[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-59. TISSUE=Heart; DOI=10.1021/bi00225a032; PubMed=1901022 [NCBI, ExPASy, EBI, Israel, Japan] Dupuis A., Skehel J.M., Walker J.E.; "A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes."; Biochemistry 30:2954-2960(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.

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.
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.
SUBCELLULAR LOCATION: Mitochondrion.
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

M58717; AAA30664.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109906; AAI09907.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A38409; A38409.

NP_777243.2; -.

3D structure databases

HSSP

P00198; 2FDN. [HSSP ENTRY / PDB]

ModBase

P42028.

Ontologies

GO:0006979;	Biological process: response to oxidative stress (inferred from direct assay from UniProtKB).
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).

BLOCKS

P42028.

Genome annotation databases

Ensembl

ENSBTAG00000012072; Bos taurus. [Contig view]

GeneID

287027; -.

KEGG

bta:287027; -.

Phylogenomic databases

HOVERGEN

P42028; -.

Other

ProtoNet

P42028.

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 36`	`36`	`Mitochondrion.`
`CHAIN`	`37 212`	`176`	`NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial.`	`PRO_0000020011`
`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).`
`CONFLICT`	`129 129`		`T -> I (in Ref. 2; AAI09907).`

Sequence information

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

Molecular weight: 23896 Da [This is the MW of the unprocessed precursor]

CRC64: 4D5F95E4C918FEF8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRCLTMPMLL RALAQAQAAR AGHASVRGLH SSAVAATYKY VNLREPSMDM KSVTDRAAQT 

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

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

       190        200        210 
EELLYNKEKL LNNGDKWEAE IAANIQADYL YR

P42028 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