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Q91WD5 (NDUS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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 2, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-49kD
Short name=CI-49kD
NADH-ubiquinone oxidoreductase 49 kDa subunit
Gene names
Name:Ndufs2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length463 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_01358

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). HAMAP-Rule MF_01358

NADH + acceptor = NAD+ + reduced acceptor. HAMAP-Rule MF_01358

Cofactor

Binds 1 4Fe-4S cluster.

Subunit structure

Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme By similarity. Interacts with NDUFAF3 By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity HAMAP-Rule MF_01358.

Sequence similarities

Belongs to the complex I 49 kDa subunit family.

Sequence caution

The sequence AAH03898.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 463430NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial HAMAP-Rule MF_01358
PRO_0000019982

Sites

Metal binding3261Iron-sulfur (4Fe-4S) Potential
Metal binding3321Iron-sulfur (4Fe-4S) Potential
Metal binding3471Iron-sulfur (4Fe-4S) Potential

Amino acid modifications

Modified residue621N6-acetyllysine Ref.4
Modified residue1181Symmetric dimethylarginine By similarity

Experimental info

Sequence conflict11M → V in AAH03898. Ref.2
Sequence conflict21A → R in BAE30656. Ref.1
Sequence conflict21A → R in BAE31936. Ref.1
Sequence conflict811T → A in BAE27028. Ref.1
Sequence conflict1861A → S in BAE27028. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91WD5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 989934D73F5C8D27

FASTA46352,626
        10         20         30         40         50         60 
MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH 

        70         80         90        100        110        120 
WKPPPWNDVD ILKEKAVTNM TLNFGPQHPA AHGVLRLVLE LSGEMVRKCD PHIGLLHRGT 

       130        140        150        160        170        180 
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSIAVEKLLN IQPPPRAQWI RVLFGEITRI 

       190        200        210        220        230        240 
LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL 

       250        260        270        280        290        300 
LDDIYEFSKN FSLRIDEVEE MLTNNRIWRN RTVDIGVVTA EDALNYGFSG VMLRGSGIQW 

       310        320        330        340        350        360 
DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIIEQCLNK MPPGEIKVDD 

       370        380        390        400        410        420 
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY 

       430        440        450        460 
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE IDR 

« 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: BALB/c and C57BL/6J.
Tissue: Bone marrow.
[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].
Strain: FVB/N.
Tissue: Mammary tumor and Salivary gland.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 57-73; 76-108; 128-138; 158-166; 172-179; 210-216; 255-266; 272-323; 373-421; 424-437 AND 441-463, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK078474 mRNA. Translation: BAC37293.1.
AK146269 mRNA. Translation: BAE27028.1.
AK150431 mRNA. Translation: BAE29554.1.
AK151746 mRNA. Translation: BAE30656.1.
AK153364 mRNA. Translation: BAE31936.1.
AK165426 mRNA. Translation: BAE38181.1.
BC003898 mRNA. Translation: AAH03898.1. Different initiation.
BC016097 mRNA. Translation: AAH16097.1.
RefSeqNP_694704.1. NM_153064.4.
UniGeneMm.21669.

3D structure databases

ProteinModelPortalQ91WD5.
SMRQ91WD5. Positions 80-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230541. 1 interaction.
IntActQ91WD5. 6 interactions.
MINTMINT-1860118.

PTM databases

PhosphoSiteQ91WD5.

Proteomic databases

PaxDbQ91WD5.
PRIDEQ91WD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000013737; ENSMUSP00000013737; ENSMUSG00000013593.
GeneID226646.
KEGGmmu:226646.
UCSCuc007dnm.1. mouse.

Organism-specific databases

CTD4720.
MGIMGI:2385112. Ndufs2.

Phylogenomic databases

eggNOGCOG0649.
GeneTreeENSGT00390000009529.
HOGENOMHOG000228264.
HOVERGENHBG000760.
InParanoidQ91WD5.
KOK03935.
OMAEYRTWTQ.
OrthoDBEOG7WT411.
PhylomeDBQ91WD5.
TreeFamTF300370.

Gene expression databases

ArrayExpressQ91WD5.
BgeeQ91WD5.
CleanExMM_NDUFS2.
GenevestigatorQ91WD5.

Family and domain databases

HAMAPMF_01358. NDH1_NuoD.
InterProIPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
[Graphical view]
PfamPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
TIGRFAMsTIGR01962. NuoD. 1 hit.
PROSITEPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378279.
PROQ91WD5.
SOURCESearch...

Entry information

Entry nameNDUS2_MOUSE
AccessionPrimary (citable) accession number: Q91WD5
Secondary accession number(s): Q3TNA8 expand/collapse secondary AC list , Q3U5Y9, Q3UJX7, Q99L23
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 102 of the entry and version 1 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