NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/j.gene.2006.03.015; PubMed=16828987 [NCBI, ExPASy, EBI, Israel, Japan]
Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B., Wallace D.C.;
"Adaptive selection of mitochondrial complex I subunits during primate radiation.";
Gene 378:11-18(2006).

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

DQ885672; ABH12181.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001073384.1; -.

3D structure databases

ModBase

Q0MQG2.

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

Q0MQG2.

Genome annotation databases

Ensembl

ENSPTRG00000012842; Pan troglodytes. [Contig view]

GeneID

459896; -.

KEGG

ptr:459896; -.

Phylogenomic databases

HOVERGEN

Q0MQG2; -.

Other

ProtoNet

Q0MQG2.

UniRef

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

Keywords

2Fe-2S; 4Fe-4S; Acetylation; 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_0000251855`
`DOMAIN`	`30 108`	`79`	`2Fe-2S ferredoxin-type.`
`METAL`	`64 64`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`75 75`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`78 78`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`92 92`		`Iron-sulfur 1 (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: 79523 Da [This is the MW of the unprocessed precursor]

CRC64: C22C6D8901A9B05F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRIPVRKAL VVLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

        70         80         90        100        110        120 
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSKKSK KAREGVMEFL 

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGNDR 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 QTFQGKDVAA IAGGLVDAEA LVALKDLLNR 

       370        380        390        400        410        420 
VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARLRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 

       670        680        690        700        710        720 
GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC

Q0MQG2 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