Q6WZ19 · NGB_BOVIN
- ProteinNeuroglobin
- GeneNGB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids151 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Monomeric globin with a bis-histidyl six-coordinate heme-iron atom through which it can bind dioxygen, carbon monoxide and nitric oxide. Could help transport oxygen and increase its availability to the metabolically active neuronal tissues, though its low quantity in tissues as well as its high affinity for dioxygen, which may limit its oxygen-releasing ability, argue against it. The ferrous/deoxygenated form exhibits a nitrite reductase activity and it could produce nitric oxide which in turn inhibits cellular respiration in response to hypoxia. In its ferrous/deoxygenated state, it may also exhibit GDI (Guanine nucleotide Dissociation Inhibitor) activity toward heterotrimeric G-alpha proteins, thereby regulating signal transduction to facilitate neuroprotective responses in the wake of hypoxia and associated oxidative stress.
Catalytic activity
- Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H+ + nitriteThis reaction proceeds in the backward direction.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial matrix | |
Molecular Function | GDP-dissociation inhibitor activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | nitrite reductase activity | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Biological Process | cellular response to hypoxia | |
Biological Process | oxygen transport | |
Biological Process | response to hypoxia |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNeuroglobin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ6WZ19
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Enriched in mitochondrial matrix upon oxygen-glucose deprivation.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053388 | 1-151 | Neuroglobin | |||
Sequence: MELPEPELIRQSWREVSRSPLEHGTVLFARLFDLEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLAGLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWGGE |
Post-translational modification
Phosphorylated during hypoxia by ERK1/ERK2. Phosphorylation regulates the heme pocket hexacoordination preventing the association of His-64 with the heme metal center. Thereby, promotes the access of dioxygen and nitrite to the heme and stimulates the nitrite reductase activity. Phosphorylation during hypoxia is stabilized by 14-3-3 proteins.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Monomer (By similarity).
Homodimer and homotetramer; disulfide-linked. Mainly monomeric but also detected as part of homodimers and homotetramers (By similarity).
Interacts with 14-3-3 proteins; regulates the phosphorylation of NGB. Could interact (ferrous form) with G-alpha(i) proteins (GTP-bound form) (By similarity).
Homodimer and homotetramer; disulfide-linked. Mainly monomeric but also detected as part of homodimers and homotetramers (By similarity).
Interacts with 14-3-3 proteins; regulates the phosphorylation of NGB. Could interact (ferrous form) with G-alpha(i) proteins (GTP-bound form) (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-149 | Globin | ||||
Sequence: MELPEPELIRQSWREVSRSPLEHGTVLFARLFDLEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLAGLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWG |
Sequence similarities
Belongs to the globin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length151
- Mass (Da)16,904
- Last updated2006-06-13 v2
- ChecksumE11B4A823039D38F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAA9SS12 | A0AAA9SS12_BOVIN | NGB | 217 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ635234 EMBL· GenBank· DDBJ | CAG25616.2 EMBL· GenBank· DDBJ | mRNA |