[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Lucas-Teixeira V.A., Marques S., Belo J.A.; "Genomic organization of the mouse NDUFS8 gene encoding the NADH dehydrogenase:ubiquinone Fe-S protein 8."; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 19-37; 60-90 AND 118-135, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Brain; Lubec G., Kang S.U.; 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).
CATALYTIC ACTIVITY: NADH + ubiquinone = NAD⁺ + ubiquinol.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
SUBUNIT: Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
SIMILARITY: Belongs to the complex I 23 kDa subunit family.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

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

AY096002; AAM34451.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PC7079; PC7079.

NP_659119.2; -.

3D structure databases

HSSP

P00198; 2FDN. [HSSP ENTRY / PDB]

ModBase

Q8K3J1.

PTM databases

PhosphoSite

Q8K3J1; -.

2D gel databases

REPRODUCTION-2DPAGE

Q8K3J1; -.

Organism-specific databases

MGI

MGI:2385079; Ndufs8.

Gene expression databases

ArrayExpress

Q8K3J1; -.

CleanEx

MM_NDUFS8; -.

GermOnline

ENSMUSG00000059734; Mus musculus.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR010226; NADH_quinone_OxRdtase_I.
Graphical view of domain structure.

Pfam

PF00037; Fer4; 2.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.

TIGRFAMs

TIGR01971; NuoI; 1.

PROSITE

PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8K3J1.

Genome annotation databases

Ensembl

ENSMUSG00000059734; Mus musculus. [Contig view]

GeneID

225887; -.

KEGG

mmu:225887; -.

NMPDR

fig|10090.3.peg.4372; -.

Phylogenomic databases

HOVERGEN

Q8K3J1; -.

Other

NextBio

377849; -.

SOURCE

Ndufs8; Mus musculus.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 34`	`34`	`Mitochondrion (By similarity).`
`CHAIN`	`35 212`	`178`	`NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial.`	`PRO_0000020014`
`DOMAIN`	`104 133`	`30`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`143 172`	`30`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`113 113`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`116 116`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`119 119`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`123 123`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`152 152`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`155 155`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`158 158`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`162 162`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`

Sequence information

Length: 212 AA [This is the length of the unprocessed precursor]

Molecular weight: 24038 Da [This is the MW of the unprocessed precursor]

CRC64: 1E06E024EA7829CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI 

        70         80         90        100        110        120 
LMWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE 

       130        140        150        160        170        180 
AICPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH 

       190        200        210 
EELLYNKEKL LNNGDKWEAE IAANIQADYL YR

Q8K3J1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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