[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-36 AND 41-50. STRAIN=YP102; PubMed=1735444 [NCBI, ExPASy, EBI, Israel, Japan] de Vries S., van Witzenburg R., Grivell L.A., Marres C.A.M.; "Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae."; Eur. J. Biochem. 203:587-592(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[4]	SUBCELLULAR LOCATION. DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan] Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.; "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."; Biochemistry 40:9758-9769(2001).
[5]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-28, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700098-MCP200; PubMed=17761666 [NCBI, ExPASy, EBI, Israel, Japan] Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."; Mol. Cell. Proteomics 6:1896-1906(2007).

Comments

FUNCTION: Catalyzes the oxidation of NADH generated inside the Mitochondrion.
CATALYTIC ACTIVITY: NADH + ubiquinone = NAD⁺ + ubiquinol.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Note=Bound to the mitochondrial inner membrane facing the matrix site.
MISCELLANEOUS: Present with 5240 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the NADH dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X61590; CAA43787.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49218; CAA89160.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY723851; AAU09768.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26704; S26704.

RefSeq

NP_013586.1; -.

3D structure databases

ModBase

P32340.

Protein-protein interaction databases

DIP

DIP:5554N; -.

IntAct

P32340; -.

Organism-specific databases

YML120c; -.

S000004589; NDI1.

Gene expression databases

ArrayExpress

P32340; -.

GermOnline

YML120C; Saccharomyces cerevisiae.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005759;	Cellular component: mitochondrial matrix (inferred from direct assay from SGD).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0001300;	Biological process: chronological cell aging (inferred from mutant phenotype from SGD).
GO:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from direct assay from SGD).
GO:0006116;	Biological process: NADH oxidation (inferred from direct assay from SGD).
GO:0043065;	Biological process: positive regulation of apoptosis (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PR00368; FADPNR.

Proteomic databases

P32340; -.

Genome annotation databases

Ensembl

YML120C; Saccharomyces cerevisiae. [Contig view]

854919; -.

Z71257_GR; YML120C.

sce:YML120C; -.

fig|4932.3.peg.4622; -.

Phylogenomic databases

HOGENOM

P32340; -.

Other

LinkHub

P32340; -.

NextBio

977929; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Phosphoprotein; Transit peptide; Ubiquinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 26`	`26`	`Mitochondrion.`
`CHAIN`	`27 513`	`487`	`Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial.`	`PRO_0000021793`
`NP_BIND`	`55 85`	`31`	`FAD (By similarity).`
`NP_BIND`	`229 265`	`37`	`NAD (By similarity).`
`MOD_RES`	`27 27`		`Phosphoserine.`
`MOD_RES`	`28 28`		`Phosphothreonine.`
`VARIANT`	`10 10`	`1`	`K -> R.`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 57250 Da [This is the MW of the unprocessed precursor]

CRC64: E3A43D75A1ADCF3B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSKNLYSNK RLLTSTNTLV RFASTRSTGV ENSGAGPTSF KTMKVIDPQH SDKPNVLILG 

        70         80         90        100        110        120 
SGWGAISFLK HIDTKKYNVS IISPRSYFLF TPLLPSAPVG TVDEKSIIEP IVNFALKKKG 

       130        140        150        160        170        180 
NVTYYEAEAT SINPDRNTVT IKSLSAVSQL YQPENHLGLH QAEPAEIKYD YLISAVGAEP 

       190        200        210        220        230        240 
NTFGIPGVTD YGHFLKEIPN SLEIRRTFAA NLEKANLLPK GDPERRRLLS IVVVGGGPTG 

       250        260        270        280        290        300 
VEAAGELQDY VHQDLRKFLP ALAEEVQIHL VEALPIVLNM FEKKLSSYAQ SHLENTSIKV 

       310        320        330        340        350        360 
HLRTAVAKVE EKQLLAKTKH EDGKITEETI PYGTLIWATG NKARPVITDL FKKIPEQNSS 

       370        380        390        400        410        420 
KRGLAVNDFL QVKGSNNIFA IGDNAFAGLP PTAQVAHQEA EYLAKNFDKM AQIPNFQKNL 

       430        440        450        460        470        480 
SSRKDKIDLL FEENNFKPFK YNDLGALAYL GSERAIATIR SGKRTFYTGG GLMTFYLWRI 

       490        500        510 
LYLSMILSAR SRLKVFFDWI KLAFFKRDFF KGL

P32340 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools