Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q91VD9 (NDUS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-75kD
Short name=CI-75kD
Gene names
Name:Ndufs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length727 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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity.

Catalytic activity

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

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Binds 2 4Fe-4S clusters per subunit By similarity.

Subunit structure

Complex I is composed of 45 different subunits By similarity.

Subcellular location

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

Post-translational modification

Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   Ligand2Fe-2S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

apoptotic mitochondrial changes

Inferred from sequence or structural similarity. Source: UniProtKB

cellular respiration

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrial intermembrane space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex I

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

electron carrier activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
PRO_0000019969

Regions

Domain30 – 108792Fe-2S ferredoxin-type
Domain245 – 301574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding641Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding751Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding781Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding921Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1241Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1281Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1761Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1791Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2261Iron-sulfur 3 (4Fe-4S) By similarity

Amino acid modifications

Modified residue841N6-acetyllysine Ref.6
Modified residue4671N6-acetyllysine Ref.6
Modified residue4991N6-acetyllysine Ref.6
Modified residue7091N6-acetyllysine Ref.6

Experimental info

Sequence conflict4911V → A in AAH06660. Ref.4
Sequence conflict4911V → A in AAH15300. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q91VD9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4A4B4BD6C330BB4F

FASTA72779,777
        10         20         30         40         50         60 
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

        70         80         90        100        110        120 
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 

       190        200        210        220        230        240 
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA 

       250        260        270        280        290        300 
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 

       310        320        330        340        350        360 
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA LVALKDLLNK 

       370        380        390        400        410        420 
VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGRH SFCEVLKDAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRDDGAAIL VAVSNMVQKI RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS PNLVRYDDIE 

       670        680        690        700        710        720 
ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC 

« 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.
Tissue: Embryonic breast, Heart and Vagina.
[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]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Kidney.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 77-84; 88-108; 185-212; 247-266; 277-289; 292-299; 312-325; 361-382; 409-417; 421-441; 451-467; 471-483; 502-511; 519-539; 544-557; 608-617; 625-643; 646-655; 674-702 AND 713-727, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"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-84; LYS-467; LYS-499 AND LYS-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK034597 mRNA. Translation: BAE20494.1.
AK036926 mRNA. Translation: BAC29641.1.
AK142711 mRNA. Translation: BAE25170.1.
AL645950 Genomic DNA. Translation: CAI24120.1.
CH466548 Genomic DNA. Translation: EDL00180.1.
CH466548 Genomic DNA. Translation: EDL00181.1.
CH466548 Genomic DNA. Translation: EDL00182.1.
CH466548 Genomic DNA. Translation: EDL00184.1.
BC006660 mRNA. Translation: AAH06660.1.
BC015300 mRNA. Translation: AAH15300.1.
RefSeqNP_001153510.1. NM_001160038.1.
NP_001153511.1. NM_001160039.1.
NP_001153512.1. NM_001160040.1.
NP_663493.2. NM_145518.2.
XP_006496014.1. XM_006495951.1.
XP_006496015.1. XM_006495952.1.
UniGeneMm.290791.

3D structure databases

ProteinModelPortalQ91VD9.
SMRQ91VD9. Positions 31-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230599. 2 interactions.
IntActQ91VD9. 6 interactions.
MINTMINT-1860504.
STRING10090.ENSMUSP00000027111.

PTM databases

PhosphoSiteQ91VD9.

2D gel databases

REPRODUCTION-2DPAGEIPI00308882.
Q91VD9.

Proteomic databases

PaxDbQ91VD9.
PRIDEQ91VD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027111; ENSMUSP00000027111; ENSMUSG00000025968.
ENSMUST00000168099; ENSMUSP00000126621; ENSMUSG00000025968.
GeneID227197.
KEGGmmu:227197.
UCSCuc007bfu.2. mouse.

Organism-specific databases

CTD4719.
MGIMGI:2443241. Ndufs1.

Phylogenomic databases

eggNOGCOG1034.
GeneTreeENSGT00390000018768.
HOGENOMHOG000031442.
HOVERGENHBG003482.
InParanoidQ3UQ73.
KOK03934.
OMAMPVMKGM.
OrthoDBEOG783MTP.
TreeFamTF105756.

Gene expression databases

ArrayExpressQ91VD9.
BgeeQ91VD9.
CleanExMM_NDUFS1.
GenevestigatorQ91VD9.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378510.
PROQ91VD9.
SOURCESearch...

Entry information

Entry nameNDUS1_MOUSE
AccessionPrimary (citable) accession number: Q91VD9
Secondary accession number(s): Q3UQ73, Q8BM16
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 114 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