK088193 mRNA. Translation: BAC40201.1.
AK146998 mRNA. Translation: BAE27595.1.
AK150404 mRNA. Translation: BAE29530.1.
AK151729 mRNA. Translation: BAE30647.1.
AK159460 mRNA. Translation: BAE35102.1.
AK166539 mRNA. Translation: BAE38841.1.
AK169143 mRNA. Translation: BAE40922.1.
BC030946 mRNA. Translation: AAH30946.1.
IPIIPI00169925.
IPI00845716.
RefSeqNP_082664.1. NM_028388.2.
UniGeneMm.2206.

3D structure databases

ProteinModelPortalQ9D6J6.
SMRQ9D6J6. Positions 62-211.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9D6J6. 4 interactions.

PTM databases

PhosphoSiteQ9D6J6.

2D gel databases

REPRODUCTION-2DPAGEQ9D6J6.

Proteomic databases

PaxDbQ9D6J6.
PRIDEQ9D6J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024909; ENSMUSP00000024909; ENSMUSG00000024099.
ENSMUST00000143987; ENSMUSP00000121557; ENSMUSG00000024099.
GeneID72900.
KEGGmmu:72900.
UCSCuc008dgw.1. mouse.
uc008dgx.1. mouse.

Organism-specific databases

CTD4729.
MGIMGI:1920150. Ndufv2.

Phylogenomic databases

eggNOGCOG1905.
GeneTreeENSGT00390000017580.
HOVERGENHBG029601.
InParanoidQ9D6J6.
KOK03943.
OMASMAYIRV.
OrthoDBEOG4QFWDW.

Gene expression databases

ArrayExpressQ9D6J6.
BgeeQ9D6J6.
CleanExMM_NDUFV2.
GenevestigatorQ9D6J6.
GermOnlineENSMUSG00000024099. Mus musculus.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002023. 2Fe-2S_Ferredox.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR10371. PTHR10371. 1 hit.
PfamPF01257. Complex1_24kDa. 1 hit.
[Graphical view]
PIRSFPIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMsTIGR01958. nuoE_fam. 1 hit.
PROSITEPS01099. COMPLEX1_24K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNDUFV2. mouse.
NextBio337117.
SOURCESearch...

Entry information

Entry nameNDUV2_MOUSE
AccessionPrimary (citable) accession number: Q9D6J6
Secondary accession number(s): Q3U9L9, Q8BU07, Q8K2L0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: May 1, 2007
Last modified: May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents