[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	PROTEIN SEQUENCE OF 185-200; 247-266; 429-441; 484-499; 519-528; 544-557 AND 625-643, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.

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 = NAD⁺ + ubiquinol.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
SUBUNIT: 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).
SIMILARITY: Belongs to the complex I 75 kDa subunit family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.

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

BC081892; AAH81892.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001005550.1; -.

UniGene

Rn.1467

3D structure databases

ModBase

Q66HF1.

PTM databases

PhosphoSite

Q66HF1; -.

Organism-specific databases

RGD

1359670; Ndufs1.

Gene expression databases

ArrayExpress

Q66HF1; -.

Ontologies

GO:0005758;	Cellular component: mitochondrial intermembrane space (inferred from sequence or structural similarity from UniProtKB).
GO:0005747;	Cellular component: mitochondrial respiratory chain complex I (inferred from sequence or structural similarity from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006915;	Biological process: apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0046034;	Biological process: ATP metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0045333;	Biological process: cellular respiration (inferred from sequence or structural similarity from UniProtKB).
GO:0006800;	Biological process: oxygen and reactive oxygen species metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0051881;	Biological process: regulation of mitochondrial membrane potential (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001041; Ferredoxin.
IPR006656; Mopterin_OxRdtase.
IPR000283; NADH_DHase_75KDa_su_CS.
IPR010228; NADH_quinone_OxRdtase_G.
IPR015405; NuoG_C.
Graphical view of domain structure.

Pfam

PF09326; DUF1982; 1.
PF00111; Fer2; 1.
PF00384; Molybdopterin; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01973; NuoG; 1.

PROSITE

PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q66HF1.

Genome annotation databases

Ensembl

ENSRNOG00000011849; Rattus norvegicus. [Contig view]

GeneID

301458; -.

KEGG

rno:301458; -.

NMPDR

fig|10116.3.peg.30141; -.

Phylogenomic databases

HOVERGEN

Q66HF1; -.

Other

ProtoNet

Q66HF1.

UniRef

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

Keywords

2Fe-2S; 4Fe-4S; Acetylation; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Respiratory chain; Transit peptide; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 23`	`23`	`Mitochondrion (By similarity).`
`CHAIN`	`24 727`	`704`	`NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial.`	`PRO_0000271388`
`DOMAIN`	`30 108`	`79`	`2Fe-2S ferredoxin-type.`
`METAL`	`64 64`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`75 75`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`78 78`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`92 92`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`124 124`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`128 128`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`131 131`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`137 137`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`176 176`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`179 179`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`182 182`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`226 226`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`MOD_RES`	`84 84`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 727 AA [This is the length of the unprocessed precursor]

Molecular weight: 79412 Da [This is the MW of the unprocessed precursor]

CRC64: EDAC634B2697984A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRIPVKRAL IGLSKSPKGY VRSTGTAASN 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 NIIDICPVGA LTSKPYAFTA 

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

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

       370        380        390        400        410        420 
VDSDTLCTEE IFPNEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGNH EFSKVLNAAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRDDGAAIL AAVSSIAQKI RVASGAAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKLLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLGEVS PNLVRYDDVE 

       670        680        690        700        710        720 
EANYFQQASE LAKLVDQEFL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC

Q66HF1 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