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Q9ER97

- NGB_MOUSE

UniProt

Q9ER97 - NGB_MOUSE

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Protein

Neuroglobin

Gene

Ngb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron (heme distal ligand)
Metal bindingi96 – 961Iron (heme proximal ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. oxygen binding Source: InterPro
  4. oxygen transporter activity Source: MGI

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. oxygen transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroglobin
Gene namesi
Name:Ngb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:2151886. Ngb.

Subcellular locationi

Perikaryon By similarity. Cytoplasm 1 Publication. Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641H → L: Improved binding of dioxygen and carbon monoxide to the iron atom. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151NeuroglobinPRO_0000053392Add
BLAST

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiQ9ER97.

Expressioni

Tissue specificityi

Predominantly expressed in brain.

Gene expression databases

BgeeiQ9ER97.
CleanExiMM_NGB.
ExpressionAtlasiQ9ER97. baseline.
GenevestigatoriQ9ER97.

Interactioni

Subunit structurei

Monomer. Homodimer and homotetramer; disulfide-linked (Probable). Interacts with 14-3-3 (By similarity).By similarityCurated

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105806.

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712
Helixi20 – 3415
Helixi36 – 416
Helixi44 – 463
Helixi52 – 554
Helixi59 – 7719
Turni78 – 803
Beta strandi82 – 854
Helixi86 – 9914
Helixi105 – 12117
Helixi122 – 1243
Helixi127 – 14519
Helixi146 – 1483

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4MU5X-ray1.80A1-151[»]
4NZIX-ray2.10A1-151[»]
4O1TX-ray1.60A1-151[»]
4O2GX-ray2.70A1-151[»]
4O35X-ray1.80A1-151[»]
ProteinModelPortaliQ9ER97.
SMRiQ9ER97. Positions 3-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ER97.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 149149GlobinAdd
BLAST

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG317570.
GeneTreeiENSGT00510000048375.
HOVERGENiHBG039321.
InParanoidiQ9ER97.
OrthoDBiEOG7JDR08.
PhylomeDBiQ9ER97.
TreeFamiTF333247.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ER97-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS
60 70 80 90 100
SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG
110 120 130 140 150
VRLSSFSTVG ESLLYMLEKC LGPDFTPATR TAWSRLYGAV VQAMSRGWDG

E
Length:151
Mass (Da):17,037
Last modified:March 1, 2001 - v1
Checksum:i377BBE4BF723CCF1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ245945 mRNA. Translation: CAC11135.1.
BC024263 mRNA. Translation: AAH24263.1.
CCDSiCCDS36501.1.
RefSeqiNP_071859.1. NM_022414.2.
UniGeneiMm.41395.

Genome annotation databases

EnsembliENSMUST00000021420; ENSMUSP00000021420; ENSMUSG00000021032.
GeneIDi64242.
KEGGimmu:64242.
UCSCiuc007oii.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ245945 mRNA. Translation: CAC11135.1 .
BC024263 mRNA. Translation: AAH24263.1 .
CCDSi CCDS36501.1.
RefSeqi NP_071859.1. NM_022414.2.
UniGenei Mm.41395.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q1F X-ray 1.50 A 1-151 [» ]
1W92 X-ray 1.70 A 1-151 [» ]
2VRY X-ray 1.87 A 1-151 [» ]
3GK9 X-ray 1.80 A 1-151 [» ]
3GKT X-ray 1.86 A 1-151 [» ]
3GLN X-ray 2.26 A 1-151 [» ]
4MU5 X-ray 1.80 A 1-151 [» ]
4NZI X-ray 2.10 A 1-151 [» ]
4O1T X-ray 1.60 A 1-151 [» ]
4O2G X-ray 2.70 A 1-151 [» ]
4O35 X-ray 1.80 A 1-151 [» ]
ProteinModelPortali Q9ER97.
SMRi Q9ER97. Positions 3-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000105806.

Proteomic databases

PRIDEi Q9ER97.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021420 ; ENSMUSP00000021420 ; ENSMUSG00000021032 .
GeneIDi 64242.
KEGGi mmu:64242.
UCSCi uc007oii.1. mouse.

Organism-specific databases

CTDi 58157.
MGIi MGI:2151886. Ngb.

Phylogenomic databases

eggNOGi NOG317570.
GeneTreei ENSGT00510000048375.
HOVERGENi HBG039321.
InParanoidi Q9ER97.
OrthoDBi EOG7JDR08.
PhylomeDBi Q9ER97.
TreeFami TF333247.

Miscellaneous databases

EvolutionaryTracei Q9ER97.
NextBioi 319968.
PROi Q9ER97.
SOURCEi Search...

Gene expression databases

Bgeei Q9ER97.
CleanExi MM_NGB.
ExpressionAtlasi Q9ER97. baseline.
Genevestigatori Q9ER97.

Family and domain databases

Gene3Di 1.10.490.10. 1 hit.
InterProi IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view ]
Pfami PF00042. Globin. 1 hit.
[Graphical view ]
SUPFAMi SSF46458. SSF46458. 1 hit.
PROSITEi PS01033. GLOBIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiNGB_MOUSE
AccessioniPrimary (citable) accession number: Q9ER97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3