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Q9ER97 (NGB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Neuroglobin
Gene names
Name:Ngb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis. Ref.3 Ref.4

Subunit structure

Monomer. Homodimer and homotetramer; disulfide-linked Probable. Interacts with 14-3-3 By similarity. Ref.4

Subcellular location

Perikaryon By similarity. Cytoplasm. Mitochondrion Ref.5.

Tissue specificity

Predominantly expressed in brain.

Post-translational modification

A redox disulfide bond regulates the heme pocket coordination and the rate of nitrite reduction to NO By similarity.

Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during hypoxia. Phosphorylation increases nitrite reductase activity By similarity.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Neuroglobin
PRO_0000053392

Regions

Region1 – 149149Globin

Sites

Metal binding641Iron (heme distal ligand)
Metal binding961Iron (heme proximal ligand)

Experimental info

Mutagenesis641H → L: Improved binding of dioxygen and carbon monoxide to the iron atom. Ref.4

Secondary structure

....................... 151
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ER97 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 377BBE4BF723CCF1

FASTA15117,037
        10         20         30         40         50         60 
MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS SPEDCLSSPE 

        70         80         90        100        110        120 
FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG VRLSSFSTVG ESLLYMLEKC 

       130        140        150 
LGPDFTPATR TAWSRLYGAV VQAMSRGWDG E 

« Hide

References

« Hide 'large scale' references
[1]"A vertebrate globin expressed in the brain."
Burmester T., Weich B., Reinhardt S., Hankeln T.
Nature 407:520-522(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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].
Tissue: Liver.
[3]"The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket."
Couture M., Burmester T., Hankeln T., Rousseau D.L.
J. Biol. Chem. 276:36377-36382(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family."
Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T., Marden M.C., Caubergs R., Moens L.
J. Biol. Chem. 276:38949-38955(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, QUATERNARY STRUCTURE, MUTAGENESIS OF HIS-64.
[5]"Mitochondrial distribution of neuroglobin and its response to oxygen-glucose deprivation in primary-cultured mouse cortical neurons."
Yu Z., Xu J., Liu N., Wang Y., Li X., Pallast S., van Leyen K., Wang X.
Neuroscience 218:235-242(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity."
Vallone B., Nienhaus K., Matthes A., Brunori M., Nienhaus G.U.
Proc. Natl. Acad. Sci. U.S.A. 101:17351-17356(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBON MONOXIDE.
[7]"The structure of murine neuroglobin: Novel pathways for ligand migration and binding."
Vallone B., Nienhaus K., Brunori M., Nienhaus G.U.
Proteins 56:85-92(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN A HEXACOORDINATED FE(3+)-BOUND FORM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245945 mRNA. Translation: CAC11135.1.
BC024263 mRNA. Translation: AAH24263.1.
RefSeqNP_071859.1. NM_022414.2.
UniGeneMm.41395.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q1FX-ray1.50A1-151[»]
1W92X-ray1.70A1-151[»]
2VRYX-ray1.87A1-151[»]
3GK9X-ray1.80A1-151[»]
3GKTX-ray1.86A1-151[»]
3GLNX-ray2.26A1-151[»]
ProteinModelPortalQ9ER97.
SMRQ9ER97. Positions 3-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000105806.

Proteomic databases

PRIDEQ9ER97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021420; ENSMUSP00000021420; ENSMUSG00000021032.
GeneID64242.
KEGGmmu:64242.
UCSCuc007oii.1. mouse.

Organism-specific databases

CTD58157.
MGIMGI:2151886. Ngb.

Phylogenomic databases

eggNOGNOG317570.
GeneTreeENSGT00510000048375.
HOVERGENHBG039321.
OrthoDBEOG7JDR08.
PhylomeDBQ9ER97.
TreeFamTF333247.

Gene expression databases

ArrayExpressQ9ER97.
BgeeQ9ER97.
CleanExMM_NGB.
GenevestigatorQ9ER97.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ER97.
NextBio319968.
PROQ9ER97.
SOURCESearch...

Entry information

Entry nameNGB_MOUSE
AccessionPrimary (citable) accession number: Q9ER97
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot