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Q91YT0 (NDUV1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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] flavoprotein 1, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-51kD
Short name=CI-51kD
NADH-ubiquinone oxidoreductase 51 kDa subunit
Gene names
Name:Ndufv1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length464 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 + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 FMN Potential.

Binds 1 4Fe-4S 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; Peripheral membrane protein; Matrix side By similarity.

Sequence similarities

Belongs to the complex I 51 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Ref.3
Chain21 – 464444NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
PRO_0000019978

Regions

Nucleotide binding87 – 9610NAD(H) By similarity
Nucleotide binding199 – 24749FMN By similarity

Sites

Metal binding3791Iron-sulfur (4Fe-4S) Potential
Metal binding3821Iron-sulfur (4Fe-4S) Potential
Metal binding3851Iron-sulfur (4Fe-4S) Potential
Metal binding4251Iron-sulfur (4Fe-4S) Potential

Amino acid modifications

Modified residue811N6-acetyllysine; alternate Ref.6
Modified residue811N6-succinyllysine; alternate Ref.5
Modified residue1041N6-acetyllysine Ref.6
Modified residue3751N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q91YT0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 611EAB1546D2A630

FASTA46450,834
        10         20         30         40         50         60 
MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG 

        70         80         90        100        110        120 
DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG 

       130        140        150        160        170        180 
EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG 

       190        200        210        220        230        240 
LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT 

       250        260        270        280        290        300 
TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI 

       310        320        330        340        350        360 
EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS 

       370        380        390        400        410        420 
TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE 

       430        440        450        460 
GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS 

« 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.
[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: Kidney.
[3]"Proteome analysis of mouse brain: two-dimensional electrophoresis profiles of tissue proteins during the course of aging."
Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T., Watanabe Y., Morimasa T., Hosokawa K., Toda T.
Electrophoresis 21:1853-1871(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-29.
Strain: C57BL/6.
Tissue: Brain.
[4]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267; 275-297; 303-329; 370-375; 387-394 AND 402-449, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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-81; LYS-104 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK075692 mRNA. Translation: BAC35893.1.
BC014818 mRNA. Translation: AAH14818.1.
BC041682 mRNA. Translation: AAH41682.1.
PIRPC7078.
RefSeqNP_598427.1. NM_133666.3.
UniGeneMm.29842.

3D structure databases

ProteinModelPortalQ91YT0.
SMRQ91YT0. Positions 38-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201719. 1 interaction.
IntActQ91YT0. 4 interactions.
MINTMINT-1861002.
STRING10090.ENSMUSP00000042967.

PTM databases

PhosphoSiteQ91YT0.

Proteomic databases

PaxDbQ91YT0.
PRIDEQ91YT0.

Protocols and materials databases

DNASU17995.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042497; ENSMUSP00000042967; ENSMUSG00000037916.
GeneID17995.
KEGGmmu:17995.
UCSCuc008fye.1. mouse.

Organism-specific databases

CTD4723.
MGIMGI:107851. Ndufv1.

Phylogenomic databases

eggNOGCOG1894.
GeneTreeENSGT00390000010641.
HOGENOMHOG000251534.
HOVERGENHBG006542.
InParanoidQ91YT0.
KOK03942.
OMAHFYRHES.
PhylomeDBQ91YT0.
TreeFamTF300381.

Gene expression databases

ArrayExpressQ91YT0.
BgeeQ91YT0.
CleanExMM_NDUFV1.
GenevestigatorQ91YT0.

Family and domain databases

InterProIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
TIGRFAMsTIGR01959. nuoF_fam. 1 hit.
PROSITEPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNDUFV1. mouse.
NextBio292979.
PROQ91YT0.
SOURCESearch...

Entry information

Entry nameNDUV1_MOUSE
AccessionPrimary (citable) accession number: Q91YT0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 109 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