Q91WD5 · NDUS2_MOUSE
- ProteinNADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
- GeneNdufs2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids463 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:26437605, PubMed:29887397, PubMed:31297047, PubMed:38575788).
Essential for the catalytic activity and assembly of complex I (PubMed:26437605, PubMed:29887397, PubMed:31297047).
Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174).
Plays an important role in carotid body sensing of hypoxia (PubMed:26437605, PubMed:29887397).
Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (PubMed:31297047).
Essential for the catalytic activity and assembly of complex I (PubMed:26437605, PubMed:29887397, PubMed:31297047).
Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174).
Plays an important role in carotid body sensing of hypoxia (PubMed:26437605, PubMed:29887397).
Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (PubMed:31297047).
Catalytic activity
- a ubiquinone + NADH + 5 H+(in) = a ubiquinol + NAD+ + 4 H+(out)
a ubiquinone RHEA-COMP:9565 + CHEBI:57945 + 5 H+ (in)CHEBI:15378= a ubiquinol RHEA-COMP:9566 + CHEBI:57540 + 4 H+ (out)CHEBI:15378
Cofactor
Note: Binds 1 [4Fe-4S] cluster.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleoplasm | |
Cellular Component | respiratory chain complex I | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | NAD binding | |
Molecular Function | NADH dehydrogenase (ubiquinone) activity | |
Molecular Function | NADH dehydrogenase activity | |
Molecular Function | oxygen sensor activity | |
Molecular Function | quinone binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | aerobic respiration | |
Biological Process | cellular response to oxygen levels | |
Biological Process | gliogenesis | |
Biological Process | mitochondrial electron transport, NADH to ubiquinone | |
Biological Process | mitochondrial respiratory chain complex I assembly | |
Biological Process | neural precursor cell proliferation | |
Biological Process | neurogenesis | |
Biological Process | proton motive force-driven mitochondrial ATP synthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91WD5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Knockout mice show early perinatal death and major defects in the CNS, compromising especially the postnatal development of dorsal cortex, corpus callosum, hippocampus and cerebellum (PubMed:31297047).
Neonatal neurogenesis and gliogenesis are deeply impaired (PubMed:31297047).
Neonatal neurogenesis and gliogenesis are deeply impaired (PubMed:31297047).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-33 | Mitochondrion | ||||
Sequence: MAALRALRCLRGVGAPVLRPGSGIRLPSQPSRG | ||||||
Chain | PRO_0000019982 | 34-463 | NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial | |||
Sequence: ARQWQPDIEWAEQFSGAVMYPSKETAHWKPPPWNDVDILKEKAVTNMTLNFGPQHPAAHGVLRLVLELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSIAVEKLLNIQPPPRAQWIRVLFGEITRILNHIMAVTTHALDIGAMTPFFWMFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLLDDIYEFSKNFSLRIDEVEEMLTNNRIWRNRTVDIGVVTAEDALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPIGSRGDCYDRYLCRVEEMRQSLRIIEQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEIDR | ||||||
Modified residue | 62 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 118 | Symmetric dimethylarginine | ||||
Sequence: R |
Post-translational modification
Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2 assembles into the complex I, leading to stabilize the early intermediate complex.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits (PubMed:38575788).
Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts with NDUFAF7 (By similarity).
Interacts with CERS2 (PubMed:32279995).
Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts with NDUFAF7 (By similarity).
Interacts with CERS2 (PubMed:32279995).
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length463
- Mass (Da)52,626
- Last updated2001-12-01 v1
- Checksum989934D73F5C8D27
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A6YW30 | A0A0A6YW30_MOUSE | Ndufs2 | 231 | ||
A0A0A6YXD3 | A0A0A6YXD3_MOUSE | Ndufs2 | 145 | ||
D3YXT0 | D3YXT0_MOUSE | Ndufs2 | 437 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1 | in Ref. 2; AAH03898 | ||||
Sequence: M → V | ||||||
Sequence conflict | 2 | in Ref. 1; BAE30656/BAE31936 | ||||
Sequence: A → R | ||||||
Sequence conflict | 81 | in Ref. 1; BAE27028 | ||||
Sequence: T → A | ||||||
Sequence conflict | 186 | in Ref. 1; BAE27028 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK078474 EMBL· GenBank· DDBJ | BAC37293.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146269 EMBL· GenBank· DDBJ | BAE27028.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150431 EMBL· GenBank· DDBJ | BAE29554.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151746 EMBL· GenBank· DDBJ | BAE30656.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153364 EMBL· GenBank· DDBJ | BAE31936.1 EMBL· GenBank· DDBJ | mRNA | ||
AK165426 EMBL· GenBank· DDBJ | BAE38181.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003898 EMBL· GenBank· DDBJ | AAH03898.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC016097 EMBL· GenBank· DDBJ | AAH16097.1 EMBL· GenBank· DDBJ | mRNA |