[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1006/geno.1996.0572; PubMed=8938450 [NCBI, ExPASy, EBI, Israel, Japan] Hyslop S.J., Duncan A.M.V., Pitkanen S., Robinson B.H.; "Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13."; Genomics 37:375-380(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan] Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.; "The DNA sequence and biology of human chromosome 19."; Nature 428:529-535(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-23. TISSUE=Brain; 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).
[4]	VARIANT LS MET-122. DOI=10.1002/1531-8249(199906)45:6<787::AID-ANA13>3.0.CO;2-6; PubMed=10360771 [NCBI, ExPASy, EBI, Israel, Japan] Triepels R.H., van den Heuvel L., Loeffen J.L.C.M., Buskens C.A.F., Smeets R.J.P., Rubio Gozalbo M.E., Budde S.M., Mariman E.C.M., Wijburg F.A., Barth P.G., Trijbels J.M.F., Smeitink J.A.M.; "Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I."; Ann. Neurol. 45:787-790(1999).
[5]	VARIANT COMPLEX I DEFICIENCY MET-122. DOI=10.1086/302432; PubMed=10330338 [NCBI, ExPASy, EBI, Israel, Japan] Smeitink J., van den Heuvel L.; "Human mitochondrial complex I in health and disease."; Am. J. Hum. Genet. 64:1505-1510(1999).

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 1 4Fe-4S cluster (Potential).
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.
DISEASE: Defects in NDUFS7 are a cause of Leigh syndrome (LS) [MIM:256000]. LS is a severe neurological disorder characterized by bilaterally symmetrical necrotic lesions in subcortical brain regions.
DISEASE: Defects in NDUFS7 are a cause of complex I mitochondrial respiratory chain deficiency [MIM:252010]. Complex I (NADH-ubiquinone oxidoreductase), the largest complex of the mitochondrial respiratory chain, contains more than 40 subunits. It is embedded in the inner mitochondrial membrane and is partly protruding in the matrix. Complex I deficiency is the most common cause of mitochondrial disorders. It represents largely one-third of all cases of respiratory chain deficiency and is responsible for a variety of clinical symptoms, ranging from neurological disorders to cardiomyopathy, liver failure, and myopathy.
SIMILARITY: Belongs to the complex I 20 kDa subunit family.
SEQUENCE CAUTION:
- Sequence=AAC27669.1; Type=Erroneous gene model prediction;
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=NDUFS7";.

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

AC005329; AAC27669.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001715; AAH01715.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005954; AAH05954.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111517; AAI11518.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_077718.3; -.

UniGene

Hs.211914

3D structure databases

ModBase

O75251.

PTM databases

PhosphoSite

O75251; -.

Enzyme and pathway databases

Reactome

REACT_6305; Electron Transport Chain.

Organism-specific databases

H-InvDB

HIX0014582; -.
HIX0092829; -.

HGNC:7714; NDUFS7.

252010; phenotype. [NCBI / EBI]
256000; phenotype. [NCBI / EBI]
601825; gene. [NCBI / EBI]

Orphanet

506; Leigh syndrome.
2597; Mitochondrial myopathy - lactic acidosis.
2609; NADH-CoQ reductase deficiency.

PharmGKB

PA31524; -.

GeneCards

O75251.

Gene expression databases

ArrayExpress

O75251; -.

CleanEx

HS_NDUFS7; -.

GermOnline

ENSG00000115286; Homo sapiens.

Ontologies

GO:0005747;	Cellular component: mitochondrial respiratory chain complex I (inferred from mutant phenotype from UniProtKB).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (non-traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (non-traceable author statement from UniProtKB).
GO:0032981;	Biological process: mitochondrial respiratory chain complex I assembly (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006138; NADH_DHase_20kDa_su.
IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
IPR006137; OxRdtase_q6.
Graphical view of domain structure.

PANTHER

PTHR11995:SF2; NADH_DH_20kDa; 1.
PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.

Pfam

PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01957; nuoB_fam; 1.

PROSITE

PS01150; COMPLEX1_20K; 1.

BLOCKS

O75251.

Genome annotation databases

Ensembl

ENSG00000115286; Homo sapiens. [Contig view]

GeneID

374291; -.

KEGG

hsa:374291; -.

Phylogenomic databases

HOVERGEN

O75251; -.

Other

DrugBank

DB00157; NADH.

SOURCE

NDUFS7; Homo sapiens.

ProtoNet

O75251.

UniRef

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

Keywords

4Fe-4S; Disease mutation; Electron transport; Iron; Iron-sulfur; Leigh syndrome; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Polymorphism; Respiratory chain; Transit peptide; Transport; Ubiquinone.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 38`	`38`	`Mitochondrion (By similarity).`
`CHAIN`	`39 213`	`175`	`NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial.`	`PRO_0000020027`
`METAL`	`88 88`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`89 89`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`153 153`		`Iron-sulfur (4Fe-4S) (Potential).`
`METAL`	`183 183`		`Iron-sulfur (4Fe-4S) (Potential).`
`VARIANT`	`23 23`	`1`	`P -> L (in dbSNP:rs1142530 [NCBI]).`	`VAR_014482`
`VARIANT`	`122 122`	`1`	`V -> M (in complex I deficiency and LS).`	`VAR_008848`

Sequence information

Length: 213 AA [This is the length of the unprocessed precursor]

Molecular weight: 23564 Da [This is the MW of the unprocessed precursor]

CRC64: B3547EA24643C1B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVLSAPGLR GFRILGLRSS VGPAVQARGV HQSVATDGPS STQPALPKAR AVAPKPSSRG 

        70         80         90        100        110        120 
EYVVAKLDDL VNWARRSSLW PMTFGLACCA VEMMHMAAPR YDMDRFGVVF RASPRQSDVM 

       130        140        150        160        170        180 
IVAGTLTNKM APALRKVYDQ MPEPRYVVSM GSCANGGGYY HYSYSVVRGC DRIVPVDIYI 

       190        200        210 
PGCPPTAEAL LYGILQLQRK IKRERRLQIW YRR

O75251 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