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O75251 (NDUS7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-20kD
Short name=CI-20kD
NADH-ubiquinone oxidoreductase 20 kDa subunit
PSST subunit
Gene names
Name:NDUFS7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. HAMAP-Rule MF_01356

Catalytic activity

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). HAMAP-Rule MF_01356

NADH + acceptor = NAD+ + reduced acceptor. HAMAP-Rule MF_01356

Cofactor

Binds 1 4Fe-4S cluster Potential.

Subunit structure

Complex I is composed of 45 different subunits This is a component of the iron-sulfur (IP) fragment of the enzyme. Ref.4

Subcellular location

Mitochondrion HAMAP-Rule MF_01356.

Involvement in disease

Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the complex I 20 kDa subunit family.

Sequence caution

The sequence AAC27669.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Leigh syndrome
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial electron transport, NADH to ubiquinone

Non-traceable author statement Ref.1PubMed 9878551. Source: UniProtKB

mitochondrial respiratory chain complex I assembly

Inferred from mutant phenotype PubMed 11112787. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial respiratory chain complex I

Inferred from direct assay Ref.4. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

synaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Non-traceable author statement PubMed 9878551. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Non-traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15186778. Source: UniProtKB

quinone binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion By similarity
Chain39 – 213175NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial HAMAP-Rule MF_01356
PRO_0000020027

Sites

Metal binding881Iron-sulfur (4Fe-4S) Potential
Metal binding891Iron-sulfur (4Fe-4S) Potential
Metal binding1531Iron-sulfur (4Fe-4S) Potential
Metal binding1831Iron-sulfur (4Fe-4S) Potential

Natural variations

Natural variant231P → L. Ref.3
Corresponds to variant rs1142530 [ dbSNP | Ensembl ].
VAR_014482
Natural variant1221V → M in MT-C1D. Ref.6 Ref.7
VAR_008848

Sequences

Sequence LengthMass (Da)Tools
O75251 [UniParc].

Last modified March 21, 2006. Version 3.
Checksum: B3547EA24643C1B0

FASTA21323,564
        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 

« Hide

References

« Hide 'large scale' references
[1]"Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13."
Hyslop S.J., Duncan A.M.V., Pitkanen S., Robinson B.H.
Genomics 37:375-380(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-23.
Tissue: Brain.
[4]"The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification."
Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A.
J. Biol. Chem. 278:13619-13622(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I."
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.
Ann. Neurol. 45:787-790(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LS MET-122.
[7]"Human mitochondrial complex I in health and disease."
Smeitink J., van den Heuvel L.
Am. J. Hum. Genet. 64:1505-1510(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MT-C1D MET-122.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC005329 Genomic DNA. Translation: AAC27669.1. Sequence problems.
BC001715 mRNA. Translation: AAH01715.2.
BC005954 mRNA. Translation: AAH05954.1.
BC111517 mRNA. Translation: AAI11518.1.
CCDSCCDS12063.1.
RefSeqNP_077718.3. NM_024407.4.
UniGeneHs.211914.

3D structure databases

ProteinModelPortalO75251.
SMRO75251. Positions 67-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid131889. 19 interactions.
IntActO75251. 5 interactions.
MINTMINT-3001113.
STRING9606.ENSP00000233627.

Chemistry

ChEMBLCHEMBL2363065.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteO75251.

Proteomic databases

MaxQBO75251.
PaxDbO75251.
PRIDEO75251.

Protocols and materials databases

DNASU374291.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233627; ENSP00000233627; ENSG00000115286.
GeneID374291.
KEGGhsa:374291.
UCSCuc002lse.4. human.

Organism-specific databases

CTD374291.
GeneCardsGC19P001384.
H-InvDBHIX0027582.
HGNCHGNC:7714. NDUFS7.
MIM252010. phenotype.
256000. phenotype.
601825. gene.
neXtProtNX_O75251.
Orphanet2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBPA31524.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0377.
HOGENOMHOG000228249.
HOVERGENHBG001576.
KOK03940.
OMAQVRGVHS.
OrthoDBEOG7C8GJ9.
PhylomeDBO75251.
TreeFamTF312859.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO75251.
BgeeO75251.
CleanExHS_NDUFS7.
GenevestigatorO75251.

Family and domain databases

Gene3D3.40.50.700. 1 hit.
HAMAPMF_01356. NDH1_NuoB.
InterProIPR006137. NADH_UbQ_OxRdtase-like_20kDa.
IPR006138. NADH_UQ_OxRdtase_20Kd_su.
[Graphical view]
PfamPF01058. Oxidored_q6. 1 hit.
[Graphical view]
TIGRFAMsTIGR01957. nuoB_fam. 1 hit.
PROSITEPS01150. COMPLEX1_20K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNDUFS7.
GenomeRNAi374291.
NextBio100146.
PROO75251.
SOURCESearch...

Entry information

Entry nameNDUS7_HUMAN
AccessionPrimary (citable) accession number: O75251
Secondary accession number(s): Q2T9H7, Q9BV17
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM